[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar; TISSUE=Liver; DOI=10.1016/0167-4781(92)90035-X; PubMed=1627650 [NCBI, ExPASy, EBI, Israel, Japan] Okafuji T., Maekawa K., Nawa K., Marumoto Y.; "The cDNA cloning and mRNA expression of rat protein C."; Biochim. Biophys. Acta 1131:329-332(1992).

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: 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.
PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.
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.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 2 EGF-like domains.
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X64336; CAA45617.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S18994; S18994.

NP_036935.1; -.

3D structure databases

HSSP

P04070; 1AUT. [HSSP ENTRY / PDB]

SMR

P31394; 213-449.

ModBase

P31394.

Protein family/group databases

MEROPS

S01.218; -.

Organism-specific databases

RGD

3411; Proc.

Gene expression databases

ArrayExpress

P31394; -.

GermOnline

ENSRNOG00000014376; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002383; Coagulation_factor_Gla.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR012224; Pept_S1A_FX.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Pfam

PF00008; EGF; 1.
PF00594; Gla; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001143; Factor_X; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00001; GLABLOOD.

SMART

SM00181; EGF; 1.
SM00179; EGF_CA; 1.
SM00069; GLA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; 2.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000014376; Rattus norvegicus. [Contig view]

GeneID

25268; -.

KEGG

rno:25268; -.

Phylogenomic databases

HOVERGEN

P31394; -.

Other

NextBio

605945; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Blood coagulation; Calcium; Cleavage on pair of basic residues; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 32`	`32`	`By similarity.`
`PROPEP`	`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`
`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.`
`ACT_SITE`	`254 254`		`Charge relay system.`
`ACT_SITE`	`300 300`		`Charge relay system.`
`ACT_SITE`	`402 402`		`Charge relay system.`
`SITE`	`212 213`	`2`	`Cleavage; by thrombin (By similarity).`
`MOD_RES`	`47 47`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`48 48`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`55 55`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`57 57`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`60 60`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`61 61`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`66 66`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`67 67`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`70 70`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`112 112`		`3-hydroxyaspartate (By similarity).`
`CARBOHYD`	`215 215`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`291 291`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`355 355`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`58 63`		`By similarity.`
`DISULFID`	`91 110`		`By similarity.`
`DISULFID`	`100 105`		`By similarity.`
`DISULFID`	`104 119`		`By similarity.`
`DISULFID`	`121 130`		`By similarity.`
`DISULFID`	`139 150`		`By similarity.`
`DISULFID`	`146 159`		`By similarity.`
`DISULFID`	`161 174`		`By similarity.`
`DISULFID`	`182 320`		`Interchain (between light and heavy chains) (By similarity).`
`DISULFID`	`239 255`		`By similarity.`
`DISULFID`	`373 387`		`By similarity.`
`DISULFID`	`398 426`		`By similarity.`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 51912 Da [This is the MW of the unprocessed precursor]

CRC64: 8A4CF93664EDACD5 [This is a checksum on the sequence]

        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

P31394 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools