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Database: UniProt
Entry: P05155
LinkDB: P05155
Original site: P05155 
ID   IC1_HUMAN               Reviewed;         500 AA.
AC   P05155; A6NMU0; A8KAI9; B2R6L5; B4E1F0; B4E1H2; Q16304; Q547W3; Q59EI5;
AC   Q7Z455; Q96FE0; Q9UC49; Q9UCF9;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   29-SEP-2021, entry version 242.
DE   RecName: Full=Plasma protease C1 inhibitor;
DE            Short=C1 Inh;
DE            Short=C1Inh;
DE   AltName: Full=C1 esterase inhibitor;
DE   AltName: Full=C1-inhibiting factor;
DE   AltName: Full=Serpin G1;
DE   Flags: Precursor;
GN   Name=SERPING1; Synonyms=C1IN, C1NH;
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 [MRNA] (ISOFORM 1).
RX   PubMed=3488058; DOI=10.1016/0006-291x(86)91123-x;
RA   Que B.G., Petra P.H.;
RT   "Isolation and analysis of a cDNA coding for human C1 inhibitor.";
RL   Biochem. Biophys. Res. Commun. 137:620-625(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP   GLYCOSYLATION AT ASN-25; THR-48; SER-64; ASN-69; THR-71; ASN-81; THR-83;
RP   THR-88; THR-92; THR-96; ASN-238; ASN-253 AND ASN-352.
RX   PubMed=3756141; DOI=10.1021/bi00363a018;
RA   Bock S.C., Skriver K., Nielsen E., Thoegersen H.-C., Wiman B.,
RA   Donaldson V.H., Eddy R.L., Marrinan J., Radziejewska E., Huber R.,
RA   Shows T.B., Magnusson S.;
RT   "Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal
RT   localization.";
RL   Biochemistry 25:4292-4301(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=3267220; DOI=10.1111/j.1432-1033.1988.tb13980.x;
RA   Carter P.E., Dunbar B., Fothergill J.E.;
RT   "Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon junctions
RT   and comparison with other serpins.";
RL   Eur. J. Biochem. 173:163-169(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2026152; DOI=10.1111/j.1432-1033.1991.tb15911.x;
RA   Carter P.E., Duponchel C., Tosi M., Fothergill J.E.;
RT   "Complete nucleotide sequence of the gene for human C1 inhibitor with an
RT   unusually high density of Alu elements.";
RL   Eur. J. Biochem. 197:301-308(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Foreskin;
RA   Heus J., Platenburg-Kootwijk E., Meershoek E., De Winter R.,
RA   Knijnenburg J., Kupers L., Habex H., Renaers I., Samuel C., Bonnarens L.,
RA   Hoffman S., Brouwer M., Hack E., Horbach D., Timmermans M., Nuijens J.,
RA   Pieper F.;
RT   "Production of recombinant human C1 inhibitor in milk of transgenic rabbits
RT   for potential use in enzyme replacement therapy for hereditary
RT   angioedema.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Heart, Liver, Ovary, and Uterus;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-480.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-480.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-480.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [11]
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   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-480.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-500 (ISOFORM 1).
RX   PubMed=3393514;
RA   Rauth G., Schumacher G., Buckel P., Mueller-Esterl W.;
RT   "Molecular cloning of the cDNA coding for human C1 inhibitor.";
RL   Protein Seq. Data Anal. 1:251-257(1988).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-188, AND VARIANT HAE
RP   84-ASP--THR-138 DEL.
RC   TISSUE=Blood;
RX   PubMed=12773530; DOI=10.1074/jbc.m302977200;
RA   Bos I.G.A., Lubbers Y.T.P., Roem D., Abrahams J.P., Hack C.E., Eldering E.;
RT   "The functional integrity of the serpin domain of C1-inhibitor depends on
RT   the unique N-terminal domain, as revealed by a pathological mutant.";
RL   J. Biol. Chem. 278:29463-29470(2003).
RN   [15]
RP   PROTEIN SEQUENCE OF 23-62.
RX   PubMed=6416294; DOI=10.1021/bi00290a019;
RA   Harrison R.A.;
RT   "Human C1 inhibitor: improved isolation and preliminary structural
RT   characterization.";
RL   Biochemistry 22:5001-5007(1983).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-228.
RX   PubMed=2154751; DOI=10.1073/pnas.87.4.1551;
RA   Stoppa-Lyonnet D., Carter P.E., Meo T., Tosi M.;
RT   "Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus
RT   to deleterious rearrangements.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1551-1555(1990).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 213-500 (ISOFORM 1/2/3).
RX   PubMed=3089875; DOI=10.1016/0378-1119(86)90230-1;
RA   Tosi M., Duponchel C., Bourgarel P., Colomb M., Meo T.;
RT   "Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-
RT   antitrypsin and other members of the serpins superfamily.";
RL   Gene 42:265-272(1986).
RN   [18]
RP   PROTEIN SEQUENCE OF 217-233.
RX   PubMed=8618290; DOI=10.1016/s0022-5347(01)66050-6;
RA   Pillai S., Wright D., Gupta A., Zhou G., Hull G., Jiang H., Zhang H.;
RT   "Molecular weights and isoelectric points of sperm antigens relevant to
RT   autoimmune infertility in men.";
RL   J. Urol. 155:1928-1933(1996).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 241-458 (ISOFORM 1/2/3), AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   PubMed=3458172; DOI=10.1073/pnas.83.10.3161;
RA   Davis A.E. III, Whitehead A.S., Harrison R.A., Dauphinias A., Bruns G.A.,
RA   Cicardi M., Rosen F.S.;
RT   "Human inhibitor of the first component of complement, C1: characterization
RT   of cDNA clones and localization of the gene to chromosome 11.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3161-3165(1986).
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-500, AND VARIANTS HAE MET-473;
RP   ARG-481; PRO-481; ARG-489 AND SER-498.
RX   PubMed=7814636; DOI=10.1172/jci117663;
RA   Verpy E., Couture-Tosi E., Eldering E., Lopez-Trascasa M., Spath P.,
RA   Meo T., Tosi M.;
RT   "Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by
RT   pathogenic mutants impaired in secretion or function.";
RL   J. Clin. Invest. 95:350-359(1995).
RN   [21]
RP   PROTEIN SEQUENCE OF 464-481, FUNCTION, AND REACTIVE SITE FOR CHYMOTRYPSIN.
RC   TISSUE=Plasma;
RX   PubMed=8495195; DOI=10.1002/pro.5560020504;
RA   Aulak K.S., Davis A.E. III, Donaldson V.H., Harrison R.A.;
RT   "Chymotrypsin inhibitory activity of normal C1-inhibitor and a P1 Arg to
RT   His mutant: evidence for the presence of overlapping reactive centers.";
RL   Protein Sci. 2:727-732(1993).
RN   [22]
RP   INTERACTION WITH MASP1.
RX   PubMed=10946292; DOI=10.4049/jimmunol.165.5.2637;
RA   Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.;
RT   "Proteolytic activities of two types of mannose-binding lectin-associated
RT   serine protease.";
RL   J. Immunol. 165:2637-2642(2000).
RN   [23]
RP   INTERACTION WITH E.COLI STCE, AND PROTEOLYTIC PROCESSING BY E.COLI STCE.
RX   PubMed=12123444; DOI=10.1046/j.1365-2958.2002.02997.x;
RA   Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B., Tarr P.I.,
RA   Welch R.A.;
RT   "StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically
RT   cleaves C1 esterase inhibitor.";
RL   Mol. Microbiol. 45:277-288(2002).
RN   [24]
RP   GLYCOSYLATION AT ASN-253.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [25]
RP   INTERACTION WITH E.COLI STCE, AND PROTEOLYTIC PROCESSING BY E.COLI STCE.
RX   PubMed=15096536; DOI=10.1084/jem.20030255;
RA   Lathem W.W., Bergsbaken T., Welch R.A.;
RT   "Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted
RT   by Escherichia coli O157:H7.";
RL   J. Exp. Med. 199:1077-1087(2004).
RN   [26]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-238; ASN-253 AND
RP   ASN-352.
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   [27]
RP   GLYCOSYLATION AT ASN-25.
RX   PubMed=16040958; DOI=10.1128/iai.73.8.4478-4487.2005;
RA   Liu D., Cramer C.C., Scafidi J., Davis A.E. III;
RT   "N-linked glycosylation at Asn3 and the positively charged residues within
RT   the amino-terminal domain of the c1 inhibitor are required for interaction
RT   of the C1 Inhibitor with Salmonella enterica serovar typhimurium
RT   lipopolysaccharide and lipid A.";
RL   Infect. Immun. 73:4478-4487(2005).
RN   [28]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-69; ASN-238; ASN-253
RP   AND ASN-352.
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   [29]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-81; ASN-238; ASN-253
RP   AND ASN-352.
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   [30]
RP   GLYCOSYLATION AT ASN-238; ASN-253 AND ASN-352.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [31]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, 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   [32]
RP   GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OF CARBOHYDRATES, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [33]
RP   GLYCOSYLATION AT THR-47 AND THR-48, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=23234360; DOI=10.1021/pr300963h;
RA   Halim A., Ruetschi U., Larson G., Nilsson J.;
RT   "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT   of human cerebrospinal fluid glycoproteins.";
RL   J. Proteome Res. 12:573-584(2013).
RN   [34]
RP   IDENTIFICATION BY 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   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 119-500, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-238.
RX   PubMed=17488724; DOI=10.1074/jbc.m700841200;
RA   Beinrohr L., Harmat V., Dobo J., Loerincz Z., Gal P., Zavodszky P.;
RT   "C1 inhibitor serpin domain structure reveals the likely mechanism of
RT   heparin potentiation and conformational disease.";
RL   J. Biol. Chem. 282:21100-21109(2007).
RN   [36]
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   [37]
RP   VARIANT HAE HIS-466.
RX   PubMed=3178731; DOI=10.1042/bj2530615;
RA   Aulak K.S., Pemberton P.A., Rosen F.S., Carrell R.W., Lachmann P.J.,
RA   Harrison R.A.;
RT   "Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-
RT   oedema plasma, contains a P1 'reactive centre' (Arg444-->His) mutation.";
RL   Biochem. J. 253:615-618(1988).
RN   [38]
RP   VARIANT HAE SER-466.
RX   PubMed=2365061; DOI=10.1016/0014-5793(90)81494-9;
RA   Aulak K.S., Cicardi M., Harrison R.A.;
RT   "Identification of a new P1 residue mutation (444Arg-->Ser) in a
RT   dysfunctional C1 inhibitor protein contained in a type II hereditary
RT   angioedema plasma.";
RL   FEBS Lett. 266:13-16(1990).
RN   [39]
RP   VARIANT HAE THR-458.
RX   PubMed=2296585; DOI=10.1073/pnas.87.1.265;
RA   Levy N.J., Ramesh N., Cicardi M., Harrison R.A., Davis A.E. III;
RT   "Type II hereditary angioneurotic edema that may result from a single
RT   nucleotide change in the codon for alanine-436 in the C1 inhibitor gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:265-268(1990).
RN   [40]
RP   VARIANT HAE LYS-273 DEL.
RX   PubMed=2118657; DOI=10.1073/pnas.87.17.6786;
RA   Parad R.B., Kramer J., Strunk R.C., Rosen F.S., Davis A.E. III;
RT   "Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition
RT   of an N-glycosylation site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6786-6790(1990).
RN   [41]
RP   VARIANTS HAE GLU-456 AND VAL-458.
RA   Siddique Z.M., McPhaden A.R., Whaley K.;
RT   "Identification of type II hereditary angio-oedema (HAE) mutations.";
RL   Clin. Exp. Immunol. 86:11-12(1991).
RN   [42]
RP   VARIANT HAE LEU-466.
RX   PubMed=1451784; DOI=10.1016/0014-5793(92)80204-t;
RA   Frange D., Aulak K.S., Cicardi M., Harrison R.A., Davis A.E. III;
RT   "A dysfunctional C1 inhibitor protein with a new reactive center mutation
RT   (Arg-444-->Leu).";
RL   FEBS Lett. 301:34-36(1992).
RN   [43]
RP   VARIANTS HAE GLU-454 AND THR-458.
RX   PubMed=1363816; DOI=10.1038/ng0892-354;
RA   Davis A.E. III, Aulak K., Parad R.B., Stecklein H.P., Eldering E.,
RA   Hack C.E., Kramer J., Strunk R.C., Bissler J., Rosen F.S.;
RT   "C1 inhibitor hinge region mutations produce dysfunction by different
RT   mechanisms.";
RL   Nat. Genet. 1:354-358(1992).
RN   [44]
RP   VARIANT HAE ARG-429.
RX   PubMed=8172583;
RA   Davis A.E. III, Bissler J.J., Cicardi M.;
RT   "Mutations in the C1 inhibitor gene that result in hereditary angioneurotic
RT   edema.";
RL   Behring Inst. Mitt. 93:313-320(1993).
RN   [45]
RP   VARIANT HAE VAL-465.
RX   PubMed=7883978; DOI=10.1172/jci117780;
RA   Zahedi R., Bissler J.J., Davis A.E. III, Andreadis C., Wisnieski J.J.;
RT   "Unique C1 inhibitor dysfunction in a kindred without angioedema. II.
RT   Identification of an Ala443-->Val substitution and functional analysis of
RT   the recombinant mutant protein.";
RL   J. Clin. Invest. 95:1299-1305(1995).
RN   [46]
RP   VARIANT HAE PRO-467.
RX   PubMed=8529136; DOI=10.1007/bf03401610;
RA   Ocejo-Vinyals J.G., Leyva-Cobian F., Fernandez-Luna J.L.;
RT   "A mutation unique in serine protease inhibitors (serpins) identified in a
RT   family with type II hereditary angioneurotic edema.";
RL   Mol. Med. 1:700-705(1995).
RN   [47]
RP   VARIANTS HAE.
RX   PubMed=8755917;
RA   Verpy E., Biasotto M., Brai M., Misiano G., Meo T., Tosi M.;
RT   "Exhaustive mutation scanning by fluorescence-assisted mismatch analysis
RT   discloses new genotype-phenotype correlations in angiodema.";
RL   Am. J. Hum. Genet. 59:308-319(1996).
RN   [48]
RP   VARIANTS HAE TYR-130; PRO-394; VAL-408; CYS-466; GLU-473; GLU-493 AND
RP   ARG-498.
RX   PubMed=14635117; DOI=10.1002/humu.9202;
RA   Kalmar L., Bors A., Farkas H., Vas S., Fandl B., Varga L., Fuest G.,
RA   Tordai A.;
RT   "Mutation screening of the C1 inhibitor gene among Hungarian patients with
RT   hereditary angioedema.";
RL   Hum. Mutat. 22:498-498(2003).
RN   [49]
RP   VARIANT HAE ARG-345, AND VARIANTS ALA-56 AND MET-480.
RX   PubMed=16409206; DOI=10.1111/j.1398-9995.2006.01010.x;
RA   Kang H.-R., Yim E.-Y., Oh S.-Y., Chang Y.-S., Kim Y.-K., Cho S.-H.,
RA   Min K.-U., Kim Y.-Y.;
RT   "Normal C1 inhibitor mRNA expression level in type I hereditary angioedema
RT   patients: newly found C1 inhibitor gene mutations.";
RL   Allergy 61:260-264(2006).
RN   [50]
RP   VARIANTS HAE ALA-118; CYS-154; PHE-170; ARG-184; PRO-230; LYS-232; ASN-272
RP   DEL; ARG-299; GLN-430; THR-441; PRO-447; SER-466; CYS-466; LEU-466; GLY-473
RP   AND GLY-497, AND VARIANTS ALA-56 AND MET-480.
RX   PubMed=22994404; DOI=10.1111/all.12024;
RA   Xu Y.Y., Zhi Y.X., Yin J., Wang L.L., Wen L.P., Gu J.Q., Guan K., Craig T.,
RA   Zhang H.Y.;
RT   "Mutational spectrum and geno-phenotype correlation in Chinese families
RT   with Hereditary Angioedema.";
RL   Allergy 67:1430-1436(2012).
RN   [51]
RP   VARIANTS HAE ARG-11; ARG-265; VAL-274; THR-458; CYS-466; HIS-466; ARG-493
RP   AND GLU-493.
RX   PubMed=24456027; DOI=10.1111/ahg.12052;
RA   Bafunno V., Bova M., Loffredo S., Divella C., Petraroli A., Marone G.,
RA   Montinaro V., Margaglione M., Triggiani M.;
RT   "Mutational spectrum of the c1 inhibitor gene in a cohort of Italian
RT   patients with hereditary angioedema: description of nine novel mutations.";
RL   Ann. Hum. Genet. 78:73-82(2014).
CC   -!- FUNCTION: Activation of the C1 complex is under control of the C1-
CC       inhibitor. It forms a proteolytically inactive stoichiometric complex
CC       with the C1r or C1s proteases. May play a potentially crucial role in
CC       regulating important physiological pathways including complement
CC       activation, blood coagulation, fibrinolysis and the generation of
CC       kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and
CC       kallikrein. {ECO:0000269|PubMed:8495195}.
CC   -!- SUBUNIT: Binds to E.coli stcE which allows localization of SERPING1 to
CC       cell membranes thus protecting the bacteria against complement-mediated
CC       lysis. Interacts with MASP1. {ECO:0000269|PubMed:10946292,
CC       ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.
CC   -!- INTERACTION:
CC       P05155; O43889-2: CREB3; NbExp=3; IntAct=EBI-1223454, EBI-625022;
CC       P05155; PRO_0000037310 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-1223454, EBI-25474098;
CC       P05155; PRO_0000037320 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-1223454, EBI-25487328;
CC       P05155; O82882: stcE; Xeno; NbExp=3; IntAct=EBI-1223454, EBI-15979286;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P05155-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P05155-2; Sequence=VSP_056662;
CC       Name=3;
CC         IsoId=P05155-3; Sequence=VSP_056663;
CC   -!- PTM: Highly glycosylated (49%) with N- and O-glycosylation. O-
CC       glycosylated with core 1 or possibly core 8 glycans. N-glycan
CC       heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor),
CC       Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
CC       {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
CC       ECO:0000269|PubMed:16040958, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490,
CC       ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
CC       ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360,
CC       ECO:0000269|PubMed:3756141}.
CC   -!- PTM: Can be proteolytically cleaved by E.coli stcE.
CC       {ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.
CC   -!- POLYMORPHISM: Chymotrypsin uses Ala-465 as its reactive site in normal
CC       plasma protease C1 inhibitor, and His-466 as its reactive site in the
CC       variant His-466.
CC   -!- DISEASE: Hereditary angioedema (HAE) [MIM:106100]: An autosomal
CC       dominant disorder characterized by episodic local swelling involving
CC       subcutaneous or submucous tissue of the upper respiratory and
CC       gastrointestinal tracts, face, extremities, and genitalia. Hereditary
CC       angioedema due to C1 esterase inhibitor deficiency is comprised of two
CC       clinically indistinguishable forms. In hereditary angioedema type 1,
CC       serum levels of C1 esterase inhibitor are decreased, while in type 2,
CC       the levels are normal or elevated, but the protein is non-functional.
CC       {ECO:0000269|PubMed:12773530, ECO:0000269|PubMed:1363816,
CC       ECO:0000269|PubMed:1451784, ECO:0000269|PubMed:14635117,
CC       ECO:0000269|PubMed:16409206, ECO:0000269|PubMed:2118657,
CC       ECO:0000269|PubMed:2296585, ECO:0000269|PubMed:22994404,
CC       ECO:0000269|PubMed:2365061, ECO:0000269|PubMed:24456027,
CC       ECO:0000269|PubMed:3178731, ECO:0000269|PubMed:7814636,
CC       ECO:0000269|PubMed:7883978, ECO:0000269|PubMed:8172583,
CC       ECO:0000269|PubMed:8529136, ECO:0000269|PubMed:8755917,
CC       ECO:0000269|Ref.41}. Note=The disease is caused by variants affecting
CC       the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA53096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=C1-inhibitor entry;
CC       URL="https://en.wikipedia.org/wiki/C1-inhibitor";
CC   -!- WEB RESOURCE: Name=SERPING1base; Note=SERPING1 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/SERPING1base/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/serping1/";
CC   ---------------------------------------------------------------------------
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DR   EMBL; M13690; AAA35613.1; -; mRNA.
DR   EMBL; M13656; AAB59387.1; -; mRNA.
DR   EMBL; X07427; CAA30314.1; -; Genomic_DNA.
DR   EMBL; X07428; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07429; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07430; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07431; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07432; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07433; CAA30314.1; JOINED; Genomic_DNA.
DR   EMBL; X07577; CAA30469.1; -; mRNA.
DR   EMBL; X54486; CAA38358.1; -; Genomic_DNA.
DR   EMBL; AF435921; AAM21515.1; -; Genomic_DNA.
DR   EMBL; AK293054; BAF85743.1; -; mRNA.
DR   EMBL; AK303809; BAG64762.1; -; mRNA.
DR   EMBL; AK303840; BAG64784.1; -; mRNA.
DR   EMBL; AK312626; BAG35512.1; -; mRNA.
DR   EMBL; BT006966; AAP35612.1; -; mRNA.
DR   EMBL; AB209826; BAD93063.1; -; mRNA.
DR   EMBL; AY904027; AAW69393.1; -; Genomic_DNA.
DR   EMBL; AP000662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW73764.1; -; Genomic_DNA.
DR   EMBL; BC011171; AAH11171.1; -; mRNA.
DR   EMBL; AY291075; AAQ19269.1; -; Genomic_DNA.
DR   EMBL; M30688; AAA53096.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M14036; AAA51848.1; -; mRNA.
DR   EMBL; M13203; AAA51849.1; -; mRNA.
DR   EMBL; S76944; AAB33044.2; -; Genomic_DNA.
DR   CCDS; CCDS7962.1; -. [P05155-1]
DR   PIR; S15386; ITHUC1.
DR   RefSeq; NP_000053.2; NM_000062.2. [P05155-1]
DR   RefSeq; NP_001027466.1; NM_001032295.1. [P05155-1]
DR   PDB; 1M6Q; Model; -; A=138-500.
DR   PDB; 2OAY; X-ray; 2.35 A; A=119-500.
DR   PDB; 5DU3; X-ray; 2.10 A; A/B=119-500.
DR   PDB; 5DUQ; X-ray; 2.90 A; A/B=118-500.
DR   PDB; 7AKV; EM; 3.60 A; A=98-500.
DR   PDBsum; 1M6Q; -.
DR   PDBsum; 2OAY; -.
DR   PDBsum; 5DU3; -.
DR   PDBsum; 5DUQ; -.
DR   PDBsum; 7AKV; -.
DR   SMR; P05155; -.
DR   BioGRID; 107171; 32.
DR   DIP; DIP-45635N; -.
DR   IntAct; P05155; 19.
DR   MINT; P05155; -.
DR   STRING; 9606.ENSP00000278407; -.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB05961; PPL-100.
DR   MEROPS; I04.024; -.
DR   GlyConnect; 749; 41 N-Linked glycans (5 sites), 7 O-Linked glycans (3 sites).
DR   GlyGen; P05155; 25 sites, 53 N-linked glycans (5 sites), 8 O-linked glycans (11 sites).
DR   iPTMnet; P05155; -.
DR   PhosphoSitePlus; P05155; -.
DR   BioMuta; SERPING1; -.
DR   DMDM; 124096; -.
DR   CPTAC; CPTAC-1305; -.
DR   CPTAC; CPTAC-684; -.
DR   CPTAC; non-CPTAC-1147; -.
DR   CPTAC; non-CPTAC-1148; -.
DR   EPD; P05155; -.
DR   jPOST; P05155; -.
DR   MassIVE; P05155; -.
DR   PaxDb; P05155; -.
DR   PeptideAtlas; P05155; -.
DR   PRIDE; P05155; -.
DR   ProteomicsDB; 51806; -. [P05155-1]
DR   ProteomicsDB; 5752; -.
DR   ProteomicsDB; 5757; -.
DR   TopDownProteomics; P05155-1; -. [P05155-1]
DR   Antibodypedia; 14214; 565 antibodies.
DR   DNASU; 710; -.
DR   Ensembl; ENST00000278407; ENSP00000278407; ENSG00000149131. [P05155-1]
DR   Ensembl; ENST00000378323; ENSP00000367574; ENSG00000149131. [P05155-3]
DR   Ensembl; ENST00000378324; ENSP00000367575; ENSG00000149131. [P05155-2]
DR   Ensembl; ENST00000676670; ENSP00000504807; ENSG00000149131. [P05155-1]
DR   GeneID; 710; -.
DR   KEGG; hsa:710; -.
DR   UCSC; uc001nkp.2; human. [P05155-1]
DR   CTD; 710; -.
DR   DisGeNET; 710; -.
DR   GeneCards; SERPING1; -.
DR   HGNC; HGNC:1228; SERPING1.
DR   HPA; ENSG00000149131; Tissue enriched (liver).
DR   MalaCards; SERPING1; -.
DR   MIM; 106100; phenotype.
DR   MIM; 606860; gene.
DR   neXtProt; NX_P05155; -.
DR   OpenTargets; ENSG00000149131; -.
DR   Orphanet; 459353; C1 inhibitor deficiency.
DR   Orphanet; 100050; Hereditary angioedema type 1.
DR   Orphanet; 100051; Hereditary angioedema type 2.
DR   PharmGKB; PA35029; -.
DR   VEuPathDB; HostDB:ENSG00000149131; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000159681; -.
DR   HOGENOM; CLU_023330_3_0_1; -.
DR   InParanoid; P05155; -.
DR   OMA; EFFDFTY; -.
DR   PhylomeDB; P05155; -.
DR   TreeFam; TF317350; -.
DR   PathwayCommons; P05155; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-9657689; Defective SERPING1 causes hereditary angioedema.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SIGNOR; P05155; -.
DR   BioGRID-ORCS; 710; 6 hits in 1010 CRISPR screens.
DR   ChiTaRS; SERPING1; human.
DR   EvolutionaryTrace; P05155; -.
DR   GeneWiki; C1-inhibitor; -.
DR   GenomeRNAi; 710; -.
DR   Pharos; P05155; Tbio.
DR   PRO; PR:P05155; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P05155; protein.
DR   Bgee; ENSG00000149131; Expressed in right lobe of liver and 242 other tissues.
DR   ExpressionAtlas; P05155; baseline and differential.
DR   Genevisible; P05155; 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; HDA:UniProtKB.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; IDA:UniProtKB.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR015553; C1-inh.
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:SF159; PTHR11461:SF159; 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; Alternative splicing; Blood coagulation; Complement pathway;
KW   Direct protein sequencing; Disease variant; Disulfide bond; Fibrinolysis;
KW   Glycoprotein; Hemostasis; Immunity; Innate immunity; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:6416294"
FT   CHAIN           23..500
FT                   /note="Plasma protease C1 inhibitor"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT                   /id="PRO_0000032514"
FT   REPEAT          85..88
FT                   /note="1"
FT   REPEAT          89..92
FT                   /note="2"
FT   REPEAT          93..96
FT                   /note="3"
FT   REPEAT          97..100
FT                   /note="4"
FT   REPEAT          101..104
FT                   /note="5"
FT   REPEAT          105..108
FT                   /note="6"
FT   REPEAT          116..119
FT                   /note="7"
FT   REGION          20..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..119
FT                   /note="7 X 4 AA tandem repeats of [QE]-P-T-[TQ]"
FT   COMPBIAS        20..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            465..466
FT                   /note="Reactive bond for chymotrypsin"
FT   SITE            466..467
FT                   /note="Reactive bond"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16040958, ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:3756141"
FT   CARBOHYD        47
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320,
FT                   ECO:0000269|PubMed:23234360"
FT   CARBOHYD        48
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:22171320,
FT                   ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:3756141"
FT   CARBOHYD        64
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3756141"
FT   CARBOHYD        71
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:3756141"
FT   CARBOHYD        83
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        88
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        92
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        96
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:3756141"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17488724,
FT                   ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:3756141"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:3756141"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine; in variant TA"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
FT                   ECO:0000269|PubMed:3756141"
FT   DISULFID        123..428
FT                   /evidence="ECO:0000269|PubMed:17488724,
FT                   ECO:0000269|PubMed:3756141"
FT   DISULFID        130..205
FT                   /evidence="ECO:0000269|PubMed:17488724,
FT                   ECO:0000269|PubMed:3756141"
FT   VAR_SEQ         1..52
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056662"
FT   VAR_SEQ         17
FT                   /note="G -> GFLEPQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056663"
FT   VARIANT         11
FT                   /note="L -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:24456027"
FT                   /id="VAR_071701"
FT   VARIANT         39
FT                   /note="D -> E (in dbSNP:rs11229062)"
FT                   /id="VAR_027374"
FT   VARIANT         56
FT                   /note="V -> A (in dbSNP:rs11546660)"
FT                   /evidence="ECO:0000269|PubMed:16409206,
FT                   ECO:0000269|PubMed:22994404"
FT                   /id="VAR_027375"
FT   VARIANT         84..138
FT                   /note="Missing (in HAE; phenotype consistent with
FT                   hereditary angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:12773530"
FT                   /id="VAR_046202"
FT   VARIANT         118
FT                   /note="T -> A (in HAE; dbSNP:rs200534715)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068832"
FT   VARIANT         130
FT                   /note="C -> Y (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117"
FT                   /id="VAR_027379"
FT   VARIANT         154
FT                   /note="Y -> C (in HAE; dbSNP:rs281875168)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068833"
FT   VARIANT         170
FT                   /note="S -> F (in HAE; dbSNP:rs281875169)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068834"
FT   VARIANT         184
FT                   /note="G -> R (in HAE; dbSNP:rs281875170)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068835"
FT   VARIANT         230
FT                   /note="L -> P (in HAE; dbSNP:rs281875171)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068836"
FT   VARIANT         232
FT                   /note="I -> K (in HAE; dbSNP:rs281875172)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068837"
FT   VARIANT         265
FT                   /note="W -> R (in HAE)"
FT                   /evidence="ECO:0000269|PubMed:24456027"
FT                   /id="VAR_071702"
FT   VARIANT         272
FT                   /note="Missing (in HAE)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068838"
FT   VARIANT         273
FT                   /note="Missing (in HAE; phenotype consistent with
FT                   hereditary angioedema type 2; creates a new glycosylation
FT                   site)"
FT                   /evidence="ECO:0000269|PubMed:2118657"
FT                   /id="VAR_007012"
FT   VARIANT         274
FT                   /note="I -> V (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:24456027"
FT                   /id="VAR_071703"
FT   VARIANT         299
FT                   /note="W -> R (in HAE; dbSNP:rs281875173)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068839"
FT   VARIANT         308
FT                   /note="T -> S (in dbSNP:rs1803212)"
FT                   /id="VAR_011751"
FT   VARIANT         345
FT                   /note="G -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:16409206"
FT                   /id="VAR_027376"
FT   VARIANT         394
FT                   /note="T -> P (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117"
FT                   /id="VAR_027380"
FT   VARIANT         408
FT                   /note="D -> V (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117"
FT                   /id="VAR_027381"
FT   VARIANT         429
FT                   /note="G -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:8172583"
FT                   /id="VAR_007013"
FT   VARIANT         430
FT                   /note="L -> Q (in HAE; dbSNP:rs281875174)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068840"
FT   VARIANT         441
FT                   /note="M -> T (in HAE; dbSNP:rs281875175)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068841"
FT   VARIANT         447
FT                   /note="L -> P (in HAE; dbSNP:rs281875176)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068842"
FT   VARIANT         454
FT                   /note="V -> E (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs121907949)"
FT                   /evidence="ECO:0000269|PubMed:1363816"
FT                   /id="VAR_007014"
FT   VARIANT         456
FT                   /note="A -> E (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|Ref.41"
FT                   /id="VAR_007015"
FT   VARIANT         458
FT                   /note="A -> T (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs121907947)"
FT                   /evidence="ECO:0000269|PubMed:1363816,
FT                   ECO:0000269|PubMed:2296585, ECO:0000269|PubMed:24456027"
FT                   /id="VAR_007016"
FT   VARIANT         458
FT                   /note="A -> V (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|Ref.41"
FT                   /id="VAR_007017"
FT   VARIANT         465
FT                   /note="A -> V (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs121907950)"
FT                   /evidence="ECO:0000269|PubMed:7883978"
FT                   /id="VAR_007018"
FT   VARIANT         466
FT                   /note="R -> C (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs28940870)"
FT                   /evidence="ECO:0000269|PubMed:14635117,
FT                   ECO:0000269|PubMed:22994404, ECO:0000269|PubMed:24456027"
FT                   /id="VAR_007019"
FT   VARIANT         466
FT                   /note="R -> H (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs121907948)"
FT                   /evidence="ECO:0000269|PubMed:24456027,
FT                   ECO:0000269|PubMed:3178731"
FT                   /id="VAR_007020"
FT   VARIANT         466
FT                   /note="R -> L (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs121907948)"
FT                   /evidence="ECO:0000269|PubMed:1451784,
FT                   ECO:0000269|PubMed:22994404"
FT                   /id="VAR_007021"
FT   VARIANT         466
FT                   /note="R -> S (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2; dbSNP:rs28940870)"
FT                   /evidence="ECO:0000269|PubMed:22994404,
FT                   ECO:0000269|PubMed:2365061"
FT                   /id="VAR_007022"
FT   VARIANT         467
FT                   /note="T -> P (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:8529136"
FT                   /id="VAR_007023"
FT   VARIANT         473
FT                   /note="V -> E (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117"
FT                   /id="VAR_027382"
FT   VARIANT         473
FT                   /note="V -> G (in HAE; dbSNP:rs281875177)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068843"
FT   VARIANT         473
FT                   /note="V -> M (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:7814636"
FT                   /id="VAR_007024"
FT   VARIANT         474
FT                   /note="Q -> E"
FT                   /id="VAR_007025"
FT   VARIANT         477
FT                   /note="F -> S (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /id="VAR_007026"
FT   VARIANT         480
FT                   /note="V -> M (in dbSNP:rs4926)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:16409206, ECO:0000269|PubMed:22994404,
FT                   ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0000269|Ref.9"
FT                   /id="VAR_007027"
FT   VARIANT         481
FT                   /note="L -> P (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:7814636"
FT                   /id="VAR_007028"
FT   VARIANT         481
FT                   /note="L -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:7814636"
FT                   /id="VAR_007029"
FT   VARIANT         489
FT                   /note="P -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:7814636"
FT                   /id="VAR_007030"
FT   VARIANT         493
FT                   /note="G -> E (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117,
FT                   ECO:0000269|PubMed:24456027"
FT                   /id="VAR_027383"
FT   VARIANT         493
FT                   /note="G -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:24456027"
FT                   /id="VAR_071704"
FT   VARIANT         497
FT                   /note="D -> G (in HAE; dbSNP:rs281875178)"
FT                   /evidence="ECO:0000269|PubMed:22994404"
FT                   /id="VAR_068844"
FT   VARIANT         498
FT                   /note="P -> R (in HAE; phenotype consistent with hereditary
FT                   angioedema type 1)"
FT                   /evidence="ECO:0000269|PubMed:14635117"
FT                   /id="VAR_027384"
FT   VARIANT         498
FT                   /note="P -> S (in HAE; phenotype consistent with hereditary
FT                   angioedema type 2)"
FT                   /evidence="ECO:0000269|PubMed:7814636"
FT                   /id="VAR_007031"
FT   CONFLICT        103
FT                   /note="T -> S (in Ref. 6; BAF85743)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="E -> Q (in Ref. 2; AAB59387)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="K -> R (in Ref. 1; AAA35613)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314..320
FT                   /note="HFKNSVI -> QLQKLSY (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="V -> M (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="V -> L (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370..375
FT                   /note="MEQALS -> TGTGSQ (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        417
FT                   /note="E -> V (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="S -> F (in Ref. 19; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           132..137
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           139..160
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           171..182
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           187..197
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           206..212
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          218..226
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           234..244
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           255..269
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          287..295
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          309..315
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          318..337
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   TURN            338..341
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          342..350
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          353..362
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           367..373
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           376..387
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          392..399
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          401..408
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           409..415
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          417..419
FT                   /evidence="ECO:0007829|PDB:2OAY"
FT   TURN            420..422
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   TURN            428..430
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          440..449
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   HELIX           458..461
FT                   /evidence="ECO:0007829|PDB:5DUQ"
FT   STRAND          469..472
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          477..483
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   TURN            484..487
FT                   /evidence="ECO:0007829|PDB:5DU3"
FT   STRAND          488..496
FT                   /evidence="ECO:0007829|PDB:5DU3"
SQ   SEQUENCE   500 AA;  55154 MW;  8B5E874833EA6C05 CRC64;
     MASRLTLLTL LLLLLAGDRA SSNPNATSSS SQDPESLQDR GEGKVATTVI SKMLFVEPIL
     EVSSLPTTNS TTNSATKITA NTTDEPTTQP TTEPTTQPTI QPTQPTTQLP TDSPTQPTTG
     SFCPGPVTLC SDLESHSTEA VLGDALVDFS LKLYHAFSAM KKVETNMAFS PFSIASLLTQ
     VLLGAGENTK TNLESILSYP KDFTCVHQAL KGFTTKGVTS VSQIFHSPDL AIRDTFVNAS
     RTLYSSSPRV LSNNSDANLE LINTWVAKNT NNKISRLLDS LPSDTRLVLL NAIYLSAKWK
     TTFDPKKTRM EPFHFKNSVI KVPMMNSKKY PVAHFIDQTL KAKVGQLQLS HNLSLVILVP
     QNLKHRLEDM EQALSPSVFK AIMEKLEMSK FQPTLLTLPR IKVTTSQDML SIMEKLEFFD
     FSYDLNLCGL TEDPDLQVSA MQHQTVLELT ETGVEAAAAS AISVARTLLV FEVQQPFLFV
     LWDQQHKFPV FMGRVYDPRA
//
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