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Protein

Vitamin K-dependent protein C

Gene

PROC

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 sitei252Charge relay system1
Active sitei298Charge relay system1
Active sitei397Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

SABIO-RKP00745.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 15Sequence analysisAdd BLAST›15
PropeptideiPRO_000002809816 – 391 PublicationAdd BLAST24
ChainiPRO_000002809940 – 456Vitamin K-dependent protein CAdd BLAST417
ChainiPRO_000002810040 – 194Vitamin K-dependent protein C light chainAdd BLAST155
ChainiPRO_0000028101197 – 456Vitamin K-dependent protein C heavy chainAdd BLAST260
PeptideiPRO_0000028102197 – 210Activation peptideAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei454-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei534-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei554-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi56 ↔ 61By similarity
Modified residuei584-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei624-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei644-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei684-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei744-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi89 ↔ 108By similarity
Disulfide bondi98 ↔ 103By similarity
Disulfide bondi102 ↔ 117By similarity
Modified residuei110(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi119 ↔ 128By similarity
Glycosylationi136N-linked (GlcNAc...)1 Publication1
Disulfide bondi137 ↔ 148By similarity
Disulfide bondi144 ↔ 157By similarity
Disulfide bondi159 ↔ 172By similarity
Disulfide bondi180 ↔ 318Interchain (between light and heavy chains)
Disulfide bondi237 ↔ 253
Glycosylationi289N-linked (GlcNAc...)1 Publication1
Glycosylationi350N-linked (GlcNAc...)1 Publication1
Glycosylationi366N-linked (GlcNAc...); atypical; partial1 Publication1
Disulfide bondi368 ↔ 382
Disulfide bondi393 ↔ 421

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.1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiP00745.
PRIDEiP00745.

Miscellaneous databases

PMAP-CutDBP00745.

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.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005163.

Structurei

3D structure databases

ProteinModelPortaliP00745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 85GlaPROSITE-ProRule annotationAdd BLAST46
Domaini94 – 129EGF-like 1PROSITE-ProRule annotationAdd BLAST36
Domaini133 – 173EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini211 – 445Peptidase S1PROSITE-ProRule annotationAdd BLAST235

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.
InParanoidiP00745.

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.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. 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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

P00745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
XTSLLLFVTI WGISSTPAPP DSVFSSSQRA HQVLRIRKRA NSFLEELRPG
60 70 80 90 100
NVERECSEEV CEFEEAREIF QNTEDTMAFW SFYSDGDQCE DRPSGSPCDL
110 120 130 140 150
PCCGRGKCID GLGGFRCDCA EGWEGRFCLH EVRFSNCSAE NGGCAHYCME
160 170 180 190 200
EEGRRHCSCA PGYRLEDDHQ LCVSKVTFPC GRLGKRMEKK RKTLKRDTNQ
210 220 230 240 250
VDQKDQLDPR IVDGQEAGWG ESPWQAVLLD SKKKLVCGAV LIHVSWVLTV
260 270 280 290 300
AHCLDSRKKL IVRLGEYDMR RWESWEVDLD IKEVIIHPNY TKSTSDNDIA
310 320 330 340 350
LLRLAKPATL SQTIVPICLP DSGLSERKLT QVGQETVVTG WGYRDETKRN
360 370 380 390 400
RTFVLSFIKV PVVPYNACVH AMENKISENM LCAGILGDPR DACEGDSGGP
410 420 430 440 450
MVTFFRGTWF LVGLVSWGEG CGRLYNYGVY TKVSRYLDWI YGHIKAQEAP

LESQVP
Length:456
Mass (Da):51,409
Last modified:August 13, 1987 - v1
Checksum:iCAAF6833F894C209
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti455 – 456VP → PV AA sequence (PubMed:6896877).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti82F → K.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02435 mRNA. Translation: AAA30685.1.
PIRiA26250. KXBO.
UniGeneiBt.49146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02435 mRNA. Translation: AAA30685.1.
PIRiA26250. KXBO.
UniGeneiBt.49146.

3D structure databases

ProteinModelPortaliP00745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005163.

Protein family/group databases

MEROPSiS01.218.

Proteomic databases

PaxDbiP00745.
PRIDEiP00745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IJRM. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00745.

Enzyme and pathway databases

SABIO-RKP00745.

Miscellaneous databases

PMAP-CutDBP00745.

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.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. 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.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROC_BOVIN
AccessioniPrimary (citable) accession number: P00745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
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, Direct protein sequencing, 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.