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P31394 (PROC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. Vitamin K-dependent protein C light chain
  2. Vitamin K-dependent protein C heavy chain
  3. Activation peptide
Gene names
Name:Proc
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Catalytic activity

Degradation of blood coagulation factors Va and VIIIa.

Subunit structure

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.

Tissue specificity

Plasma; synthesized in the liver.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Propeptide33 – 419 By similarity
PRO_0000028127
Chain42 – 461420Vitamin K-dependent protein C
PRO_0000028128
Chain42 – 196155Vitamin K-dependent protein C light chain By similarity
PRO_0000028129
Chain199 – 461263Vitamin K-dependent protein C heavy chain By similarity
PRO_0000028130
Peptide199 – 21214Activation peptide By similarity
PRO_0000028131

Regions

Domain42 – 8746Gla
Domain96 – 13136EGF-like 1
Domain135 – 17541EGF-like 2
Domain213 – 450238Peptidase S1

Sites

Active site2541Charge relay system
Active site3001Charge relay system
Active site4021Charge relay system
Site212 – 2132Cleavage; by thrombin By similarity

Amino acid modifications

Modified residue4714-carboxyglutamate By similarity
Modified residue4814-carboxyglutamate By similarity
Modified residue5514-carboxyglutamate By similarity
Modified residue5714-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6114-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6714-carboxyglutamate By similarity
Modified residue7014-carboxyglutamate By similarity
Modified residue1121(3R)-3-hydroxyaspartate By similarity
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 63 By similarity
Disulfide bond91 ↔ 110 By similarity
Disulfide bond100 ↔ 105 By similarity
Disulfide bond104 ↔ 119 By similarity
Disulfide bond121 ↔ 130 By similarity
Disulfide bond139 ↔ 150 By similarity
Disulfide bond146 ↔ 159 By similarity
Disulfide bond161 ↔ 174 By similarity
Disulfide bond182 ↔ 320Interchain (between light and heavy chains) By similarity
Disulfide bond239 ↔ 255 By similarity
Disulfide bond373 ↔ 387 By similarity
Disulfide bond398 ↔ 426 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31394 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 8A4CF93664EDACD5

FASTA46151,912
        10         20         30         40         50         60 
MWQFRIFLLF ASTWGISGVS AHPDPVFSSS EGAHQVLRVR RANSFLEEVR AGSLERECME 

        70         80         90        100        110        120 
EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSTPPLDHQC DSPCCGHGTC IDGLGGFSCS 

       130        140        150        160        170        180 
CDKGWEGRFC QQEMGFQDCR VKNGGCYHYC LEETRGRRCR CAPGYELADD HMHCRPTVNF 

       190        200        210        220        230        240 
PCGKLWKRTD KKRKNFKRDI DPEDEELELG PRIVNGTLTK QGDSPWQAIL LDSKKKLACG 

       250        260        270        280        290        300 
GVLIHTSWVL TAAHCLESSK KLTVRLGEYD LRRRDPWELD LDIKEVLVHP NYTRSNSDND 

       310        320        330        340        350        360 
IALLRLSQPA TLSKTIVPIC LPNSGLAQEL SQAGQETVVT GWGYQSDKVK DGRRNRTFIL 

       370        380        390        400        410        420 
TFIRIPLAAR NDCMQVMNNV VSENMLCAGI IGDTRDACDG DSGGPMVVFF RGTWFLVGLV 

       430        440        450        460 
SWGEGCGHLN NYGVYTKVGS YLKWIHSYIG ERDVSLKSPK L

« Hide

References

[1]"The cDNA cloning and mRNA expression of rat protein C."
Okafuji T., Maekawa K., Nawa K., Marumoto Y.
Biochim. Biophys. Acta 1131:329-332(1992) [PubMed: 1627650] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X64336 mRNA. Translation: CAA45617.1.
IPIIPI00211817.
PIRS18994.
RefSeqNP_036935.1. NM_012803.1.
UniGeneRn.91064.

3D structure databases

ProteinModelPortalP31394.
SMRP31394. Positions 43-87, 90-186, 213-449.
ModBaseSearch...

Protein-protein interaction databases

STRINGP31394.

Protein family/group databases

MEROPSS01.218.

Proteomic databases

PRIDEP31394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25268.
KEGGrno:25268.
UCSCNM_012803. rat.

Organism-specific databases

CTD5624.
RGD3411. Proc.

Phylogenomic databases

eggNOGroNOG10647.
HOVERGENHBG013304.
InParanoidP31394.
OrthoDBEOG43BMNX.

Gene expression databases

ArrayExpressP31394.
GenevestigatorP31394.
GermOnlineENSRNOG00000014376. Rattus norvegicus.

Family and domain databases

InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR006209. EGF.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
KOK01344.
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio605945.

Entry information

Entry namePROC_RAT
AccessionPrimary (citable) accession number: P31394
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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