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Database: UniProt
Entry: P01008
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Original site: P01008 
ID   ANT3_HUMAN              Reviewed;         464 AA.
AC   P01008; B2R6P0; P78439; P78447; Q13815; Q5TC78; Q7KZ43; Q7KZ97; Q9UC78;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 254.
DE   RecName: Full=Antithrombin-III;
DE            Short=ATIII;
DE   AltName: Full=Serpin C1;
DE   Flags: Precursor;
GN   Name=SERPINC1; Synonyms=AT3; ORFNames=PRO0309;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6298709; DOI=10.1093/nar/10.24.8113;
RA   Bock S.C., Wion K.L., Vehar G.A., Lawn R.M.;
RT   "Cloning and expression of the cDNA for human antithrombin III.";
RL   Nucleic Acids Res. 10:8113-8125(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6572945; DOI=10.1073/pnas.80.7.1845;
RA   Chandra T., Stackhouse R., Kidd V.J., Woo S.L.C.;
RT   "Isolation and sequence characterization of a cDNA clone of human
RT   antithrombin III.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:1845-1848(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT3D MET-438.
RA   Tsuji H., Takada O., Nakagawa M., Tanaka S., Hashimoto-Gotoh T.;
RT   "Hereditary antithrombin III deficiency: identification of an arginine-406
RT   to methionine point mutation near protease reactive site.";
RL   (In) Yoshida T.O., Wilson J.M. (eds.);
RL   Molecular approaches to the study and treatment of Human diseases,
RL   pp.51-55, Elsevier, Amsterdam (1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8476848; DOI=10.1021/bi00067a008;
RA   Olds R.J., Lane D.A., Chowdhury V., de Stefano V., Leone G., Thein S.L.;
RT   "Complete nucleotide sequence of the antithrombin gene: evidence for
RT   homologous recombination causing thrombophilia.";
RL   Biochemistry 32:4216-4224(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA   Gao F., Liu M., He F.;
RT   "Functional prediction of the coding sequences of 75 new genes deduced by
RT   analysis of cDNA clones from human fetal liver.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-30 AND ALA-147.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PROTEIN SEQUENCE OF 33-464, GLYCOSYLATION AT ASN-128; ASN-167; ASN-187 AND
RP   ASN-224, AND DISULFIDE BONDS.
RA   Petersen T.E., Dudek-Wojciechowska G., Sottrup-Jensen L., Magnusson S.;
RT   "Primary structure of antithrombin-III (heparin cofactor). Partial homology
RT   between alpha-1-antitrypsin and antithrombin-III.";
RL   (In) Collen D., Wiman B., Verstraete M. (eds.);
RL   The physiological inhibitors of blood coagulation and fibrinolysis,
RL   pp.43-54, Elsevier, Amsterdam (1979).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-464.
RX   PubMed=6305982;
RA   Prochownik E.V., Markham A.F., Orkin S.H.;
RT   "Isolation of a cDNA clone for human antithrombin III.";
RL   J. Biol. Chem. 258:8389-8394(1983).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-208, AND VARIANT AT3D LEU-439.
RX   PubMed=3191114; DOI=10.1021/bi00416a052;
RA   Bock S.C., Marrinan J.A., Radziejewska E.;
RT   "Antithrombin III Utah: proline-407 to leucine mutation in a highly
RT   conserved region near the inhibitor reactive site.";
RL   Biochemistry 27:6171-6178(1988).
RN   [13]
RP   PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, AND VARIANT AT3D THR-414.
RC   TISSUE=Plasma;
RX   PubMed=7734359; DOI=10.1111/j.1365-2141.1995.tb08368.x;
RA   Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F.,
RA   Panico M., Morris H.R.;
RT   "Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency
RT   undergoes the S-to-R transition and is associated with a plasma-inactive
RT   high-molecular-weight complex of aggregated antithrombin.";
RL   Br. J. Haematol. 89:589-601(1995).
RN   [14]
RP   REACTIVE SITE.
RX   PubMed=7238875; DOI=10.1016/0014-5793(81)80255-4;
RA   Bjoerk I., Danielsson A., Fenton J.W. II, Joernvall H.;
RT   "The site in human antithrombin for functional proteolytic cleavage by
RT   human thrombin.";
RL   FEBS Lett. 126:257-260(1981).
RN   [15]
RP   HEPARIN-BINDING SITE.
RX   PubMed=6693405;
RA   Blackburn M.N., Smith R.L., Carson J., Sibley C.C.;
RT   "The heparin-binding site of antithrombin III. Identification of a critical
RT   tryptophan in the amino acid sequence.";
RL   J. Biol. Chem. 259:939-941(1984).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
RC   TISSUE=Bile;
RX   PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA   Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA   Argani P., Goggins M.G., Maitra A., Pandey A.;
RT   "A proteomic analysis of human bile.";
RL   Mol. Cell. Proteomics 3:715-728(2004).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [18]
RP   FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
RP   HETERODIMER WITH TMPRSS7.
RX   PubMed=15853774; DOI=10.1042/bj20050299;
RA   Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
RT   "Matriptase-3 is a novel phylogenetically preserved membrane-anchored
RT   serine protease with broad serpin reactivity.";
RL   Biochem. J. 390:231-242(2005).
RN   [19]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-187 AND ASN-224.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [21]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [22]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND STRUCTURE OF
RP   CARBOHYDRATES.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA   Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [25]
RP   PHOSPHORYLATION AT THR-63 AND SER-68.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8087553; DOI=10.1016/s0969-2126(00)00028-9;
RA   Carrell R.W., Stein P.E., Fermi G., Wardell M.R.;
RT   "Biological implications of a 3 A structure of dimeric antithrombin.";
RL   Structure 2:257-270(1994).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   PubMed=7656006; DOI=10.1038/nsb0194-48;
RA   Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M.,
RA   Grootenhuis P.D.J., Hol W.G.J.;
RT   "The intact and cleaved human antithrombin III complex as a model for
RT   serpin-proteinase interactions.";
RL   Nat. Struct. Biol. 1:48-54(1994).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=9067613; DOI=10.1006/jmbi.1996.0798;
RA   Skinner R., Abrahams J.P., Whisstock J.C., Lesk A.M., Carrel R.W.,
RA   Wardell M.R.;
RT   "The 2.6 A structure of antithrombin indicates a conformational change at
RT   the heparin binding site.";
RL   J. Mol. Biol. 266:601-609(1997).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   PubMed=9761669; DOI=10.1006/jmbi.1998.2083;
RA   Skinner R., Chang W.-S.W., Jin L., Pei X.Y., Huntington J.A.,
RA   Abrahams J.P., Carrell R.W., Lomas D.A.;
RT   "Implications for function and therapy of a 2.9 A structure of binary-
RT   complexed antithrombin.";
RL   J. Mol. Biol. 283:9-14(1998).
RN   [30]
RP   REVIEW.
RX   PubMed=2126464; DOI=10.1016/0300-9084(90)90123-x;
RA   Mourey L., Samama J.-P., Delarue M., Choay J., Lormeau J.C., Petitou M.,
RA   Moras D.;
RT   "Antithrombin III: structural and functional aspects.";
RL   Biochimie 72:599-608(1990).
RN   [31]
RP   REVIEW ON VARIANTS.
RX   PubMed=8236149;
RA   Lane D.A., Olds R.J., Boisclair M., Chowdhury V., Thein S.L., Cooper D.N.,
RA   Blajchman M., Perry D., Emmerich J., Aiach M.;
RT   "Antithrombin III mutation database: first update. For the Thrombin and its
RT   Inhibitors Subcommittee of the Scientific and Standardization Committee of
RT   the International Society on Thrombosis and Haemostasis.";
RL   Thromb. Haemost. 70:361-369(1993).
RN   [32]
RP   REVIEW ON VARIANTS.
RX   PubMed=7749926; DOI=10.1038/nsb0295-96;
RA   Stein P.E., Carrell R.W.;
RT   "What do dysfunctional serpins tell us about molecular mobility and
RT   disease?";
RL   Nat. Struct. Biol. 2:96-113(1995).
RN   [33]
RP   REVIEW ON VARIANTS.
RX   PubMed=8664906;
RX   DOI=10.1002/(sici)1098-1004(1996)7:1<7::aid-humu2>3.0.co;2-b;
RA   Perry D.J., Carrell R.W.;
RT   "Molecular genetics of human antithrombin deficiency.";
RL   Hum. Mutat. 7:7-22(1996).
RN   [34]
RP   VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79;
RP   SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112;
RP   PHE-131; VAL-131; LYS-133; PHE-138-139-LYS DEL; PRO-148; PRO-150; PRO-158;
RP   TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219; LYS-219; ARG-257;
RP   LYS-269; ILE-283; ASN-316; LYS-334; ARG-412; THR-414; PRO-416; SER-416;
RP   VAL-419; ASP-424; CYS-425; HIS-425; PRO-425; LEU-426; CYS-434; LEU-434;
RP   SER-434; THR-436; LYS-437; GLY-438; MET-438; LEU-439; THR-439; THR-453;
RP   ARG-456; THR-457; ASP-459; LEU-461 AND PHE-462, AND VARIANTS GLU-30; THR-52
RP   AND CYS-190.
RX   PubMed=9031473;
RG   The plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis;
RA   Lane D.A., Bayston T., Olds R.J., Fitches A.C., Cooper D.N., Millar D.S.,
RA   Jochmans K., Perry D.J., Okajima K., Thein S.L., Emmerich J.;
RT   "Antithrombin mutation database: 2nd (1997) update.";
RL   Thromb. Haemost. 77:197-211(1997).
RN   [35]
RP   VARIANT AT3D CYS-79.
RX   PubMed=6582486; DOI=10.1073/pnas.81.2.289;
RA   Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N.;
RT   "Antithrombin III Toyama: replacement of arginine-47 by cysteine in
RT   hereditary abnormal antithrombin III that lacks heparin-binding ability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:289-293(1984).
RN   [36]
RP   VARIANT AT3D LEU-73, AND CHARACTERIZATION OF VARIANT AT3D LEU-73.
RX   PubMed=3080419;
RA   Chang J.Y., Tran T.H.;
RT   "Antithrombin III Basel. Identification of a Pro-Leu substitution in a
RT   hereditary abnormal antithrombin with impaired heparin cofactor activity.";
RL   J. Biol. Chem. 261:1174-1176(1986).
RN   [37]
RP   VARIANT AT3D LEU-426.
RX   PubMed=3805013;
RA   Stephens A.W., Thalley B.S., Hirs C.H.W.;
RT   "Antithrombin-III Denver, a reactive site variant.";
RL   J. Biol. Chem. 262:1044-1048(1987).
RN   [38]
RP   VARIANT AT3D THR-414.
RX   PubMed=3179438;
RA   Devrak-Kizuk R., Chui D.H.K., Prochownik E.V., Carter C.J., Ofosu F.A.,
RA   Blajchman M.A.;
RT   "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to
RT   adenine) in codon 382 causing impaired serine protease reactivity.";
RL   Blood 72:1518-1523(1988).
RN   [39]
RP   VARIANTS AT3D CYS-425 AND HIS-425.
RX   PubMed=3162733;
RA   Erdjument H., Laned D.A., Panico M., di Marzo V., Morris H.R.;
RT   "Single amino acid substitutions in the reactive site of antithrombin
RT   leading to thrombosis. Congenital substitution of arginine 393 to cysteine
RT   in antithrombin Northwick Park and to histidine in antithrombin Glasgow.";
RL   J. Biol. Chem. 263:5589-5593(1988).
RN   [40]
RP   VARIANT AT3D HIS-425.
RX   PubMed=2781509; DOI=10.1016/0049-3848(89)90127-8;
RA   Erdjument H., Lane D.A., Panico M., di Marzo V., Morris H.R., Bauer K.,
RA   Rosenberg R.D.;
RT   "Antithrombin Chicago, amino acid substitution of arginine 393 to
RT   histidine.";
RL   Thromb. Res. 54:613-619(1989).
RN   [41]
RP   VARIANT AT3D CYS-56.
RX   PubMed=2365065; DOI=10.1016/0014-5793(90)81530-2;
RA   Borg J.Y., Brennan S.O., Carrell R.W., George P., Perry D.J., Shaw J.;
RT   "Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution to
RT   heparin binding.";
RL   FEBS Lett. 266:163-166(1990).
RN   [42]
RP   VARIANT GLU-30.
RX   PubMed=1977621; DOI=10.1016/0014-5793(90)81057-u;
RA   Daly M., Bruce D., Perry D.J., Price J., Harper P.L., O'Meara A.,
RA   Carrell R.W.;
RT   "Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has an
RT   aberrant signal peptidase cleavage site.";
RL   FEBS Lett. 273:87-90(1990).
RN   [43]
RP   VARIANT AT3D GLN-161.
RX   PubMed=2229057;
RA   Gandrille S., Aiach M., Lane D.A., Vidaud D., Molho-Sabatier P., Caso R.,
RA   de Moerloose P., Fiessinger J.-N., Clauser E.;
RT   "Important role of arginine 129 in heparin-binding site of antithrombin
RT   III. Identification of a novel mutation arginine 129 to glutamine.";
RL   J. Biol. Chem. 265:18997-19001(1990).
RN   [44]
RP   CHARACTERIZATION OF VARIANT AT3D THR-414, AND MUTAGENESIS OF ALA-414.
RX   PubMed=2013320; DOI=10.1016/0014-5793(91)80305-m;
RA   Austin R.C., Rachubinski R.A., Blachjman M.A.;
RT   "Site-directed mutagenesis of alanine-382 of human antithrombin III.";
RL   FEBS Lett. 280:254-258(1991).
RN   [45]
RP   VARIANT AT3D SER-416.
RX   PubMed=1906811; DOI=10.1016/0014-5793(91)80809-h;
RA   Perry D.J., Daly M., Harper P.L., Tait R.C., Price J., Walker I.D.,
RA   Carrell R.W.;
RT   "Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of
RT   the reactive centre loop in the inhibitory function of the serpins.";
RL   FEBS Lett. 285:248-250(1991).
RN   [46]
RP   VARIANT AT3D PHE-131.
RX   PubMed=1555650; DOI=10.1016/0014-5793(92)80854-a;
RA   Olds R.J., Lane D.A., Boisclair M., Sas G., Bock S.C., Thein S.L.;
RT   "Antithrombin Budapest 3. An antithrombin variant with reduced heparin
RT   affinity resulting from the substitution L99F.";
RL   FEBS Lett. 300:241-246(1992).
RN   [47]
RP   VARIANT AT3D ASP-424.
RX   PubMed=1547341;
RA   Blajchman M.A., Fernandez-Rachubinski F., Sheffield W.P., Austin R.C.,
RA   Schulman S.;
RT   "Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with normal
RT   heparin binding and impaired serine protease reactivity.";
RL   Blood 79:1428-1434(1992).
RN   [48]
RP   VARIANT AT3D PRO-148.
RX   PubMed=8443391;
RA   Okajima K., Abe H., Maeda S., Motomura M., Tsujihata M., Nagataki S.,
RA   Okabe H., Takatsuki K.;
RT   "Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with
RT   defective heparin binding associated with thrombosis.";
RL   Blood 81:1300-1305(1993).
RN   [49]
RP   VARIANT AT3D 138-PHE-LYS-139 DEL.
RX   PubMed=8486379; DOI=10.1006/geno.1993.1184;
RA   Olds R.J., Lane D.A., Beresford C.H., Abildgaard U., Hughes P.M.,
RA   Thein S.L.;
RT   "A recurrent deletion in the antithrombin gene, AT106-108(-6 bp),
RT   identified by DNA heteroduplex detection.";
RL   Genomics 16:298-299(1993).
RN   [50]
RP   VARIANTS AT3D HIS-79 AND TYR-160.
RX   PubMed=7981186; DOI=10.1161/01.atv.14.12.1958;
RA   Emmerich J., Vidaud D., Alhenc-Gelas M., Chadeuf G., Gouault-Heilmann M.,
RA   Aillaud M.-F., Aiach M.;
RT   "Three novel mutations of antithrombin inducing high-molecular-mass
RT   compounds.";
RL   Arterioscler. Thromb. 14:1958-1965(1994).
RN   [51]
RP   VARIANTS AT3D THR-112; TYR-152 AND ILE-283, AND VARIANT CYS-190.
RX   PubMed=7959685; DOI=10.1007/bf00211016;
RA   Millar D.S., Wacey A.I., Ribando J., Melissari E., Laursen B., Woods P.,
RA   Kakkar V.V., Cooper D.N.;
RT   "Three novel missense mutations in the antithrombin III (AT3) gene causing
RT   recurrent venous thrombosis.";
RL   Hum. Genet. 94:509-512(1994).
RN   [52]
RP   VARIANT AT3D ARG-456.
RX   PubMed=8274732;
RA   Jochmans K., Lissens W., Vervoort R., Peeters S., de Waelwe M.,
RA   Liebaers I.;
RT   "Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1
RT   antithrombin deficiency and neonatal thrombosis.";
RL   Blood 83:146-151(1994).
RN   [53]
RP   VARIANTS AT3D SER-95; THR-453 AND PHE-462.
RX   PubMed=7994035;
RA   van Boven H.H., Olds R.J., Thein S.L., Reitsma P.H., Lane D.A., Briet E.,
RA   Vandenbroucke J.P., Rosendaal F.R.;
RT   "Hereditary antithrombin deficiency: heterogeneity of the molecular basis
RT   and mortality in Dutch families.";
RL   Blood 84:4209-4213(1994).
RN   [54]
RP   VARIANT AT3D ASP-219.
RX   PubMed=7989582; DOI=10.1172/jci117589;
RA   Bruce D., Perry D.J., Borg J.-Y., Carrell R.W., Wardell M.R.;
RT   "Thromboembolic disease due to thermolabile conformational changes of
RT   antithrombin Rouen-VI (187 Asn-->Asp).";
RL   J. Clin. Invest. 94:2265-2274(1994).
RN   [55]
RP   VARIANTS AT3D VAL-131 AND PRO-150.
RA   Chowdhury V., Olds R.J., Lane D.A., Mille B., Pabinger I., Thein S.L.;
RT   "Two novel antithrombin variants (L99V and Q118P) which alter the heparin
RT   binding domain.";
RL   Nouv. Rev. Fr. Hematol. 86:268-268(1994).
RN   [56]
RP   VARIANT AT3D 273-LYS--LYS-307 DEL.
RX   PubMed=7878627;
RA   Emmerich J., Chadeuf G., Alhenc-Gelas M., Gouault-Heilman M., Toulon P.,
RA   Fiessinger J.-N., Aiach M.;
RT   "Molecular basis of antithrombin type I deficiency: the first large in-
RT   frame deletion and two novel mutations in exon 6.";
RL   Thromb. Haemost. 72:534-539(1994).
RN   [57]
RP   VARIANT AT3D HIS-425.
RX   PubMed=7832187; DOI=10.1002/ajh.2830480104;
RA   Okajima K., Abe H., Wagatsuma M., Okabe H., Takatsuki K.;
RT   "Antithrombin III Kumamoto II; a single mutation at Arg393-His increased
RT   the affinity of antithrombin III for heparin.";
RL   Am. J. Hematol. 48:12-18(1995).
RN   [58]
RP   VARIANT AT3D ARG-127.
RX   PubMed=9157604;
RA   Ozawa T., Takikawa Y., Niiya K., Fujiwara T., Suzuki K., Sato S.,
RA   Sakuragawa N.;
RT   "Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing type
RT   I antithrombin deficiency.";
RL   Thromb. Haemost. 77:403-403(1997).
RN   [59]
RP   VARIANT AT3D PRO-23.
RX   PubMed=9845533;
RA   Fitches A.C., Appleby R., Lane D.A., De Stefano V., Leone G., Olds R.J.;
RT   "Impaired cotranslational processing as a mechanism for type I antithrombin
RT   deficiency.";
RL   Blood 92:4671-4676(1998).
RN   [60]
RP   VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412.
RX   PubMed=9759613;
RA   Jochmans K., Lissens W., Seneca S., Capel P., Chatelain B., Meeus P.,
RA   Osselaer J.C., Peerlinck K., Seghers J., Slacmeulder M., Stibbe J.,
RA   van de Loo J., Vermylen J., Liebaers I., De Waele M.;
RT   "The molecular basis of antithrombin deficiency in Belgian and Dutch
RT   families.";
RL   Thromb. Haemost. 80:376-381(1998).
RN   [61]
RP   VARIANT THR-167.
RX   PubMed=10361121;
RA   Bayston T.A., Tripodi A., Mannucci P.M., Thompson E., Ireland H.,
RA   Fitches A.C., Hananeia L., Olds R.J., Lane D.A.;
RT   "Familial overexpression of beta-antithrombin caused by an Asn135-to-Thr
RT   substitution.";
RL   Blood 93:4242-4247(1999).
RN   [62]
RP   VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397.
RX   PubMed=10997988; DOI=10.1046/j.1365-2141.2000.02245.x;
RA   Picard V., Bura A., Emmerich J., Alhenc-Gelas M., Biron C.,
RA   Houbouyan-Reveillard L.L., Molho P., Labatide-Alanore A., Sie P.,
RA   Toulon P., Verdy E., Aiach M.;
RT   "Molecular bases of antithrombin deficiency in French families:
RT   identification of seven novel mutations in the antithrombin gene.";
RL   Br. J. Haematol. 110:731-734(2000).
RN   [63]
RP   VARIANT AT3D 152-HIS--PHE-154 DEL.
RX   PubMed=11794707; DOI=10.1007/bf02982095;
RA   Niiya K., Kiguchi T., Dansako H., Fujimura K., Fujimoto T., Iijima K.,
RA   Tanimoto M., Harada M.;
RT   "Two novel gene mutations in type I antithrombin deficiency.";
RL   Int. J. Hematol. 74:469-472(2001).
RN   [64]
RP   VARIANT AT3D PRO-223.
RX   PubMed=11713457; DOI=10.1067/mpd.2001.118191;
RA   Baud O., Picard V., Durand P., Duchemin J., Proulle V., Alhenc-Gelas M.,
RA   Devictor D., Dreyfus M.;
RT   "Intracerebral hemorrhage associated with a novel antithrombin gene
RT   mutation in a neonate.";
RL   J. Pediatr. 139:741-743(2001).
RN   [65]
RP   VARIANT AT3D GLU-146.
RX   PubMed=12353073; DOI=10.1267/THRO88030436;
RA   Mushunje A., Zhou A., Huntington J.A., Conard J., Carrell R.W.;
RT   "Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin
RT   affinity.";
RL   Thromb. Haemost. 88:436-443(2002).
RN   [66]
RP   VARIANT AT3D LEU-261.
RX   PubMed=12595305; DOI=10.1182/blood-2002-11-3391;
RA   Picard V., Dautzenberg M.-D., Villoutreix B.O., Orliaguet G.,
RA   Alhenc-Gelas M., Aiach M.;
RT   "Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous
RT   antithrombin polymerization in vivo associated with severe childhood
RT   thrombosis.";
RL   Blood 102:919-925(2003).
RN   [67]
RP   VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441.
RX   PubMed=12894857; DOI=10.1007/bf02983246;
RA   Nagaizumi K., Inaba H., Amano K., Suzuki M., Arai M., Fukutake K.;
RT   "Five novel and four recurrent point mutations in the antithrombin gene
RT   causing venous thrombosis.";
RL   Int. J. Hematol. 78:79-83(2003).
RN   [68]
RP   VARIANTS AT3D LEU-179; CYS-425 AND LEU-426.
RX   PubMed=15164384; DOI=10.1002/ajh.20067;
RA   David D., Ribeiro S., Ferrao L., Gago T., Crespo F.;
RT   "Molecular basis of inherited antithrombin deficiency in Portuguese
RT   families: identification of genetic alterations and screening for
RT   additional thrombotic risk factors.";
RL   Am. J. Hematol. 76:163-171(2004).
RN   [69]
RP   VARIANT AT3D HIS-398.
RX   PubMed=16908819; DOI=10.1001/archopht.124.8.1165;
RA   Kuhli C., Jochmans K., Scharrer I., Luechtenberg M., Hattenbach L.-O.;
RT   "Retinal vein occlusion associated with antithrombin deficiency secondary
RT   to a novel G9840C missense mutation.";
RL   Arch. Ophthalmol. 124:1165-1169(2006).
RN   [70]
RP   VARIANTS AT3D PHE-53; LEU-73; ASP-125; PRO-170; ASN-218; GLY-248; PRO-293;
RP   ARG-401; CYS-425; GLY-438 AND ALA-439, AND VARIANT GLU-30.
RX   PubMed=23910795; DOI=10.1111/jth.12364;
RA   Puurunen M., Salo P., Engelbarth S., Javela K., Perola M.;
RT   "Type II antithrombin deficiency caused by a founder mutation Pro73Leu in
RT   the Finnish population: clinical picture.";
RL   J. Thromb. Haemost. 11:1844-1849(2013).
CC   -!- FUNCTION: Most important serine protease inhibitor in plasma that
CC       regulates the blood coagulation cascade. AT-III inhibits thrombin,
CC       matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its
CC       inhibitory activity is greatly enhanced in the presence of heparin.
CC       {ECO:0000269|PubMed:15853774}.
CC   -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
CC   -!- INTERACTION:
CC       P01008; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-1039832, EBI-7147442;
CC       P01008; P01008: SERPINC1; NbExp=2; IntAct=EBI-1039832, EBI-1039832;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Found in plasma.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000269|PubMed:26091039}.
CC   -!- MASS SPECTROMETRY: Mass=57863; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7734359};
CC   -!- MASS SPECTROMETRY: Mass=57911; Method=Electrospray; Note=Variant Thr-
CC       414.; Evidence={ECO:0000269|PubMed:7734359};
CC   -!- DISEASE: Antithrombin III deficiency (AT3D) [MIM:613118]: An important
CC       risk factor for hereditary thrombophilia, a hemostatic disorder
CC       characterized by a tendency to recurrent thrombosis. Antithrombin-III
CC       deficiency is classified into 4 types. Type I: characterized by a 50%
CC       decrease in antigenic and functional levels. Type II: has defects
CC       affecting the thrombin-binding domain. Type III: alteration of the
CC       heparin-binding domain. Plasma AT-III antigen levels are normal in type
CC       II and III. Type IV: consists of miscellaneous group of unclassifiable
CC       mutations. {ECO:0000269|PubMed:10997988, ECO:0000269|PubMed:11713457,
CC       ECO:0000269|PubMed:11794707, ECO:0000269|PubMed:12353073,
CC       ECO:0000269|PubMed:12595305, ECO:0000269|PubMed:12894857,
CC       ECO:0000269|PubMed:15164384, ECO:0000269|PubMed:1547341,
CC       ECO:0000269|PubMed:1555650, ECO:0000269|PubMed:16908819,
CC       ECO:0000269|PubMed:1906811, ECO:0000269|PubMed:2013320,
CC       ECO:0000269|PubMed:2229057, ECO:0000269|PubMed:2365065,
CC       ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:2781509,
CC       ECO:0000269|PubMed:3080419, ECO:0000269|PubMed:3162733,
CC       ECO:0000269|PubMed:3179438, ECO:0000269|PubMed:3191114,
CC       ECO:0000269|PubMed:3805013, ECO:0000269|PubMed:6582486,
CC       ECO:0000269|PubMed:7734359, ECO:0000269|PubMed:7832187,
CC       ECO:0000269|PubMed:7878627, ECO:0000269|PubMed:7959685,
CC       ECO:0000269|PubMed:7981186, ECO:0000269|PubMed:7989582,
CC       ECO:0000269|PubMed:7994035, ECO:0000269|PubMed:8274732,
CC       ECO:0000269|PubMed:8443391, ECO:0000269|PubMed:8486379,
CC       ECO:0000269|PubMed:9031473, ECO:0000269|PubMed:9157604,
CC       ECO:0000269|PubMed:9759613, ECO:0000269|PubMed:9845533,
CC       ECO:0000269|Ref.3, ECO:0000269|Ref.55}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Antithrombin entry;
CC       URL="https://en.wikipedia.org/wiki/Antithrombin";
CC   -!- WEB RESOURCE: Name=Antithrombin mutation database;
CC       URL="https://www1.imperial.ac.uk/departmentofmedicine/divisions/experimentalmedicine/haematology/coag/antithrombin/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/serpinc1/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=SERPINC1";
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DR   EMBL; L00185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L00186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L00190; AAB40025.1; -; Genomic_DNA.
DR   EMBL; D29832; BAA06212.1; -; mRNA.
DR   EMBL; X68793; CAA48690.1; -; Genomic_DNA.
DR   EMBL; AF130100; AAG35525.1; -; mRNA.
DR   EMBL; AK312654; BAG35537.1; -; mRNA.
DR   EMBL; AF386078; AAK60337.1; -; Genomic_DNA.
DR   EMBL; AL136170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW90969.1; -; Genomic_DNA.
DR   EMBL; M21643; AAA51793.1; -; Genomic_DNA.
DR   EMBL; M21644; AAA51794.1; -; Genomic_DNA.
DR   EMBL; M21643; AAA51794.1; JOINED; Genomic_DNA.
DR   EMBL; M21642; AAA51796.1; -; Genomic_DNA.
DR   EMBL; M21636; AAA51796.1; JOINED; Genomic_DNA.
DR   EMBL; M21637; AAA51796.1; JOINED; Genomic_DNA.
DR   EMBL; M21638; AAA51796.1; JOINED; Genomic_DNA.
DR   EMBL; M21640; AAA51796.1; JOINED; Genomic_DNA.
DR   EMBL; M21641; AAA51796.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS1313.1; -.
DR   PIR; A49494; XHHU3.
DR   RefSeq; NP_000479.1; NM_000488.3.
DR   PDB; 1ANT; X-ray; 3.00 A; I/L=33-464.
DR   PDB; 1ATH; X-ray; 3.20 A; A/B=33-464.
DR   PDB; 1AZX; X-ray; 2.90 A; I/L=33-464.
DR   PDB; 1BR8; X-ray; 2.90 A; I/L=33-464.
DR   PDB; 1DZG; X-ray; 2.80 A; I/L=33-464.
DR   PDB; 1DZH; X-ray; 2.85 A; I/L=33-464.
DR   PDB; 1E03; X-ray; 2.90 A; I/L=33-464.
DR   PDB; 1E04; X-ray; 2.60 A; I/L=33-464.
DR   PDB; 1E05; X-ray; 2.62 A; I/L=33-464.
DR   PDB; 1JVQ; X-ray; 2.60 A; I/L=33-464.
DR   PDB; 1LK6; X-ray; 2.80 A; I/L=33-464.
DR   PDB; 1NQ9; X-ray; 2.60 A; I/L=33-464.
DR   PDB; 1OYH; X-ray; 2.62 A; I/L=33-464.
DR   PDB; 1R1L; X-ray; 2.70 A; I/L=33-464.
DR   PDB; 1SR5; X-ray; 3.10 A; A=33-464.
DR   PDB; 1T1F; X-ray; 2.75 A; A/B/C=33-464.
DR   PDB; 1TB6; X-ray; 2.50 A; I=33-464.
DR   PDB; 2ANT; X-ray; 2.60 A; I/L=33-464.
DR   PDB; 2B4X; X-ray; 2.80 A; I/L=37-463.
DR   PDB; 2B5T; X-ray; 2.10 A; I=33-464.
DR   PDB; 2BEH; X-ray; 2.70 A; I/L=33-464.
DR   PDB; 2GD4; X-ray; 3.30 A; C/I=22-464.
DR   PDB; 2HIJ; X-ray; 2.90 A; I/L=33-464.
DR   PDB; 2ZNH; X-ray; 2.80 A; A/B=33-464.
DR   PDB; 3EVJ; X-ray; 3.00 A; I/L=33-464.
DR   PDB; 3KCG; X-ray; 1.70 A; I=33-464.
DR   PDB; 4EB1; X-ray; 2.80 A; I/L=33-464.
DR   PDBsum; 1ANT; -.
DR   PDBsum; 1ATH; -.
DR   PDBsum; 1AZX; -.
DR   PDBsum; 1BR8; -.
DR   PDBsum; 1DZG; -.
DR   PDBsum; 1DZH; -.
DR   PDBsum; 1E03; -.
DR   PDBsum; 1E04; -.
DR   PDBsum; 1E05; -.
DR   PDBsum; 1JVQ; -.
DR   PDBsum; 1LK6; -.
DR   PDBsum; 1NQ9; -.
DR   PDBsum; 1OYH; -.
DR   PDBsum; 1R1L; -.
DR   PDBsum; 1SR5; -.
DR   PDBsum; 1T1F; -.
DR   PDBsum; 1TB6; -.
DR   PDBsum; 2ANT; -.
DR   PDBsum; 2B4X; -.
DR   PDBsum; 2B5T; -.
DR   PDBsum; 2BEH; -.
DR   PDBsum; 2GD4; -.
DR   PDBsum; 2HIJ; -.
DR   PDBsum; 2ZNH; -.
DR   PDBsum; 3EVJ; -.
DR   PDBsum; 3KCG; -.
DR   PDBsum; 4EB1; -.
DR   PCDDB; P01008; -.
DR   SMR; P01008; -.
DR   BioGRID; 106953; 27.
DR   DIP; DIP-38009N; -.
DR   IntAct; P01008; 16.
DR   MINT; P01008; -.
DR   STRING; 9606.ENSP00000356671; -.
DR   BindingDB; P01008; -.
DR   ChEMBL; CHEMBL1950; -.
DR   DrugBank; DB11598; Antithrombin III human.
DR   DrugBank; DB00407; Ardeparin.
DR   DrugBank; DB09258; Bemiparin.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB06779; Dalteparin.
DR   DrugBank; DB06754; Danaparoid.
DR   DrugBank; DB01225; Enoxaparin.
DR   DrugBank; DB00569; Fondaparinux.
DR   DrugBank; DB01109; Heparin.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   DrugBank; DB08813; Nadroparin.
DR   DrugBank; DB09141; Protamine sulfate.
DR   DrugBank; DB05361; SR-123781A.
DR   DrugBank; DB06271; Sulodexide.
DR   DrugBank; DB06822; Tinzaparin.
DR   DrugCentral; P01008; -.
DR   GuidetoPHARMACOLOGY; 2632; -.
DR   MEROPS; I04.018; -.
DR   CarbonylDB; P01008; -.
DR   GlyConnect; 766; 21 N-Linked glycans (5 sites).
DR   GlyGen; P01008; 7 sites, 24 N-linked glycans (4 sites), 2 O-linked glycans (1 site).
DR   iPTMnet; P01008; -.
DR   PhosphoSitePlus; P01008; -.
DR   BioMuta; SERPINC1; -.
DR   DMDM; 113936; -.
DR   DOSAC-COBS-2DPAGE; P01008; -.
DR   REPRODUCTION-2DPAGE; P01008; -.
DR   SWISS-2DPAGE; P01008; -.
DR   CPTAC; non-CPTAC-1070; -.
DR   CPTAC; non-CPTAC-1071; -.
DR   CPTAC; non-CPTAC-1072; -.
DR   EPD; P01008; -.
DR   jPOST; P01008; -.
DR   MassIVE; P01008; -.
DR   MaxQB; P01008; -.
DR   PaxDb; P01008; -.
DR   PeptideAtlas; P01008; -.
DR   PRIDE; P01008; -.
DR   ProteomicsDB; 12609; -.
DR   ProteomicsDB; 51299; -.
DR   Antibodypedia; 793; 853 antibodies.
DR   DNASU; 462; -.
DR   Ensembl; ENST00000367698; ENSP00000356671; ENSG00000117601.
DR   GeneID; 462; -.
DR   KEGG; hsa:462; -.
DR   UCSC; uc001gjt.4; human.
DR   CTD; 462; -.
DR   DisGeNET; 462; -.
DR   GeneCards; SERPINC1; -.
DR   HGNC; HGNC:775; SERPINC1.
DR   HPA; ENSG00000117601; Tissue enriched (liver).
DR   MalaCards; SERPINC1; -.
DR   MIM; 107300; gene.
DR   MIM; 613118; phenotype.
DR   neXtProt; NX_P01008; -.
DR   OpenTargets; ENSG00000117601; -.
DR   Orphanet; 82; Hereditary thrombophilia due to congenital antithrombin deficiency.
DR   PharmGKB; PA35026; -.
DR   VEuPathDB; HostDB:ENSG00000117601; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000157967; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P01008; -.
DR   OMA; PICIYRN; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; P01008; -.
DR   TreeFam; TF343094; -.
DR   PathwayCommons; P01008; -.
DR   Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SIGNOR; P01008; -.
DR   BioGRID-ORCS; 462; 7 hits in 1009 CRISPR screens.
DR   ChiTaRS; SERPINC1; human.
DR   EvolutionaryTrace; P01008; -.
DR   GeneWiki; Antithrombin; -.
DR   GenomeRNAi; 462; -.
DR   Pharos; P01008; Tclin.
DR   PRO; PR:P01008; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P01008; protein.
DR   Bgee; ENSG00000117601; Expressed in right lobe of liver and 104 other tissues.
DR   ExpressionAtlas; P01008; baseline and differential.
DR   Genevisible; P01008; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   GO; GO:2000266; P:regulation of blood coagulation, intrinsic pathway; IEA:InterPro.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   CDD; cd02045; serpinC1_AT3; 1.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR033829; Antithrombin_3_serpin_domain.
DR   InterPro; IPR015555; AT-III.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   PANTHER; PTHR11461:SF53; PTHR11461:SF53; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Glycoprotein; Hemostasis; Heparin-binding;
KW   Phosphoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal; Thrombophilia.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|Ref.10"
FT   CHAIN           33..464
FT                   /note="Antithrombin-III"
FT                   /id="PRO_0000032489"
FT   BINDING         81
FT                   /note="Heparin"
FT   BINDING         161
FT                   /note="Heparin"
FT   BINDING         177
FT                   /note="Heparin"
FT   SITE            425..426
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000269|PubMed:7238875"
FT   MOD_RES         63
FT                   /note="Phosphothreonine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         68
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|Ref.10"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|Ref.10"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT                   ECO:0000269|Ref.10"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16263699,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10"
FT   DISULFID        40..160
FT                   /evidence="ECO:0000269|Ref.10"
FT   DISULFID        53..127
FT                   /evidence="ECO:0000269|Ref.10"
FT   DISULFID        279..462
FT                   /evidence="ECO:0000269|Ref.10"
FT   VARIANT         17
FT                   /note="Y -> S (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_027450"
FT   VARIANT         23
FT                   /note="L -> P (in AT3D; type-I; does not undergo post-
FT                   translational glycosylation; dbSNP:rs387906575)"
FT                   /evidence="ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|PubMed:9845533"
FT                   /id="VAR_012748"
FT   VARIANT         30
FT                   /note="V -> E (in Dublin; dbSNP:rs2227624)"
FT                   /evidence="ECO:0000269|PubMed:1977621,
FT                   ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_007032"
FT   VARIANT         32
FT                   /note="C -> R (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9759613"
FT                   /id="VAR_027451"
FT   VARIANT         39
FT                   /note="I -> N (in AT3D; type-II; Rouen-3; lack of heparin-
FT                   binding properties; dbSNP:rs121909558)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007033"
FT   VARIANT         52
FT                   /note="M -> T (previously Whitechapel; dbSNP:rs892712171)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007034"
FT   VARIANT         53
FT                   /note="C -> F (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071199"
FT   VARIANT         56
FT                   /note="R -> C (in AT3D; type-II; Rouen-4; lack of heparin-
FT                   binding properties; dbSNP:rs28929469)"
FT                   /evidence="ECO:0000269|PubMed:2365065,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007035"
FT   VARIANT         73
FT                   /note="P -> L (in AT3D; type-II; lacks heparin-binding
FT                   ability; dbSNP:rs121909551)"
FT                   /evidence="ECO:0000269|PubMed:23910795,
FT                   ECO:0000269|PubMed:3080419, ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|PubMed:9759613"
FT                   /id="VAR_007036"
FT   VARIANT         79
FT                   /note="R -> C (in AT3D; Tours/Alger/Amiens/Toyama/Paris-1/
FT                   Paris-2/Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; lacks
FT                   heparin-binding ability; dbSNP:rs121909547)"
FT                   /evidence="ECO:0000269|PubMed:6582486,
FT                   ECO:0000269|PubMed:9031473, ECO:0000269|PubMed:9759613"
FT                   /id="VAR_007037"
FT   VARIANT         79
FT                   /note="R -> H (in AT3D; type-II; Rouen-1/Padua-1/Bligny/
FT                   Budapest-2; lack of heparin-binding properties;
FT                   dbSNP:rs121909552)"
FT                   /evidence="ECO:0000269|PubMed:7981186,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007038"
FT   VARIANT         79
FT                   /note="R -> S (in AT3D; type-II; Rouen-2; lack of heparin-
FT                   binding properties; dbSNP:rs121909547)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007039"
FT   VARIANT         87
FT                   /note="Missing (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007040"
FT   VARIANT         89
FT                   /note="R -> C (in AT3D; type-I; dbSNP:rs147266200)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007041"
FT   VARIANT         90
FT                   /note="F -> L (in AT3D; type-I; Budapest-6)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007042"
FT   VARIANT         95
FT                   /note="Y -> C (in AT3D; type-I; dbSNP:rs907768931)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_027452"
FT   VARIANT         95
FT                   /note="Y -> S (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7994035,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_012316"
FT   VARIANT         98
FT                   /note="L -> P (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_027453"
FT   VARIANT         108..109
FT                   /note="Missing (in AT3D; type-I)"
FT                   /id="VAR_007043"
FT   VARIANT         112
FT                   /note="P -> T (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7959685,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007044"
FT   VARIANT         121
FT                   /note="M -> K (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:12894857"
FT                   /id="VAR_027454"
FT   VARIANT         125
FT                   /note="G -> D (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071200"
FT   VARIANT         127
FT                   /note="C -> R (in AT3D; type-I; dbSNP:rs121909573)"
FT                   /evidence="ECO:0000269|PubMed:9157604"
FT                   /id="VAR_027455"
FT   VARIANT         131
FT                   /note="L -> F (in AT3D; type-II; Budapest-3/Budapest-7;
FT                   dbSNP:rs121909567)"
FT                   /evidence="ECO:0000269|PubMed:1555650,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007045"
FT   VARIANT         131
FT                   /note="L -> V (in AT3D; type-II; Southport)"
FT                   /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.55"
FT                   /id="VAR_007046"
FT   VARIANT         133
FT                   /note="Q -> K (in AT3D; type I; dbSNP:rs1411331203)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007047"
FT   VARIANT         138..139
FT                   /note="Missing (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:8486379"
FT                   /id="VAR_007048"
FT   VARIANT         146
FT                   /note="K -> E (in AT3D; Dreux; complete loss af heparin
FT                   binding; dbSNP:rs1170430756)"
FT                   /evidence="ECO:0000269|PubMed:12353073"
FT                   /id="VAR_027456"
FT   VARIANT         147
FT                   /note="T -> A (in dbSNP:rs2227606)"
FT                   /evidence="ECO:0000269|Ref.7"
FT                   /id="VAR_013085"
FT   VARIANT         148
FT                   /note="S -> P (in AT3D; type-II; Nagasaki; defective
FT                   heparin binding associated with thrombosis;
FT                   dbSNP:rs121909569)"
FT                   /evidence="ECO:0000269|PubMed:8443391,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007049"
FT   VARIANT         150
FT                   /note="Q -> P (in AT3D; type-II; Vienna;
FT                   dbSNP:rs765445413)"
FT                   /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.55"
FT                   /id="VAR_007050"
FT   VARIANT         152..154
FT                   /note="Missing (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:11794707"
FT                   /id="VAR_012749"
FT   VARIANT         152
FT                   /note="H -> Y (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7959685"
FT                   /id="VAR_007051"
FT   VARIANT         153
FT                   /note="Missing (in AT3D; type-I)"
FT                   /id="VAR_007052"
FT   VARIANT         158
FT                   /note="L -> P (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007053"
FT   VARIANT         160
FT                   /note="C -> Y (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7981186,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_027457"
FT   VARIANT         161
FT                   /note="R -> Q (in AT3D; type-II; Geneva;
FT                   dbSNP:rs121909563)"
FT                   /evidence="ECO:0000269|PubMed:2229057,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007054"
FT   VARIANT         167
FT                   /note="N -> T (in dbSNP:rs121909570)"
FT                   /evidence="ECO:0000269|PubMed:10361121"
FT                   /id="VAR_012750"
FT   VARIANT         170
FT                   /note="S -> P (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071201"
FT   VARIANT         178
FT                   /note="L -> H (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:12894857"
FT                   /id="VAR_027458"
FT   VARIANT         179
FT                   /note="F -> L (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:15164384"
FT                   /id="VAR_027459"
FT   VARIANT         190
FT                   /note="Y -> C (variant of uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:7959685,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007055"
FT   VARIANT         198
FT                   /note="Y -> C (in AT3D; type-I and -II; Whitechapel;
FT                   dbSNP:rs1425532034)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007056"
FT   VARIANT         198
FT                   /note="Y -> H (in AT3D; type-I; dbSNP:rs1572090114)"
FT                   /evidence="ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|PubMed:9759613"
FT                   /id="VAR_027460"
FT   VARIANT         214
FT                   /note="S -> F (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:10997988"
FT                   /id="VAR_027461"
FT   VARIANT         214
FT                   /note="S -> Y (in AT3D; type-I; dbSNP:rs483352854)"
FT                   /id="VAR_007057"
FT   VARIANT         218
FT                   /note="I -> N (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071202"
FT   VARIANT         218
FT                   /note="Missing (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_027462"
FT   VARIANT         219
FT                   /note="N -> D (in AT3D; type-II; Rouen-6; increases
FT                   affinity for heparin; dbSNP:rs121909571)"
FT                   /evidence="ECO:0000269|PubMed:7989582,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007059"
FT   VARIANT         219
FT                   /note="N -> K (in AT3D; type-II; Glasgow-3)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007058"
FT   VARIANT         223
FT                   /note="S -> P (in AT3D; type-I; dbSNP:rs121909572)"
FT                   /evidence="ECO:0000269|PubMed:10997988,
FT                   ECO:0000269|PubMed:11713457"
FT                   /id="VAR_027463"
FT   VARIANT         243
FT                   /note="T -> I (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:10997988"
FT                   /id="VAR_027464"
FT   VARIANT         248
FT                   /note="V -> G (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071203"
FT   VARIANT         251
FT                   /note="I -> T (in AT3D; type-I; dbSNP:rs1423630663)"
FT                   /evidence="ECO:0000269|PubMed:10997988"
FT                   /id="VAR_027465"
FT   VARIANT         257
FT                   /note="W -> R (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|PubMed:9759613"
FT                   /id="VAR_027466"
FT   VARIANT         261
FT                   /note="F -> L (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:12595305"
FT                   /id="VAR_027467"
FT   VARIANT         269
FT                   /note="E -> K (in AT3D; type-II; Truro; increases affinity
FT                   for heparin; dbSNP:rs758087836)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007060"
FT   VARIANT         273..307
FT                   /note="Missing (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7878627"
FT                   /id="VAR_007061"
FT   VARIANT         283
FT                   /note="M -> I (in AT3D; type-II)"
FT                   /evidence="ECO:0000269|PubMed:7959685,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007062"
FT   VARIANT         283
FT                   /note="M -> V (in AT3D; type-II)"
FT                   /evidence="ECO:0000269|PubMed:10997988"
FT                   /id="VAR_027468"
FT   VARIANT         293
FT                   /note="R -> P (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071204"
FT   VARIANT         302
FT                   /note="L -> P (in AT3D; type-I)"
FT                   /id="VAR_007063"
FT   VARIANT         316
FT                   /note="I -> N (in AT3D; type-II; Haslar/Whitechapel)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007064"
FT   VARIANT         323
FT                   /note="S -> P (in AT3D)"
FT                   /id="VAR_027469"
FT   VARIANT         334
FT                   /note="E -> K (in AT3D; type-II)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007065"
FT   VARIANT         344
FT                   /note="Missing (in AT3D; type-I)"
FT                   /id="VAR_007066"
FT   VARIANT         381
FT                   /note="S -> P (in AT3D; type-I; dbSNP:rs121909565)"
FT                   /id="VAR_007067"
FT   VARIANT         391
FT                   /note="R -> Q (in dbSNP:rs201541724)"
FT                   /id="VAR_007068"
FT   VARIANT         397
FT                   /note="S -> P (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:10997988"
FT                   /id="VAR_027470"
FT   VARIANT         398
FT                   /note="D -> H (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:16908819"
FT                   /id="VAR_027471"
FT   VARIANT         401
FT                   /note="H -> R (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071205"
FT   VARIANT         412
FT                   /note="S -> R (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:9031473,
FT                   ECO:0000269|PubMed:9759613"
FT                   /id="VAR_027472"
FT   VARIANT         414
FT                   /note="A -> T (in AT3D; type-II; Hamilton/Glasgow-2;
FT                   reduces interaction with thrombin by 90%;
FT                   dbSNP:rs121909557)"
FT                   /evidence="ECO:0000269|PubMed:2013320,
FT                   ECO:0000269|PubMed:3179438, ECO:0000269|PubMed:7734359,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007069"
FT   VARIANT         416
FT                   /note="A -> P (in AT3D; type-II; Charleville/Sudbury/
FT                   Vicenza/Cambridge-1; dbSNP:rs121909548)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007070"
FT   VARIANT         416
FT                   /note="A -> S (in AT3D; type-II; Cambridge-2;
FT                   dbSNP:rs121909548)"
FT                   /evidence="ECO:0000269|PubMed:1906811,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007071"
FT   VARIANT         419
FT                   /note="A -> V (in AT3D; type-I; dbSNP:rs121909568)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007072"
FT   VARIANT         424
FT                   /note="G -> D (in AT3D; type-II; Stockholm;
FT                   dbSNP:rs121909566)"
FT                   /evidence="ECO:0000269|PubMed:1547341,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007073"
FT   VARIANT         425
FT                   /note="R -> C (in AT3D; type-II; dbSNP:rs121909554)"
FT                   /evidence="ECO:0000269|PubMed:12894857,
FT                   ECO:0000269|PubMed:15164384, ECO:0000269|PubMed:23910795,
FT                   ECO:0000269|PubMed:3162733, ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007075"
FT   VARIANT         425
FT                   /note="R -> H (in AT3D; type-II; Glasgow/Sheffield/Chicago/
FT                   Avranches/Kumamoto-2; increases affinity for heparin;
FT                   deprived of inhibitory activity; dbSNP:rs121909549)"
FT                   /evidence="ECO:0000269|PubMed:12894857,
FT                   ECO:0000269|PubMed:2781509, ECO:0000269|PubMed:3162733,
FT                   ECO:0000269|PubMed:7832187, ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007074"
FT   VARIANT         425
FT                   /note="R -> P (in AT3D; type-II; Pescara; deprived of
FT                   inhibitory of activity; dbSNP:rs121909549)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007076"
FT   VARIANT         426
FT                   /note="S -> L (in AT3D; type-II; Denver/Milano-2; deprived
FT                   of inhibitory activity; dbSNP:rs121909550)"
FT                   /evidence="ECO:0000269|PubMed:15164384,
FT                   ECO:0000269|PubMed:3805013, ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007077"
FT   VARIANT         434
FT                   /note="F -> C (in AT3D; type-II; Rosny;
FT                   dbSNP:rs1572084546)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007078"
FT   VARIANT         434
FT                   /note="F -> L (in AT3D; type-II; Maisons-Laffite)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007080"
FT   VARIANT         434
FT                   /note="F -> S (in AT3D; type-II; Torino)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007079"
FT   VARIANT         436
FT                   /note="A -> T (in AT3D; type-II; Oslo/Paris-3;
FT                   dbSNP:rs121909546)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007081"
FT   VARIANT         437
FT                   /note="N -> K (in AT3D; type-II; La Rochelle;
FT                   dbSNP:rs1301351856)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007082"
FT   VARIANT         438
FT                   /note="R -> G (in AT3D; type I and type-II)"
FT                   /evidence="ECO:0000269|PubMed:23910795,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_009258"
FT   VARIANT         438
FT                   /note="R -> M (in AT3D; type-II; Kyoto)"
FT                   /evidence="ECO:0000269|PubMed:9031473, ECO:0000269|Ref.3"
FT                   /id="VAR_007083"
FT   VARIANT         439
FT                   /note="P -> A (in AT3D)"
FT                   /evidence="ECO:0000269|PubMed:23910795"
FT                   /id="VAR_071206"
FT   VARIANT         439
FT                   /note="P -> L (in AT3D; type-II; Utah; deprived of
FT                   inhibitory activity; dbSNP:rs121909555)"
FT                   /evidence="ECO:0000269|PubMed:3191114,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007084"
FT   VARIANT         439
FT                   /note="P -> T (in AT3D; type-II; Budapest-5;
FT                   dbSNP:rs1487411568)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007085"
FT   VARIANT         441
FT                   /note="L -> P (in AT3D; type-II; dbSNP:rs1188571702)"
FT                   /evidence="ECO:0000269|PubMed:12894857"
FT                   /id="VAR_027473"
FT   VARIANT         453
FT                   /note="I -> T (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7994035,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007086"
FT   VARIANT         456
FT                   /note="G -> R (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:8274732,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007087"
FT   VARIANT         457
FT                   /note="R -> T (in AT3D; type-II)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007088"
FT   VARIANT         459..461
FT                   /note="Missing (in AT3D; type-I)"
FT                   /id="VAR_007089"
FT   VARIANT         459
FT                   /note="A -> D (in AT3D; type-I; dbSNP:rs1572084448)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007090"
FT   VARIANT         461
FT                   /note="P -> L (in AT3D; type-II; Budapest;
FT                   dbSNP:rs121909564)"
FT                   /evidence="ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007091"
FT   VARIANT         462
FT                   /note="C -> F (in AT3D; type-I)"
FT                   /evidence="ECO:0000269|PubMed:7994035,
FT                   ECO:0000269|PubMed:9031473"
FT                   /id="VAR_007092"
FT   MUTAGEN         414
FT                   /note="A->K: Reduces interaction with thrombin by 99%."
FT                   /evidence="ECO:0000269|PubMed:2013320"
FT   MUTAGEN         414
FT                   /note="A->Q: Reduces interaction with thrombin by 80%."
FT                   /evidence="ECO:0000269|PubMed:2013320"
FT   CONFLICT        69..70
FT                   /note="EQ -> QE (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="N -> NN (in Ref. 3; BAA06212)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="H -> R (in Ref. 5; AAG35525)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="A -> T (in Ref. 6; BAG35537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        226
FT                   /note="T -> A (in Ref. 6; BAG35537)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247..249
FT                   /note="Missing (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="Missing (in Ref. 13; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="Y -> YA (in Ref. 13; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:1OYH"
FT   HELIX           78..101
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:1DZG"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           112..123
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           128..137
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:2B5T"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           151..166
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          170..181
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:1E04"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           207..225
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            226..228
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:2B4X"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:1DZG"
FT   STRAND          245..255
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:2B5T"
FT   STRAND          278..294
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          300..306
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          309..317
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:2B5T"
FT   HELIX           324..329
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          344..353
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          355..362
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           364..369
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            384..386
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          389..392
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          398..407
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          409..413
FT                   /evidence="ECO:0007829|PDB:2B5T"
FT   STRAND          419..422
FT                   /evidence="ECO:0007829|PDB:1E04"
FT   STRAND          423..426
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          432..435
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          440..446
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   TURN            447..450
FT                   /evidence="ECO:0007829|PDB:3KCG"
FT   STRAND          451..459
FT                   /evidence="ECO:0007829|PDB:3KCG"
SQ   SEQUENCE   464 AA;  52602 MW;  9A4E324F00683D9D CRC64;
     MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK
     KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA
     MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG
     DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN
     ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ
     VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG
     FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV
     VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK
//
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