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Q28315 (PROC_CAPHI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:PROC
OrganismCapra hircus (Goat)
Taxonomic identifier9925 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Protein attributes

Sequence length157 AA.
Sequence statusFragment.
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.

Tissue specificity

Plasma; synthesized in the liver.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›157›157Vitamin K-dependent protein C
PRO_0000088708

Regions

Domain‹1 – ›157›157Peptidase S1

Sites

Active site261Charge relay system
Active site1251Charge relay system

Amino acid modifications

Glycosylation171N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 110 By similarity
Disulfide bond121 ↔ 149 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1571

Sequences

Sequence LengthMass (Da)Tools
Q28315 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B89790F9954B610A

FASTA15717,251
        10         20         30         40         50         60 
ESWEVDLDIK EVIVRPNYTK STSDNDIALL HLAKPATLSQ TIVPICLPDS GLSERKLTQV 

        70         80         90        100        110        120 
GQETVVTGWG YRDETKKNRT SILNFIKIPV VSYNACVHAM ENKVSENMLC AGILGNPRDA 

       130        140        150 
CEGDSGGPMV TFFRGTWFLV GLVSWGEGCG RLNNYGI 

« Hide

References

[1]"A comparative study of partial primary structures of the catalytic region of mammalian protein C."
Murakawa M., Okamura T., Kamura T., Kuroiwa M., Harada M., Niho Y.
Br. J. Haematol. 86:590-600(1994) [PubMed: 8043441] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D43752 Genomic DNA. Translation: BAA07809.1.

3D structure databases

ProteinModelPortalQ28315.
SMRQ28315. Positions 1-157.
ModBaseSearch...

Protein family/group databases

MEROPSS01.218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. Partial match.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROC_CAPHI
AccessionPrimary (citable) accession number: Q28315
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 63 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