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Database: UniProt
Entry: P04070
LinkDB: P04070
Original site: P04070 
ID   PROC_HUMAN              Reviewed;         461 AA.
AC   P04070; B4DPQ7; Q15189; Q15190; Q16001; Q53S74; Q9UC55;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-SEP-2014, entry version 197.
DE   RecName: Full=Vitamin K-dependent protein C;
DE            EC=3.4.21.69;
DE   AltName: Full=Anticoagulant protein C;
DE   AltName: Full=Autoprothrombin IIA;
DE   AltName: Full=Blood coagulation factor XIV;
DE   Contains:
DE     RecName: Full=Vitamin K-dependent protein C light chain;
DE   Contains:
DE     RecName: Full=Vitamin K-dependent protein C heavy chain;
DE   Contains:
DE     RecName: Full=Activation peptide;
DE   Flags: Precursor;
GN   Name=PROC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2991859; DOI=10.1093/nar/13.14.5233;
RA   Beckmann R.J., Schmidt R.J., Santerre R.F., Plutzky J., Crabtree G.R.,
RA   Long G.L.;
RT   "The structure and evolution of a 461 amino acid human protein C
RT   precursor and its messenger RNA, based upon the DNA sequence of cloned
RT   human liver cDNAs.";
RL   Nucleic Acids Res. 13:5233-5247(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], HYDROXYLATION AT ASP-113,
RP   GLYCOSYLATION AT ASN-290; ASN-355 AND ASN-371, AND
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-48; GLU-49; GLU-56; GLU-58; GLU-61;
RP   GLU-62; GLU-67; GLU-68 AND GLU-71.
RX   PubMed=2991887; DOI=10.1073/pnas.82.14.4673;
RA   Foster D.C., Yoshitake S., Davie E.W.;
RT   "The nucleotide sequence of the gene for human protein C.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4673-4677(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3511471; DOI=10.1073/pnas.83.3.546;
RA   Plutzky J., Hoskins J.A., Long G.L., Crabtree G.R.;
RT   "Evolution and organization of the human protein C gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:546-550(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 42-57, AND VARIANT THPH3 SER-42.
RC   TISSUE=Blood;
RX   PubMed=8560401;
RA   Miyata T., Zheng Y.-Z., Sakata T., Kato H.;
RT   "Protein C Osaka 10 with aberrant propeptide processing: loss of
RT   anticoagulant activity due to an amino acid substitution in the
RT   protein C precursor.";
RL   Thromb. Haemost. 74:1003-1008(1995).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-64, AND VARIANT PROC
RP   DEFICIENCY GLY-57.
RX   PubMed=8477066;
RA   Mimuro J., Muramatsu S., Kaneko M., Yoshitake S., Iijima K.,
RA   Nakamura K., Sakata Y., Matsuda M.;
RT   "An abnormal protein C (protein C Yonago) with an amino acid
RT   substitution of Gly for Arg-15 caused by a single base mutation of C
RT   to G in codon 57 (CGG-->GGG). Deteriorated calcium-dependent
RT   conformation of the gamma-carboxyglutamic acid domain relevant to a
RT   thrombotic tendency.";
RL   Int. J. Hematol. 57:9-14(1993).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 106-461 (ISOFORM 1).
RX   PubMed=6589623; DOI=10.1073/pnas.81.15.4766;
RA   Foster D.C., Davie E.W.;
RT   "Characterization of a cDNA coding for human protein C.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4766-4770(1984).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-178 AND 267-332, AND VARIANTS
RP   THPH4 PRO-178 AND HIS-328.
RX   PubMed=7878626;
RA   Long G.L., Tomczak J.A., Rainville I.R., Dreyfus M., Schramm W.,
RA   Schwarz H.P.;
RT   "Homozygous type I protein C deficiency in two unrelated families
RT   exhibiting thrombophilia related to Ala136-->Pro or Arg286-->His
RT   mutations.";
RL   Thromb. Haemost. 72:526-533(1994).
RN   [13]
RP   GLYCOSYLATION AT ASN-371.
RX   PubMed=1694179;
RA   Miletich J.P., Broze G.J. Jr.;
RT   "Beta protein C is not glycosylated at asparagine 329. The rate of
RT   translation may influence the frequency of usage at asparagine-X-
RT   cysteine sites.";
RL   J. Biol. Chem. 265:11397-11404(1990).
RN   [14]
RP   HYDROXYLATION.
RX   PubMed=1544894;
RA   Harris R.J., Ling V.T., Spellman M.W.;
RT   "O-linked fucose is present in the first epidermal growth factor
RT   domain of factor XII but not protein C.";
RL   J. Biol. Chem. 267:5102-5107(1992).
RN   [15]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-290.
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.,
RA   Moore R.J., 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   [16]
RP   GLYCOSYLATION AT THR-19, 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
RT   N-and O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [17]
RP   3D-STRUCTURE MODELING OF 175-450.
RX   PubMed=8003977; DOI=10.1002/pro.5560030407;
RA   Fisher C.L., Greengard J.S., Griffin J.H.;
RT   "Models of the serine protease domain of the human antithrombotic
RT   plasma factor activated protein C and its zymogen.";
RL   Protein Sci. 3:588-599(1994).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 84-461.
RX   PubMed=9003757;
RA   Mather T., Oganessyan V., Hof P., Huber R., Foundling S., Esmon C.,
RA   Bode W.;
RT   "The 2.8 A crystal structure of Gla-domainless activated protein C.";
RL   EMBO J. 15:6822-6831(1996).
RN   [19]
RP   REVIEW ON PROC VARIANTS.
RX   PubMed=8446940;
RA   Reitsma P.H., Poort S.R., Bernardi F., Gandrille S., Long G.L.,
RA   Sala N., Cooper D.N.;
RT   "Protein C deficiency: a database of mutations.";
RL   Thromb. Haemost. 69:77-84(1993).
RN   [20]
RP   VARIANT THPH3 CYS-444.
RX   PubMed=2437584; DOI=10.1073/pnas.84.9.2829;
RA   Romeo G., Hassan H.J., Staempfli S., Roncuzzi L., Cianetti L.,
RA   Leonardi A., Vicente V., Mannucci P.M., Bertina R.M., Peschle C.,
RA   Cortese R.;
RT   "Hereditary thrombophilia: identification of nonsense and missense
RT   mutations in the protein C gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:2829-2832(1987).
RN   [21]
RP   VARIANT THPH3 TRP-211.
RX   PubMed=2602169; DOI=10.1093/nar/17.24.10513;
RA   Grundy C.B., Chitolie A., Talbot S., Bevan D., Kakkar V.V.,
RA   Cooper D.N.;
RT   "Protein C London 1: recurrent mutation at Arg-169 (CGG-->TGG) in the
RT   protein C gene causing thrombosis.";
RL   Nucleic Acids Res. 17:10513-10513(1989).
RN   [22]
RP   VARIANT THPH3 CYS-272.
RX   PubMed=1868249;
RA   Reitsma P.H., Poort S.R., Allaart C.F., Briet E., Bertina R.M.;
RT   "The spectrum of genetic defects in a panel of 40 Dutch families with
RT   symptomatic protein C deficiency type I: heterogeneity and founder
RT   effects.";
RL   Blood 78:890-894(1991).
RN   [23]
RP   VARIANTS THPH3 ALA-62 AND MET-76.
RX   PubMed=1347706;
RA   Bovill E.G., Tomczak J.A., Grant B., Bhushan F., Pillemer E.,
RA   Rainville I.R., Long G.L.;
RT   "Protein CVermont: symptomatic type II protein C deficiency associated
RT   with two GLA domain mutations.";
RL   Blood 79:1456-1465(1992).
RN   [24]
RP   VARIANT THPH4 ASP-418.
RX   PubMed=1611081;
RA   Sugahara Y., Miura O., Yuen P., Aoki N.;
RT   "Protein C deficiency Hong Kong 1 and 2: hereditary protein C
RT   deficiency caused by two mutant alleles, a 5-nucleotide deletion and a
RT   missense mutation.";
RL   Blood 80:126-133(1992).
RN   [25]
RP   VARIANT THPH4 LEU-289.
RX   PubMed=1511988;
RA   Grundy C.B., Chisholm M., Kakkar V.V., Cooper D.N.;
RT   "A novel homozygous missense mutation in the protein C (PROC) gene
RT   causing recurrent venous thrombosis.";
RL   Hum. Genet. 89:683-684(1992).
RN   [26]
RP   VARIANTS THPH3 GLN-220 AND TRP-220.
RX   PubMed=1511989;
RA   Grundy C.B., Schulman S., Tengborn L., Kakkar V.V., Cooper D.N.;
RT   "Two different missense mutations at Arg 178 of the protein C (PROC)
RT   gene causing recurrent venous thrombosis.";
RL   Hum. Genet. 89:685-686(1992).
RN   [27]
RP   VARIANT THPH3 GLN-220.
RX   PubMed=1301959; DOI=10.1002/humu.1380010607;
RA   Gandrille S., Vidaud M., Aiach M., Alhenc-Gelas M., Fischer A.M.,
RA   Gouault-Heilman M., Toulon P., Fiessinger J.-N., Goossens M.;
RT   "Two novel mutations responsible for hereditary type I protein C
RT   deficiency: characterization by denaturing gradient gel
RT   electrophoresis.";
RL   Hum. Mutat. 1:491-500(1992).
RN   [28]
RP   VARIANT THPH4 SER-334.
RX   PubMed=1593215;
RA   Yamamoto K., Matsushita T., Sugiura I., Takamatsu J., Iwasaki E.,
RA   Wada H., Deguchi K., Shirakawa S., Saito H.;
RT   "Homozygous protein C deficiency: identification of a novel missense
RT   mutation that causes impaired secretion of the mutant protein C.";
RL   J. Lab. Clin. Med. 119:682-689(1992).
RN   [29]
RP   VARIANTS TRP-38; CYS-42; HIS-42; GLN-271 AND ASN-294.
RX   PubMed=8324221;
RA   Gandrille S., Alhenc-Gelas M., Gaussem P., Aillaud M.-F., Dupuy E.,
RA   Juhan-Vague I., Aiach M.;
RT   "Five novel mutations located in exons III and IX of the protein C
RT   gene in patients presenting with defective protein C anticoagulant
RT   activity.";
RL   Blood 82:159-168(1993).
RN   [30]
RP   VARIANTS GLY-14; GLN-211; TYR-244; GLN-253; LEU-321; CYS-328; ILE-385;
RP   THR-388 AND VAL-388.
RX   PubMed=8499565;
RA   Poort S.R., Pabinger-Fasching I., Mannhalter C., Reitsma P.H.,
RA   Bertina R.M.;
RT   "Twelve novel and two recurrent mutations in 14 Austrian families with
RT   hereditary protein C deficiency.";
RL   Blood Coagul. Fibrinolysis 4:273-280(1993).
RN   [31]
RP   VARIANT THPH3 TRP-57.
RX   PubMed=8499568;
RA   Millar D.S., Grundy C.B., Bignell P., Moffat E.H., Martin R.,
RA   Kakkar V.V., Cooper D.N.;
RT   "A Gla domain mutation (Arg 15-->Trp) in the protein C (PROC) gene
RT   causing type 2 protein C deficiency and recurrent venous thrombosis.";
RL   Blood Coagul. Fibrinolysis 4:345-347(1993).
RN   [32]
RP   VARIANTS THPH3 ARG-145; LEU-210; TRP-211; THR-243; LEU-321; MET-340
RP   AND TYR-426.
RX   PubMed=8292730;
RA   Tsay W., Greengard J.S., Montgomery R.R., McPherson R.A., Fucci J.C.,
RA   Koerper M.A., Coughlin J., Griffin J.H.;
RT   "Genetic mutations in ten unrelated American patients with symptomatic
RT   type 1 protein C deficiency.";
RL   Blood Coagul. Fibrinolysis 4:791-796(1993).
RN   [33]
RP   VARIANT THPH3 SER-423.
RX   PubMed=8398832; DOI=10.1111/j.1365-2141.1993.tb03066.x;
RA   Marchetti G., Patracchini P., Gemmati D., Castaman G., Rodeghiero F.,
RA   Wacey A., Cooper D.N., Tuddenham E.G., Bernardi F.;
RT   "Symptomatic type II protein C deficiency caused by a missense
RT   mutation (Gly 381-->Ser) in the substrate-binding pocket.";
RL   Br. J. Haematol. 84:285-289(1993).
RN   [34]
RP   VARIANT PRO-312.
RX   PubMed=7919373;
RA   Gandrille S., Jude B., Alhenc-Gelas M., Emmerich J., Aiach M.;
RT   "First de novo mutations in the protein C gene of two patients with
RT   type I deficiency: a missense mutation and a splice site deletion.";
RL   Blood 84:2566-2570(1994).
RN   [35]
RP   VARIANT THPH4 144-ASN-GLY-145 DELINS LYS.
RX   PubMed=7841323;
RA   Millar D.S., Allgrove J., Rodeck C., Kakkar V.V., Cooper D.N.;
RT   "A homozygous deletion/insertion mutation in the protein C (PROC) gene
RT   causing neonatal Purpura fulminans: prenatal diagnosis in an at-risk
RT   pregnancy.";
RL   Blood Coagul. Fibrinolysis 5:647-649(1994).
RN   [36]
RP   VARIANT THPH4 ALA-367.
RX   PubMed=7841324;
RA   Witt I., Beck S., Seydewitz H.H., Tasangil C., Schenck W.;
RT   "A novel homozygous missense mutation (Val 325-->Ala) in the protein C
RT   gene causing neonatal purpura fulminans.";
RL   Blood Coagul. Fibrinolysis 5:651-653(1994).
RN   [37]
RP   VARIANTS THPH3 LEU-369; ARG-392; ASN-401 AND HIS-441.
RX   PubMed=7865674;
RA   Zheng Y.-Z., Sakata T., Matsusue T., Umeyama H., Kato H., Miyata T.;
RT   "Six missense mutations associated with type I and type II protein C
RT   deficiency and implications obtained from molecular modelling.";
RL   Blood Coagul. Fibrinolysis 5:687-696(1994).
RN   [38]
RP   VARIANT ASP-49.
RX   PubMed=7974343;
RA   Gaussem P., Gandrille S., Duchemin J., Emmerich J., Alhenc-Gelas M.,
RA   Aillaud M.-F., Aiach M.;
RT   "Influence of six mutations of the protein C gene on the Gla domain
RT   conformation and calcium affinity.";
RL   Thromb. Haemost. 71:748-754(1994).
RN   [39]
RP   VARIANTS CYS-89; PRO-220 AND THR-301.
RX   PubMed=7605880;
RA   Millar D.S., Bevan D., Chitolie A., Reynaud J., Chisholm M.,
RA   Kakkar V.V., Cooper D.N.;
RT   "Three novel mutations in the protein C (PROC) gene causing venous
RT   thrombosis.";
RL   Blood Coagul. Fibrinolysis 6:138-140(1995).
RN   [40]
RP   VARIANTS THPH3 TRP-57; ARG-114; ARG-324; CYS-328 AND LEU-369, AND
RP   VARIANT THR-43.
RX   PubMed=7792728;
RA   Lind B., Schwartz M., Thorsen S.;
RT   "Six different point mutations in seven Danish families with
RT   symptomatic protein C deficiency.";
RL   Thromb. Haemost. 73:186-193(1995).
RN   [41]
RP   VARIANTS THPH3 CYS-32 AND ASN-436.
RX   PubMed=8829639;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:2<176::AID-HUMU16>3.3.CO;2-W;
RA   Ireland H.A., Boisclair M.D., Taylor J., Thompson E., Thein S.L.,
RA   Girolami A., de Caterina M., Scopacasa F., de Stefano V., Leone G.,
RA   Finazzi G., Cohen H., Lane D.A.;
RT   "Two novel (R(-11)C; T394D) and two repeat missense mutations in the
RT   protein C gene associated with venous thrombosis in six kindreds.";
RL   Hum. Mutat. 7:176-179(1996).
RN   [42]
RP   VARIANTS THPH3 GLN-220 AND MET-340.
RX   PubMed=9798967;
RA   Couture P., Demers C., Morissette J., Delage R., Jomphe M.,
RA   Couture L., Simard J.;
RT   "Type I protein C deficiency in French Canadians: evidence of a
RT   founder effect and association of specific protein C gene mutations
RT   with plasma protein C levels.";
RL   Thromb. Haemost. 80:551-556(1998).
CC   -!- FUNCTION: Protein C is a vitamin K-dependent serine protease that
CC       regulates blood coagulation by inactivating factors Va and VIIIa
CC       in the presence of calcium ions and phospholipids.
CC   -!- CATALYTIC ACTIVITY: Degradation of blood coagulation factors Va
CC       and VIIIa.
CC   -!- SUBUNIT: Synthesized as a single chain precursor, which is cleaved
CC       into a light chain and a heavy chain held together by a disulfide
CC       bond. The enzyme is then activated by thrombin, which cleaves a
CC       tetradecapeptide from the amino end of the heavy chain; this
CC       reaction, which occurs at the surface of endothelial cells, is
CC       strongly promoted by thrombomodulin.
CC   -!- INTERACTION:
CC       P51511:MMP15; NbExp=2; IntAct=EBI-1383018, EBI-1383043;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P04070-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P04070-2; Sequence=VSP_054393, VSP_054394;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu
CC       residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-
CC       371 with an atypical N-X-C site produces a higher molecular weight
CC       form referred to as alpha. The lower molecular weight form, not N-
CC       glycosylated at Asn-371, is beta. O-glycosylated with core 1 or
CC       possibly core 8 glycans.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- PTM: May be phosphorylated on a Ser or Thr in a region (AA 25-30)
CC       of the propeptide.
CC   -!- DISEASE: Thrombophilia due to protein C deficiency, autosomal
CC       dominant (THPH3) [MIM:176860]: A hemostatic disorder characterized
CC       by impaired regulation of blood coagulation and a tendency to
CC       recurrent venous thrombosis. Individuals with decreased amounts of
CC       protein C are classically referred to as having type I protein C
CC       deficiency and those with normal amounts of a functionally
CC       defective protein as having type II deficiency. Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Thrombophilia due to protein C deficiency, autosomal
CC       recessive (THPH4) [MIM:612304]: A hemostatic disorder
CC       characterized by impaired regulation of blood coagulation and a
CC       tendency to recurrent venous thrombosis. It results in a
CC       thrombotic condition that can manifest as a severe neonatal
CC       disorder or as a milder disorder with late-onset thrombophilia.
CC       The severe form leads to neonatal death through massive neonatal
CC       venous thrombosis. Often associated with ecchymotic skin lesions
CC       which can turn necrotic called purpura fulminans, this disorder is
CC       very rare. Note=The disease is caused by mutations affecting the
CC       gene represented in this entry.
CC   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to
CC       another site, beyond the GLA domain. This GLA-independent binding
CC       site is necessary for the recognition of the thrombin-
CC       thrombomodulin complex.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=S76088; Type=Erroneous termination; Positions=151; Note=Translated as Cys;
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Protein C entry;
CC       URL="http://en.wikipedia.org/wiki/Protein_C";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/proc/";
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DR   EMBL; X02750; CAA26528.1; -; mRNA.
DR   EMBL; M11228; AAA60166.1; -; Genomic_DNA.
DR   EMBL; M12712; AAA60165.1; -; Genomic_DNA.
DR   EMBL; M12683; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12684; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12685; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12686; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; M12687; AAA60165.1; JOINED; Genomic_DNA.
DR   EMBL; AF378903; AAK56377.1; -; Genomic_DNA.
DR   EMBL; AK298454; BAG60669.1; -; mRNA.
DR   EMBL; AC068282; AAY15044.1; -; Genomic_DNA.
DR   EMBL; CH471103; EAW95320.1; -; Genomic_DNA.
DR   EMBL; BC034377; AAH34377.1; -; mRNA.
DR   EMBL; S58668; AAB26335.1; -; Genomic_DNA.
DR   EMBL; K02059; AAA60164.1; -; mRNA.
DR   EMBL; S76088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S76090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS2145.1; -. [P04070-1]
DR   PIR; A22331; KXHU.
DR   RefSeq; NP_000303.1; NM_000312.3. [P04070-1]
DR   RefSeq; XP_005263773.1; XM_005263716.2. [P04070-2]
DR   UniGene; Hs.224698; -.
DR   PDB; 1AUT; X-ray; 2.80 A; C=212-461, L=84-197.
DR   PDB; 1LQV; X-ray; 1.60 A; C/D=43-75.
DR   PDB; 1PCU; Model; -; A=175-450.
DR   PDB; 2PCT; Model; -; A=175-450.
DR   PDB; 3F6U; X-ray; 2.80 A; H=212-451, L=91-188.
DR   PDB; 3JTC; X-ray; 1.60 A; C/D=43-75.
DR   PDB; 4DT7; X-ray; 1.90 A; E/F=204-223.
DR   PDBsum; 1AUT; -.
DR   PDBsum; 1LQV; -.
DR   PDBsum; 1PCU; -.
DR   PDBsum; 2PCT; -.
DR   PDBsum; 3F6U; -.
DR   PDBsum; 3JTC; -.
DR   PDBsum; 4DT7; -.
DR   ProteinModelPortal; P04070; -.
DR   SMR; P04070; 43-451.
DR   BioGrid; 111608; 5.
DR   IntAct; P04070; 3.
DR   MINT; MINT-8247437; -.
DR   STRING; 9606.ENSP00000234071; -.
DR   BindingDB; P04070; -.
DR   ChEMBL; CHEMBL4444; -.
DR   DrugBank; DB00025; Antihemophilic Factor.
DR   DrugBank; DB00055; Drotrecogin alfa.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB00464; Sodium Tetradecyl Sulfate.
DR   MEROPS; S01.218; -.
DR   PhosphoSite; P04070; -.
DR   UniCarbKB; P04070; -.
DR   DMDM; 131067; -.
DR   MaxQB; P04070; -.
DR   PaxDb; P04070; -.
DR   PeptideAtlas; P04070; -.
DR   PRIDE; P04070; -.
DR   DNASU; 5624; -.
DR   Ensembl; ENST00000234071; ENSP00000234071; ENSG00000115718.
DR   Ensembl; ENST00000422777; ENSP00000409543; ENSG00000115718.
DR   Ensembl; ENST00000453608; ENSP00000404030; ENSG00000115718.
DR   GeneID; 5624; -.
DR   KEGG; hsa:5624; -.
DR   UCSC; uc002tok.3; human. [P04070-1]
DR   CTD; 5624; -.
DR   GeneCards; GC02P128176; -.
DR   HGNC; HGNC:9451; PROC.
DR   HPA; CAB016721; -.
DR   HPA; CAB016792; -.
DR   HPA; HPA005550; -.
DR   MIM; 176860; phenotype.
DR   MIM; 612283; gene.
DR   MIM; 612304; phenotype.
DR   neXtProt; NX_P04070; -.
DR   Orphanet; 745; Hereditary thrombophilia due to congenital protein C deficiency.
DR   PharmGKB; PA33799; -.
DR   eggNOG; COG5640; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01344; -.
DR   PhylomeDB; P04070; -.
DR   TreeFam; TF327329; -.
DR   Reactome; REACT_1050; Gamma-carboxylation of protein precursors.
DR   Reactome; REACT_12051; Cell surface interactions at the vascular wall.
DR   Reactome; REACT_1439; Common Pathway.
DR   Reactome; REACT_1906; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; REACT_733; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   EvolutionaryTrace; P04070; -.
DR   GeneWiki; Protein_C; -.
DR   GenomeRNAi; 5624; -.
DR   NextBio; 21860; -.
DR   PMAP-CutDB; P04070; -.
DR   PRO; PR:P04070; -.
DR   ArrayExpress; P04070; -.
DR   Bgee; P04070; -.
DR   CleanEx; HS_PROC; -.
DR   Genevestigator; P04070; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; TAS:UniProtKB.
DR   GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR018114; Peptidase_S1_AS.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW   Hydrolase; Hydroxylation; Polymorphism; Protease; Reference proteome;
KW   Repeat; Serine protease; Signal; Thrombophilia; Zymogen.
FT   SIGNAL        1     18       Potential.
FT   PROPEP       19     42
FT                                /FTId=PRO_0000028107.
FT   CHAIN        43    461       Vitamin K-dependent protein C.
FT                                /FTId=PRO_0000028108.
FT   CHAIN        43    197       Vitamin K-dependent protein C light
FT                                chain.
FT                                /FTId=PRO_0000028109.
FT   CHAIN       200    461       Vitamin K-dependent protein C heavy
FT                                chain.
FT                                /FTId=PRO_0000028110.
FT   PEPTIDE     200    211       Activation peptide.
FT                                /FTId=PRO_0000028111.
FT   DOMAIN       43     88       Gla.
FT   DOMAIN       97    132       EGF-like 1.
FT   DOMAIN      136    176       EGF-like 2.
FT   DOMAIN      212    450       Peptidase S1.
FT   ACT_SITE    253    253       Charge relay system.
FT   ACT_SITE    299    299       Charge relay system.
FT   ACT_SITE    402    402       Charge relay system.
FT   SITE        211    212       Cleavage; by thrombin.
FT   MOD_RES      48     48       4-carboxyglutamate.
FT   MOD_RES      49     49       4-carboxyglutamate.
FT   MOD_RES      56     56       4-carboxyglutamate.
FT   MOD_RES      58     58       4-carboxyglutamate.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT   MOD_RES      62     62       4-carboxyglutamate.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT   MOD_RES      68     68       4-carboxyglutamate.
FT   MOD_RES      71     71       4-carboxyglutamate.
FT   MOD_RES     113    113       (3R)-3-hydroxyaspartate.
FT   CARBOHYD     19     19       O-linked (GalNAc...).
FT   CARBOHYD    139    139       N-linked (GlcNAc...).
FT   CARBOHYD    290    290       N-linked (GlcNAc...).
FT   CARBOHYD    355    355       N-linked (GlcNAc...).
FT   CARBOHYD    371    371       N-linked (GlcNAc...); partial; atypical.
FT   DISULFID     59     64
FT   DISULFID     92    111
FT   DISULFID    101    106
FT   DISULFID    105    120
FT   DISULFID    122    131
FT   DISULFID    140    151
FT   DISULFID    147    160
FT   DISULFID    162    175
FT   DISULFID    183    319       Interchain (between light and heavy
FT                                chains).
FT   DISULFID    238    254
FT   DISULFID    373    387
FT   DISULFID    398    426
FT   VAR_SEQ       1      1       M -> MAAGRRTCSISTTRPCASASRM (in isoform
FT                                2).
FT                                /FTId=VSP_054393.
FT   VAR_SEQ     133    133       R -> RGEGERWMLAGGGAGLGPGWGRGTSTSCPRPPLPA
FT                                (in isoform 2).
FT                                /FTId=VSP_054394.
FT   VARIANT      14     14       W -> G (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006634.
FT   VARIANT      32     32       R -> C (in THPH3).
FT                                /FTId=VAR_006635.
FT   VARIANT      38     38       R -> W (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006636.
FT   VARIANT      42     42       R -> C (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006638.
FT   VARIANT      42     42       R -> H (in Malakoff; low anticoagulant
FT                                activity).
FT                                /FTId=VAR_006637.
FT   VARIANT      42     42       R -> S (in THPH3; type II; Osaka-10;
FT                                alters proteolytic processing so that S-
FT                                42 is the N-terminus of the mature
FT                                protein).
FT                                /FTId=VAR_055074.
FT   VARIANT      43     43       A -> T.
FT                                /FTId=VAR_006639.
FT   VARIANT      49     49       E -> D (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006640.
FT   VARIANT      51     51       R -> C (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006641.
FT   VARIANT      57     57       R -> G (in Yonago; defective
FT                                anticoagulant activity).
FT                                /FTId=VAR_006643.
FT   VARIANT      57     57       R -> Q (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006644.
FT   VARIANT      57     57       R -> W (in THPH3).
FT                                /FTId=VAR_006642.
FT   VARIANT      62     62       E -> A (in THPH3; Vermont-1).
FT                                /FTId=VAR_006645.
FT   VARIANT      76     76       V -> M (in THPH3; Vermont-1).
FT                                /FTId=VAR_006646.
FT   VARIANT      89     89       G -> C (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006647.
FT   VARIANT     108    108       H -> N (in patients with PROC deficiency;
FT                                La Jolla-1).
FT                                /FTId=VAR_006648.
FT   VARIANT     109    109       G -> R (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006649.
FT   VARIANT     114    118       Missing (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006650.
FT   VARIANT     114    114       G -> R (in THPH3).
FT                                /FTId=VAR_006651.
FT   VARIANT     118    118       F -> L (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006652.
FT   VARIANT     119    124       Missing (in patients with PROC
FT                                deficiency; St Louis-2).
FT                                /FTId=VAR_006653.
FT   VARIANT     120    125       Missing (in patients with PROC
FT                                deficiency; St Louis-3).
FT                                /FTId=VAR_006654.
FT   VARIANT     144    145       NG -> K (in THPH4; neonatal purpura
FT                                fulminans).
FT                                /FTId=VAR_006655.
FT   VARIANT     145    145       G -> R (in THPH3).
FT                                /FTId=VAR_006656.
FT   VARIANT     147    147       C -> Y (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006657.
FT   VARIANT     149    149       H -> P (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006658.
FT   VARIANT     161    161       S -> R (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006659.
FT   VARIANT     178    178       A -> P (in THPH4; Clamart).
FT                                /FTId=VAR_006660.
FT   VARIANT     183    183       C -> R (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006661.
FT   VARIANT     189    189       R -> W (in patients with PROC deficiency;
FT                                La Jolla-3; dbSNP:rs146922325).
FT                                /FTId=VAR_006662.
FT   VARIANT     194    194       R -> C (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006663.
FT   VARIANT     210    210       P -> L (in THPH3).
FT                                /FTId=VAR_006664.
FT   VARIANT     211    211       R -> Q (in patients with PROC deficiency;
FT                                dbSNP:rs28933987).
FT                                /FTId=VAR_006666.
FT   VARIANT     211    211       R -> W (in THPH3; London-1/Tochigi;
FT                                dbSNP:rs28933986).
FT                                /FTId=VAR_006665.
FT   VARIANT     220    220       R -> P (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006667.
FT   VARIANT     220    220       R -> Q (in THPH3; Vermont-3).
FT                                /FTId=VAR_006669.
FT   VARIANT     220    220       R -> W (in THPH3).
FT                                /FTId=VAR_006668.
FT   VARIANT     226    226       Q -> H (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006670.
FT   VARIANT     243    243       I -> T (in THPH3).
FT                                /FTId=VAR_006671.
FT   VARIANT     244    244       H -> Y (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006672.
FT   VARIANT     253    253       H -> Q (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006673.
FT   VARIANT     265    265       L -> F (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006674.
FT   VARIANT     271    271       R -> Q (in Marseille; low anticoagulant
FT                                activity).
FT                                /FTId=VAR_006675.
FT   VARIANT     271    271       R -> W (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006676.
FT   VARIANT     272    272       R -> C (in THPH3).
FT                                /FTId=VAR_006677.
FT   VARIANT     281    281       D -> DLD (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006678.
FT   VARIANT     289    289       P -> L (in THPH4).
FT                                /FTId=VAR_006679.
FT   VARIANT     294    294       S -> N (in Paris; low anticoagulant
FT                                activity).
FT                                /FTId=VAR_006680.
FT   VARIANT     298    298       N -> D (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006681.
FT   VARIANT     301    301       A -> T (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006682.
FT   VARIANT     301    301       A -> V (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006683.
FT   VARIANT     309    309       A -> T (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006684.
FT   VARIANT     312    312       S -> L (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006685.
FT   VARIANT     312    312       S -> P (in a patient with PROC
FT                                deficiency; sporadic case).
FT                                /FTId=VAR_006686.
FT   VARIANT     321    321       P -> L (in THPH3).
FT                                /FTId=VAR_006687.
FT   VARIANT     324    324       G -> R (in THPH3).
FT                                /FTId=VAR_006688.
FT   VARIANT     328    328       R -> C (in THPH3).
FT                                /FTId=VAR_006689.
FT   VARIANT     328    328       R -> H (in THPH4; Muenchen).
FT                                /FTId=VAR_006690.
FT   VARIANT     334    334       G -> S (in THPH4).
FT                                /FTId=VAR_006691.
FT   VARIANT     340    340       T -> M (in THPH3; Vermont-2).
FT                                /FTId=VAR_006692.
FT   VARIANT     343    343       G -> D (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006693.
FT   VARIANT     363    363       Missing (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006694.
FT   VARIANT     367    367       V -> A (in THPH4; neonatal purpura
FT                                fulminans).
FT                                /FTId=VAR_006695.
FT   VARIANT     369    369       P -> L (in THPH3; Osaka-6).
FT                                /FTId=VAR_006696.
FT   VARIANT     385    385       M -> I (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006697.
FT   VARIANT     388    388       A -> T (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006698.
FT   VARIANT     388    388       A -> V (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006699.
FT   VARIANT     392    392       G -> R (in THPH3; Osaka-9).
FT                                /FTId=VAR_006700.
FT   VARIANT     394    394       R -> W (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006701.
FT   VARIANT     401    401       D -> N (in THPH3; La Jolla-2/Osaka-7 and
FT                                -8).
FT                                /FTId=VAR_006702.
FT   VARIANT     418    418       G -> D (in THPH4; Hong Kong-2).
FT                                /FTId=VAR_006703.
FT   VARIANT     423    423       G -> S (in THPH3).
FT                                /FTId=VAR_006704.
FT   VARIANT     426    426       C -> Y (in THPH3).
FT                                /FTId=VAR_006705.
FT   VARIANT     433    433       G -> S (in patients with PROC deficiency;
FT                                Purmerend).
FT                                /FTId=VAR_006706.
FT   VARIANT     436    436       T -> N (in THPH3).
FT                                /FTId=VAR_006707.
FT   VARIANT     441    441       Y -> H (in THPH3; Osaka-4).
FT                                /FTId=VAR_006708.
FT   VARIANT     444    444       W -> C (in THPH3).
FT                                /FTId=VAR_006709.
FT   VARIANT     445    445       I -> M (in patients with PROC
FT                                deficiency).
FT                                /FTId=VAR_006710.
FT   CONFLICT    106    106       C -> Q (in Ref. 11; AAA60164).
FT   CONFLICT    445    445       I -> IL (in Ref. 3; AAA60165).
FT   HELIX        48     50
FT   HELIX        55     59
FT   HELIX        66     73
FT   STRAND      100    103
FT   TURN        104    107
FT   STRAND      108    111
FT   STRAND      120    122
FT   STRAND      126    128
FT   STRAND      137    142
FT   HELIX       143    146
FT   STRAND      148    153
FT   STRAND      155    161
FT   STRAND      166    168
FT   STRAND      175    177
FT   STRAND      179    181
FT   STRAND      226    230
FT   STRAND      236    244
FT   STRAND      247    250
FT   HELIX       252    254
FT   STRAND      255    257
FT   STRAND      262    266
FT   STRAND      269    272
FT   STRAND      278    287
FT   TURN        293    296
FT   STRAND      301    307
FT   HELIX       323    328
FT   TURN        329    331
FT   STRAND      336    341
FT   STRAND      357    359
FT   STRAND      361    368
FT   HELIX       370    376
FT   STRAND      385    388
FT   STRAND      405    410
FT   STRAND      413    422
FT   STRAND      424    427
FT   STRAND      433    436
FT   HELIX       438    440
FT   HELIX       442    449
SQ   SEQUENCE   461 AA;  52071 MW;  3531B0AE5345B39A CRC64;
     MWQLTSLLLF VATWGISGTP APLDSVFSSS ERAHQVLRIR KRANSFLEEL RHSSLERECI
     EEICDFEEAK EIFQNVDDTL AFWSKHVDGD QCLVLPLEHP CASLCCGHGT CIDGIGSFSC
     DCRSGWEGRF CQREVSFLNC SLDNGGCTHY CLEEVGWRRC SCAPGYKLGD DLLQCHPAVK
     FPCGRPWKRM EKKRSHLKRD TEDQEDQVDP RLIDGKMTRR GDSPWQVVLL DSKKKLACGA
     VLIHPSWVLT AAHCMDESKK LLVRLGEYDL RRWEKWELDL DIKEVFVHPN YSKSTTDNDI
     ALLHLAQPAT LSQTIVPICL PDSGLAEREL NQAGQETLVT GWGYHSSREK EAKRNRTFVL
     NFIKIPVVPH NECSEVMSNM VSENMLCAGI LGDRQDACEG DSGGPMVASF HGTWFLVGLV
     SWGEGCGLLH NYGVYTKVSR YLDWIHGHIR DKEAPQKSWA P
//
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