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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] (Fragment)

 PROC_RABIT              Reviewed;         458 AA.
Q28661;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 133.
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; Fragment;
Name=PROC;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Shen L., He X., Dahlback B.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
-!- 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:
Reaction=Degradation of blood coagulation factors Va and VIIIa.;
EC=3.4.21.69;
-!- 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; U49933; AAA92956.1; -; mRNA.
UniGene; Ocu.2057; -.
ProteinModelPortal; Q28661; -.
STRING; 9986.ENSOCUP00000013608; -.
MEROPS; S01.218; -.
eggNOG; ENOG410IJRM; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; Q28661; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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-like_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; 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; 1.
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 27 {ECO:0000250}.
PROPEP 28 36 {ECO:0000250}.
/FTId=PRO_0000028122.
CHAIN 37 458 Vitamin K-dependent protein C.
/FTId=PRO_0000028123.
CHAIN 37 192 Vitamin K-dependent protein C light
chain. {ECO:0000250}.
/FTId=PRO_0000028124.
CHAIN 195 458 Vitamin K-dependent protein C heavy
chain. {ECO:0000250}.
/FTId=PRO_0000028125.
PEPTIDE 195 209 Activation peptide. {ECO:0000250}.
/FTId=PRO_0000028126.
DOMAIN 37 82 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 91 126 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 130 170 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 210 447 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 250 250 Charge relay system.
ACT_SITE 296 296 Charge relay system.
ACT_SITE 399 399 Charge relay system.
SITE 209 210 Cleavage; by thrombin. {ECO:0000250}.
MOD_RES 42 42 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 43 43 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 50 50 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 52 52 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 56 56 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 62 62 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 65 65 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P00745,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 107 107 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 58 {ECO:0000250}.
DISULFID 86 105 {ECO:0000250}.
DISULFID 95 100 {ECO:0000250}.
DISULFID 99 114 {ECO:0000250}.
DISULFID 116 125 {ECO:0000250}.
DISULFID 134 145 {ECO:0000250}.
DISULFID 141 154 {ECO:0000250}.
DISULFID 156 169 {ECO:0000250}.
DISULFID 177 316 Interchain (between light and heavy
chains). {ECO:0000255|PROSITE-
ProRule:PRU00076, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00463}.
DISULFID 235 251 {ECO:0000250}.
DISULFID 370 384 {ECO:0000250}.
DISULFID 395 423 {ECO:0000250}.
NON_TER 1 1
SEQUENCE 458 AA; 51088 MW; D75A5F990C8F29D7 CRC64;
IPDDVGYRNQ KTASKEGVCV VSKCQDGPNT LPRAKRANSF LEELRPSSLE RECVEEVCDL
EEAKEIFQSV DDTLAFWYKY VDGDQCAALP SEHPCSSQCC GHGTCADSIG GFSCQCHGGW
EGSFCQYEVR FSNCSVDNGG CAHYCLEEEA GRSCSCAPGY ELADDHLQCE PAVRFPCGRL
GWKRIEKKRG NVKRDLEQVD EMDEVDPRLI DGKLTRRGDS PWQVILLDSK KKLACGAVLI
HVSWVLTAAH CMEEPKKLFV RLGEYDLRRK ERWELDLNIQ EVLIHPNYSR STTDNDIALL
RLAQPATLSQ TIVPICLPDN GLAERELMQA GQETVVTGWG YHSSREKEAK RNRTFILNFI
TVPVAPQNEC EQVMSNIISE NMLCAGILGD RRDACDGDSG GPMVASFRGT WFLVGLVSWG
EGCGDLNNYG VYTKVSRYLD WIHSHIEEKE AAPESPAP


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