Reviewed, UniProtKB/Swiss-Prot Q28661 (PROC_RABIT)

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

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	458 AA.
Sequence status	Fragment.
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 apoptosis Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
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 – 27	›27	By similarity
	Propeptide	28 – 36	9	By similarity		PRO_0000028122
	Chain	37 – 458	422	Vitamin K-dependent protein C		PRO_0000028123
	Chain	37 – 192	156	Vitamin K-dependent protein C light chain By similarity		PRO_0000028124
	Chain	195 – 458	264	Vitamin K-dependent protein C heavy chain By similarity		PRO_0000028125
	Peptide	195 – 209	15	Activation peptide By similarity		PRO_0000028126
Regions
	Domain	37 – 82	46	Gla
	Domain	91 – 126	36	EGF-like 1
	Domain	130 – 170	41	EGF-like 2
	Domain	210 – 447	238	Peptidase S1
Sites
	Active site	250	1	Charge relay system
	Active site	296	1	Charge relay system
	Active site	399	1	Charge relay system
	Site	209 – 210	2	Cleavage; by thrombin By similarity
Amino acid modifications
	Modified residue	42	1	4-carboxyglutamate By similarity
	Modified residue	43	1	4-carboxyglutamate By similarity
	Modified residue	50	1	4-carboxyglutamate By similarity
	Modified residue	52	1	4-carboxyglutamate By similarity
	Modified residue	55	1	4-carboxyglutamate By similarity
	Modified residue	56	1	4-carboxyglutamate By similarity
	Modified residue	61	1	4-carboxyglutamate By similarity
	Modified residue	62	1	4-carboxyglutamate By similarity
	Modified residue	65	1	4-carboxyglutamate By similarity
	Modified residue	107	1	(3R)-3-hydroxyaspartate By similarity
	Glycosylation	133	1	N-linked (GlcNAc...) Potential
	Glycosylation	287	1	N-linked (GlcNAc...) Potential
	Glycosylation	352	1	N-linked (GlcNAc...) Potential
	Disulfide bond	53 ↔ 58		By similarity
	Disulfide bond	86 ↔ 105		By similarity
	Disulfide bond	95 ↔ 100		By similarity
	Disulfide bond	99 ↔ 114		By similarity
	Disulfide bond	116 ↔ 125		By similarity
	Disulfide bond	134 ↔ 145		By similarity
	Disulfide bond	141 ↔ 154		By similarity
	Disulfide bond	156 ↔ 169		By similarity
	Disulfide bond	177 ↔ 316		Interchain (between light and heavy chains) By similarity
	Disulfide bond	235 ↔ 251		By similarity
	Disulfide bond	370 ↔ 384		By similarity
	Disulfide bond	395 ↔ 423		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q28661-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D75A5F990C8F29D7	FASTA	458	51,088
	10 20 30 40 50 60 IPDDVGYRNQ KTASKEGVCV VSKCQDGPNT LPRAKRANSF LEELRPSSLE RECVEEVCDL 70 80 90 100 110 120 EEAKEIFQSV DDTLAFWYKY VDGDQCAALP SEHPCSSQCC GHGTCADSIG GFSCQCHGGW 130 140 150 160 170 180 EGSFCQYEVR FSNCSVDNGG CAHYCLEEEA GRSCSCAPGY ELADDHLQCE PAVRFPCGRL 190 200 210 220 230 240 GWKRIEKKRG NVKRDLEQVD EMDEVDPRLI DGKLTRRGDS PWQVILLDSK KKLACGAVLI 250 260 270 280 290 300 HVSWVLTAAH CMEEPKKLFV RLGEYDLRRK ERWELDLNIQ EVLIHPNYSR STTDNDIALL 310 320 330 340 350 360 RLAQPATLSQ TIVPICLPDN GLAERELMQA GQETVVTGWG YHSSREKEAK RNRTFILNFI 370 380 390 400 410 420 TVPVAPQNEC EQVMSNIISE NMLCAGILGD RRDACDGDSG GPMVASFRGT WFLVGLVSWG 430 440 450 EGCGDLNNYG VYTKVSRYLD WIHSHIEEKE AAPESPAP

References

[1]	Shen L., He X., Dahlback B. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49933 mRNA. Translation: AAA92956.1.
UniGene	Ocu.2057
3D structure databases
HSSP	HSSP built from PDB template 1AUT based on UniProtKB P04070.
SMR	Q28661. Positions 85-179, 209-446.
ModBase	Search...
Protein family/group databases
MEROPS	S01.218.
Genome annotation databases
Ensembl	ENSOCUG00000015846. Oryctolagus cuniculus. [Contig view]
Phylogenomic databases
HOVERGEN	Q28661.
Enzyme and pathway databases
BRENDA	3.4.21.69. 255.
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. 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. 2 hits. 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...

Entry information

Entry name

PROC_RABIT

Accession

Primary (citable) accession number: Q28661

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)