Reviewed, UniProtKB/Swiss-Prot Q9GLP2 (PROC_PIG)

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

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	459 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 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 – 18	18	By similarity
	Propeptide	19 – 41	23	By similarity		PRO_0000028117
	Chain	42 – 459	418	Vitamin K-dependent protein C		PRO_0000028118
	Chain	42 – 196	155	Vitamin K-dependent protein C light chain By similarity		PRO_0000028119
	Chain	199 – 459	261	Vitamin K-dependent protein C heavy chain By similarity		PRO_0000028120
	Peptide	199 – 213	15	Activation peptide By similarity		PRO_0000028121
Regions
	Domain	42 – 87	46	Gla
	Domain	96 – 131	36	EGF-like 1
	Domain	135 – 175	41	EGF-like 2
	Domain	214 – 448	235	Peptidase S1
Sites
	Active site	255	1	Charge relay system
	Active site	301	1	Charge relay system
	Active site	400	1	Charge relay system
	Site	213 – 214	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	138	1	N-linked (GlcNAc...) Potential
	Glycosylation	292	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	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 ↔ 321		Interchain (between light and heavy chains) By similarity
	Disulfide bond	240 ↔ 256		By similarity
	Disulfide bond	371 ↔ 385		By similarity
	Disulfide bond	396 ↔ 424		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9GLP2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 8541AAC14CC16D09	FASTA	459	51,867
	10 20 30 40 50 60 MWQLASLLLL LIIWAVSSTP VPPDSVFSSS QRAHQMLRSK RANSFLEELR PSSLERECKE 70 80 90 100 110 120 ETCDFEEARE IFQNTENTMA FWSKYHDGDQ CAVSPPEHLC DSPCCGRGTC IDGLGGFRCD 130 140 150 160 170 180 CAQGWEGRFC LHEVRFSNCS TENGGCAHYC LEEEGGRRCA CAPGYRLGDD HLQCEPKVRS 190 200 210 220 230 240 PCGRLGNRME KKRKNLKRDT DQVDKKEDQI DPRLVNGKQS PWGESPWQVI LLDSKKKLAC 250 260 270 280 290 300 GAVLIHVSWV LTAAHCLDDY KKLTVRLGEY DLRRREKWEV DLDIKEFLVH PNYTRSTSDN 310 320 330 340 350 360 DIALLRLAEP ATFSQTIVPI CLPDSGLSER ELTRVGQETV VTGWGYRSEA KTNRSFILNF 370 380 390 400 410 420 IKVPVAPHNE CVQAMHNKIS ENMLCAGILG DSRDACEGDS GGPMVASFRG TWFLVGLVSW 430 440 450 GEGCGRLHNY GVYTKVSRYL DWIHGHIRME EAFHKNQVP

References

[1]

"Porcine factor V: cDNA cloning, gene mapping, three-dimensional protein modeling of membrane binding sites and comparative anatomy of domains." Grimm D.R., Colter M.B., Braunschweig M., Alexander L.J., Neame P.J., Kim H.K.W. Cell. Mol. Life Sci. 58:148-159(2001) [PubMed: 11229814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF191307 mRNA. Translation: AAG28380.1.
RefSeq	NP_999083.1.
UniGene	Ssc.2763
3D structure databases
HSSP	HSSP built from PDB template 1AUT based on UniProtKB P04070.
SMR	Q9GLP2. Positions 214-448.
ModBase	Search...
Protein family/group databases
MEROPS	S01.218.
Genome annotation databases
GeneID	396954.
KEGG	ssc:396954.
Phylogenomic databases
HOVERGEN	Q9GLP2.
Enzyme and pathway databases
BRENDA	3.4.21.69. 249.
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. 2 hits. 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_PIG

Accession

Primary (citable) accession number: Q9GLP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)