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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6091100 [NCBI, ExPASy, EBI, Israel, Japan]
Long G.L.,
Balagaje R.M.,
McGillivray R.T.A.;
"Cloning and sequencing of liver cDNA coding for bovine protein C.";
Proc. Natl. Acad. Sci. U.S.A. 81:5653-5656(1984).
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[2]
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PROTEIN SEQUENCE OF 40-194, AND GLYCOSYLATION AT ASN-136.
PubMed=6896876 [NCBI, ExPASy, EBI, Israel, Japan]
Fernlund P.,
Stenflo J.;
"Amino acid sequence of the light chain of bovine protein C.";
J. Biol. Chem. 257:12170-12179(1982).
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[3]
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SEQUENCE REVISION TO 110.
PubMed=6572939 [NCBI, ExPASy, EBI, Israel, Japan]
Drakenberg T.,
Fernlund P.,
Roepstorff P.,
Stenflo J.;
"Beta-hydroxyaspartic acid in vitamin K-dependent protein C.";
Proc. Natl. Acad. Sci. U.S.A. 80:1802-1806(1983).
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[4]
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PROTEIN SEQUENCE OF 197-456, AND GLYCOSYLATION AT ASN-289; ASN-350 AND ASN-366.
PubMed=6896877 [NCBI, ExPASy, EBI, Israel, Japan]
Stenflo J.,
Fernlund P.;
"Amino acid sequence of the heavy chain of bovine protein C.";
J. Biol. Chem. 257:12180-12190(1982).
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[5]
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PROTEOLYTIC PROCESSING, AND CALCIUM-BINDING DATA.
PubMed=6304092 [NCBI, ExPASy, EBI, Israel, Japan]
Esmon N.L.,
Debault L.E.,
Esmon C.T.;
"Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C.";
J. Biol. Chem. 258:5548-5553(1983).
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[6]
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PROTEOLYTIC PROCESSING, AND CALCIUM-BINDING DATA.
PubMed=6406503 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson A.E.,
Esmon N.L.,
Laue T.M.,
Esmon C.T.;
"Structural changes required for activation of protein C are induced by Ca2+ binding to a high affinity site that does not contain gamma-carboxyglutamic acid.";
J. Biol. Chem. 258:5554-5560(1983).
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- FUNCTION: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids.
- CATALYTIC ACTIVITY: Degradation of blood coagulation factors Va and VIIIa.
- SUBUNIT: Synthesized as a single chain precursor, which is cleaved into a light chain and a heavy chain held together by a disulfide bond. The enzyme is then activated by thrombin, which cleaves a tetradecapeptide from the amino end of the heavy chain; this reaction, which occurs at the surface of endothelial cells, is strongly promoted by thrombomodulin.
- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
- PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
- MISCELLANEOUS: Calcium also binds, with stronger affinity to another site, beyond the GLA domain. This GLA-independent binding site is necessary for the recognition of the thrombin-thrombomodulin complex.
- SIMILARITY: Belongs to the peptidase S1 family [view classification].
- SIMILARITY: Contains 2 EGF-like domains.
- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
- SIMILARITY: Contains 1 peptidase S1 domain [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 456 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 51409 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: CAAF6833F894C209 [This is a checksum on the sequence] |
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10 20 30 40 50 60
XTSLLLFVTI WGISSTPAPP DSVFSSSQRA HQVLRIRKRA NSFLEELRPG NVERECSEEV
70 80 90 100 110 120
CEFEEAREIF QNTEDTMAFW SFYSDGDQCE DRPSGSPCDL PCCGRGKCID GLGGFRCDCA
130 140 150 160 170 180
EGWEGRFCLH EVRFSNCSAE NGGCAHYCME EEGRRHCSCA PGYRLEDDHQ LCVSKVTFPC
190 200 210 220 230 240
GRLGKRMEKK RKTLKRDTNQ VDQKDQLDPR IVDGQEAGWG ESPWQAVLLD SKKKLVCGAV
250 260 270 280 290 300
LIHVSWVLTV AHCLDSRKKL IVRLGEYDMR RWESWEVDLD IKEVIIHPNY TKSTSDNDIA
310 320 330 340 350 360
LLRLAKPATL SQTIVPICLP DSGLSERKLT QVGQETVVTG WGYRDETKRN RTFVLSFIKV
370 380 390 400 410 420
PVVPYNACVH AMENKISENM LCAGILGDPR DACEGDSGGP MVTFFRGTWF LVGLVSWGEG
430 440 450
CGRLYNYGVY TKVSRYLDWI YGHIKAQEAP LESQVP
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P00745 in FASTA format |
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