Reviewed, UniProtKB/Swiss-Prot P31394 (PROC_RAT)

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
Cleaved into the following 3 chains:
    1- Recommended name:
            Vitamin K-dependent protein C light chain
    2- Recommended name:
            Vitamin K-dependent protein C heavy chain
    3- Recommended name:
            Activation peptide

Gene names

Name:

Proc

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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.

Ontologies

Keywords
Biological process	Blood coagulation
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Zymogen
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of inflammatory response Traceable author statement. Source: RGD proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from direct assay. Source: RGD
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Signal peptide	1 – 32	32	By similarity
	Propeptide	33 – 41	9	By similarity		PRO_0000028127
	Chain	42 – 461	420	Vitamin K-dependent protein C		PRO_0000028128
	Chain	42 – 196	155	Vitamin K-dependent protein C light chain By similarity		PRO_0000028129
	Chain	199 – 461	263	Vitamin K-dependent protein C heavy chain By similarity		PRO_0000028130
	Peptide	199 – 212	14	Activation peptide By similarity		PRO_0000028131
Regions
	Domain	42 – 87	46	Gla
	Domain	96 – 131	36	EGF-like 1
	Domain	135 – 175	41	EGF-like 2
	Domain	213 – 450	238	Peptidase S1
Sites
	Active site	254	1	Charge relay system
	Active site	300	1	Charge relay system
	Active site	402	1	Charge relay system
	Site	212 – 213	2	Cleavage; by thrombin By similarity
Amino acid modifications
	Modified residue	47	1	4-carboxyglutamate By similarity
	Modified residue	48	1	4-carboxyglutamate By similarity
	Modified residue	55	1	4-carboxyglutamate By similarity
	Modified residue	57	1	4-carboxyglutamate By similarity
	Modified residue	60	1	4-carboxyglutamate By similarity
	Modified residue	61	1	4-carboxyglutamate By similarity
	Modified residue	66	1	4-carboxyglutamate By similarity
	Modified residue	67	1	4-carboxyglutamate By similarity
	Modified residue	70	1	4-carboxyglutamate By similarity
	Modified residue	112	1	(3R)-3-hydroxyaspartate By similarity
	Glycosylation	215	1	N-linked (GlcNAc...) Potential
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Disulfide bond	58 ↔ 63		By similarity
	Disulfide bond	91 ↔ 110		By similarity
	Disulfide bond	100 ↔ 105		By similarity
	Disulfide bond	104 ↔ 119		By similarity
	Disulfide bond	121 ↔ 130		By similarity
	Disulfide bond	139 ↔ 150		By similarity
	Disulfide bond	146 ↔ 159		By similarity
	Disulfide bond	161 ↔ 174		By similarity
	Disulfide bond	182 ↔ 320		Interchain (between light and heavy chains) By similarity
	Disulfide bond	239 ↔ 255		By similarity
	Disulfide bond	373 ↔ 387		By similarity
	Disulfide bond	398 ↔ 426		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31394-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 8A4CF93664EDACD5	FASTA	461	51,912
	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64336 mRNA. Translation: CAA45617.1.
IPI	IPI00211817.
PIR	S18994.
RefSeq	NP_036935.1.
UniGene	Rn.91064
3D structure databases
HSSP	HSSP built from PDB template 1AUT based on UniProtKB P04070.
SMR	P31394. Positions 213-449.
ModBase	Search...
Proteomic databases
PRIDE	P31394.
Genome annotation databases
Ensembl	ENSRNOG00000014376. Rattus norvegicus. [Contig view]
GeneID	25268.
KEGG	rno:25268.
Organism-specific databases
RGD	3411. Proc.
Phylogenomic databases
HOVERGEN	P31394.
Enzyme and pathway databases
BRENDA	3.4.21.69. 248.
Gene expression databases
ArrayExpress	P31394.
GermOnline	ENSRNOG00000014376. Rattus norvegicus.
Family and domain databases
InterPro	IPR002383. Coagulation_factor_Gla. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. IPR000742. EGF_3. IPR001881. EGF_Ca_bd. IPR018097. EGF_Ca_bd_CS. IPR000294. GLA_domain. IPR012224. Pept_S1A_FX. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00008. EGF. 1 hit. PF00594. Gla. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001143. Factor_X. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00001. GLABLOOD.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 1 hit. SM00069. GLA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. 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]
ProtoNet	Search...
Other Resources
NextBio	605945.

Entry information

Entry name

PROC_RAT

Accession

Primary (citable) accession number: P31394

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)