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Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide]

 PROC_PIG                Reviewed;         459 AA.
Q9GLP2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Vitamin K-dependent protein C;
EC=3.4.21.69;
AltName: Full=Anticoagulant protein C;
AltName: Full=Autoprothrombin IIA;
AltName: Full=Blood coagulation factor XIV;
Contains:
RecName: Full=Vitamin K-dependent protein C light chain;
Contains:
RecName: Full=Vitamin K-dependent protein C heavy chain;
Contains:
RecName: Full=Activation peptide;
Flags: Precursor;
Name=PROC;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=11229814; DOI=10.1007/PL00000775;
Grimm D.R., Colter M.B., Braunschweig M., Alexander L.J., Neame P.J.,
Kim H.K.W.;
"Porcine factor V: cDNA cloning, gene mapping, three-dimensional
protein modeling of membrane binding sites and comparative anatomy of
domains.";
Cell. Mol. Life Sci. 58:148-159(2001).
-!- 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. Exerts a
protective effect on the endothelial cell barrier function.
{ECO:0000250|UniProtKB:P04070}.
-!- 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.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}.
Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic
reticulum {ECO:0000250|UniProtKB:P04070}.
-!- 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.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF191307; AAG28380.1; -; mRNA.
RefSeq; NP_999083.1; NM_213918.1.
UniGene; Ssc.2763; -.
ProteinModelPortal; Q9GLP2; -.
SMR; Q9GLP2; -.
STRING; 9823.ENSSSCP00000026729; -.
MEROPS; S01.218; -.
PaxDb; Q9GLP2; -.
PeptideAtlas; Q9GLP2; -.
PRIDE; Q9GLP2; -.
GeneID; 396954; -.
KEGG; ssc:396954; -.
CTD; 5624; -.
eggNOG; ENOG410IJRM; Eukaryota.
eggNOG; COG5640; LUCA.
HOVERGEN; HBG013304; -.
InParanoid; Q9GLP2; -.
KO; K01344; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030195; P:negative regulation of blood coagulation; IBA:GO_Central.
GO; GO:0050819; P:negative regulation of coagulation; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISS:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; EGF-like domain;
Endoplasmic reticulum; Gamma-carboxyglutamic acid; Glycoprotein;
Golgi apparatus; Hemostasis; Hydrolase; Hydroxylation; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 18 {ECO:0000250}.
PROPEP 19 41 {ECO:0000250}.
/FTId=PRO_0000028117.
CHAIN 42 459 Vitamin K-dependent protein C.
/FTId=PRO_0000028118.
CHAIN 42 196 Vitamin K-dependent protein C light
chain. {ECO:0000250}.
/FTId=PRO_0000028119.
CHAIN 199 459 Vitamin K-dependent protein C heavy
chain. {ECO:0000250}.
/FTId=PRO_0000028120.
PEPTIDE 199 213 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028121.
DOMAIN 42 87 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 96 131 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 135 175 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 214 448 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 255 255 Charge relay system.
ACT_SITE 301 301 Charge relay system.
ACT_SITE 400 400 Charge relay system.
SITE 213 214 Cleavage; by thrombin. {ECO:0000250}.
MOD_RES 47 47 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 48 48 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 55 55 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 57 57 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 60 60 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 61 61 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 66 66 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 67 67 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 70 70 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 76 76 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 112 112 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 63 {ECO:0000250}.
DISULFID 91 110 {ECO:0000250}.
DISULFID 100 105 {ECO:0000250}.
DISULFID 104 119 {ECO:0000250}.
DISULFID 121 130 {ECO:0000250}.
DISULFID 139 150 {ECO:0000250}.
DISULFID 146 159 {ECO:0000250}.
DISULFID 161 174 {ECO:0000250}.
DISULFID 182 321 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00076, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463}.
DISULFID 240 256 {ECO:0000250}.
DISULFID 371 385 {ECO:0000250}.
DISULFID 396 424 {ECO:0000250}.
SEQUENCE 459 AA; 51867 MW; 8541AAC14CC16D09 CRC64;
MWQLASLLLL LIIWAVSSTP VPPDSVFSSS QRAHQMLRSK RANSFLEELR PSSLERECKE
ETCDFEEARE IFQNTENTMA FWSKYHDGDQ CAVSPPEHLC DSPCCGRGTC IDGLGGFRCD
CAQGWEGRFC LHEVRFSNCS TENGGCAHYC LEEEGGRRCA CAPGYRLGDD HLQCEPKVRS
PCGRLGNRME KKRKNLKRDT DQVDKKEDQI DPRLVNGKQS PWGESPWQVI LLDSKKKLAC
GAVLIHVSWV LTAAHCLDDY KKLTVRLGEY DLRRREKWEV DLDIKEFLVH PNYTRSTSDN
DIALLRLAEP ATFSQTIVPI CLPDSGLSER ELTRVGQETV VTGWGYRSEA KTNRSFILNF
IKVPVAPHNE CVQAMHNKIS ENMLCAGILG DSRDACEGDS GGPMVASFRG TWFLVGLVSW
GEGCGRLHNY GVYTKVSRYL DWIHGHIRME EAFHKNQVP


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