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Protein

Vitamin K-dependent protein C

Gene

Proc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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.By similarity

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.

Catalytic activityi

Degradation of blood coagulation factors Va and VIIIa.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei254Charge relay system1
Active sitei300Charge relay system1
Active sitei402Charge relay system1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • oligopeptidase activity Source: RGD
  • protein self-association Source: RGD
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • liver development Source: RGD
  • negative regulation of blood coagulation Source: RGD
  • negative regulation of coagulation Source: UniProtKB
  • negative regulation of inflammatory response Source: UniProtKB
  • positive regulation of establishment of endothelial barrier Source: UniProtKB
  • proteolysis Source: RGD

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium

Protein family/group databases

MEROPSiS01.218

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent protein C (EC:3.4.21.69)
Alternative name(s):
Anticoagulant protein C
Autoprothrombin IIA
Blood coagulation factor XIV
Cleaved into the following 3 chains:
Gene namesi
Name:Proc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3411 Proc

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002812719 – 41By similarityAdd BLAST23
ChainiPRO_000002812842 – 461Vitamin K-dependent protein CAdd BLAST420
ChainiPRO_000002812942 – 196Vitamin K-dependent protein C light chainBy similarityAdd BLAST155
ChainiPRO_0000028130199 – 461Vitamin K-dependent protein C heavy chainBy similarityAdd BLAST263
PeptideiPRO_0000028131199 – 212Activation peptideBy similarityAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei484-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei554-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi58 ↔ 63By similarity
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei704-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi91 ↔ 110By similarity
Disulfide bondi100 ↔ 105By similarity
Disulfide bondi104 ↔ 119By similarity
Modified residuei112(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi121 ↔ 130By similarity
Disulfide bondi139 ↔ 150By similarity
Disulfide bondi146 ↔ 159By similarity
Disulfide bondi161 ↔ 174By similarity
Disulfide bondi182 ↔ 320Interchain (between light and heavy chains)PROSITE-ProRule annotation
Glycosylationi215N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi239 ↔ 255By similarity
Glycosylationi291N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi355N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi373 ↔ 387By similarity
Disulfide bondi398 ↔ 426By similarity

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei212 – 213Cleavage; by thrombinBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

PaxDbiP31394
PRIDEiP31394

PTM databases

PhosphoSitePlusiP31394

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Interactioni

Subunit structurei

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.

GO - Molecular functioni

  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019596

Structurei

3D structure databases

ProteinModelPortaliP31394
SMRiP31394
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 87GlaPROSITE-ProRule annotationAdd BLAST46
Domaini96 – 131EGF-like 1PROSITE-ProRule annotationAdd BLAST36
Domaini135 – 175EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini213 – 450Peptidase S1PROSITE-ProRule annotationAdd BLAST238

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IJRM Eukaryota
COG5640 LUCA
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP31394
KOiK01344
PhylomeDBiP31394

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_Gla_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31394-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWQFRIFLLF ASTWGISGVS AHPDPVFSSS EGAHQVLRVR RANSFLEEVR
60 70 80 90 100
AGSLERECME EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSTPPLDHQC
110 120 130 140 150
DSPCCGHGTC IDGLGGFSCS CDKGWEGRFC QQEMGFQDCR VKNGGCYHYC
160 170 180 190 200
LEETRGRRCR CAPGYELADD HMHCRPTVNF PCGKLWKRTD KKRKNFKRDI
210 220 230 240 250
DPEDEELELG PRIVNGTLTK QGDSPWQAIL LDSKKKLACG GVLIHTSWVL
260 270 280 290 300
TAAHCLESSK KLTVRLGEYD LRRRDPWELD LDIKEVLVHP NYTRSNSDND
310 320 330 340 350
IALLRLSQPA TLSKTIVPIC LPNSGLAQEL SQAGQETVVT GWGYQSDKVK
360 370 380 390 400
DGRRNRTFIL TFIRIPLAAR NDCMQVMNNV VSENMLCAGI IGDTRDACDG
410 420 430 440 450
DSGGPMVVFF RGTWFLVGLV SWGEGCGHLN NYGVYTKVGS YLKWIHSYIG
460
ERDVSLKSPK L
Length:461
Mass (Da):51,912
Last modified:July 1, 1993 - v1
Checksum:i8A4CF93664EDACD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64336 mRNA Translation: CAA45617.1
PIRiS18994
RefSeqiNP_036935.1, NM_012803.1
UniGeneiRn.91064

Genome annotation databases

GeneIDi25268
KEGGirno:25268
UCSCiRGD:3411 rat

Similar proteinsi

Entry informationi

Entry nameiPROC_RAT
AccessioniPrimary (citable) accession number: P31394
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 23, 2018
This is version 159 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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