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Protein

Vitamin K-dependent protein C

Gene

Proc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3411. Proc.

Subcellular locationi

  • Secreted By similarity
  • Golgi apparatus By similarity
  • Endoplasmic reticulum By similarity

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • extracellular space Source: RGD
  • Golgi apparatus Source: UniProtKB
Complete GO annotation...

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...)Sequence analysis1
Disulfide bondi239 ↔ 255By similarity
Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
Glycosylationi355N-linked (GlcNAc...)Sequence 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.
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
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.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.
InterProiIPR017857. Coagulation_fac_subgr_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.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP31394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019596.

Protein family/group databases

MEROPSiS01.218.

PTM databases

PhosphoSitePlusiP31394.

Proteomic databases

PaxDbiP31394.
PRIDEiP31394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25268.
KEGGirno:25268.
UCSCiRGD:3411. rat.

Organism-specific databases

CTDi5624.
RGDi3411. Proc.

Phylogenomic databases

eggNOGiENOG410IJRM. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP31394.
KOiK01344.
PhylomeDBiP31394.

Miscellaneous databases

PROiP31394.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_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.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROC_RAT
AccessioniPrimary (citable) accession number: P31394
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.