Reviewed, UniProtKB/Swiss-Prot Q28315 (PROC_CAPHI)

Names and origin

Protein names

Recommended name:
    Vitamin K-dependent protein C
    EC=3.4.21.69
Alternative name(s):
    Autoprothrombin IIA
    Anticoagulant protein C
    Blood coagulation factor XIV

Gene names

Name:

PROC

Organism

Capra hircus (Goat)

Taxonomic identifier

9925 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Capra

Protein attributes

Sequence length	157 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Blood coagulation
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›157	›157	Vitamin K-dependent protein C		PRO_0000088708
Regions
	Domain	‹1 – ›157	›157	Peptidase S1
Sites
	Active site	26	1	Charge relay system
	Active site	125	1	Charge relay system
Amino acid modifications
	Glycosylation	17	1	N-linked (GlcNAc...) Potential
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Disulfide bond	96 ↔ 110		By similarity
	Disulfide bond	121 ↔ 149		By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	157	1

Sequences

	Sequence		Length	Mass (Da)
	Q28315-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B89790F9954B610A	FASTA	157	17,251
	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

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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D43752 Genomic DNA. Translation: BAA07809.1.
3D structure databases
HSSP	HSSP built from PDB template 1AUT based on UniProtKB P04070.
SMR	Q28315. Positions 1-157.
ModBase	Search...
Protein family/group databases
MEROPS	S01.218.
Phylogenomic databases
HOVERGEN	Q28315.
Enzyme and pathway databases
BRENDA	3.4.21.69. 1312.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROC_CAPHI

Accession

Primary (citable) accession number: Q28315

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 5, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)