Reviewed, UniProtKB/Swiss-Prot Q28278 (PROC_CANFA)

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 2 chains:
    1- Recommended name:
            Vitamin K-dependent protein C light chain
    2- Recommended name:
            Vitamin K-dependent protein C heavy chain

Gene names

Name:

PROC

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	456 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 By similarity.
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 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 – 20	20	Potential
	Propeptide	21 – 42	22	By similarity		PRO_0000028103
	Chain	43 – 456	414	Vitamin K-dependent protein C		PRO_0000028104
	Chain	43 – 197	155	Vitamin K-dependent protein C light chain		PRO_0000028105
	Chain	200 – 456	257	Vitamin K-dependent protein C heavy chain		PRO_0000028106
Regions
	Domain	47 – 88	42	Gla
	Domain	97 – 132	36	EGF-like 1
	Domain	136 – 176	41	EGF-like 2
	Domain	211 – 445	235	Peptidase S1
Sites
	Active site	252	1	Charge relay system By similarity
	Active site	298	1	Charge relay system By similarity
	Active site	397	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	48	1	4-carboxyglutamate By similarity
	Modified residue	49	1	4-carboxyglutamate By similarity
	Modified residue	56	1	4-carboxyglutamate By similarity
	Modified residue	58	1	4-carboxyglutamate By similarity
	Modified residue	61	1	4-carboxyglutamate By similarity
	Modified residue	62	1	4-carboxyglutamate By similarity
	Modified residue	67	1	4-carboxyglutamate By similarity
	Modified residue	68	1	4-carboxyglutamate By similarity
	Modified residue	71	1	4-carboxyglutamate By similarity
	Modified residue	113	1	(3R)-3-hydroxyaspartate By similarity
	Glycosylation	139	1	N-linked (GlcNAc...) Potential
	Glycosylation	202	1	N-linked (GlcNAc...) Potential
	Glycosylation	289	1	N-linked (GlcNAc...) Potential
	Glycosylation	350	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 64		By similarity
	Disulfide bond	92 ↔ 111		By similarity
	Disulfide bond	101 ↔ 106		By similarity
	Disulfide bond	105 ↔ 120		By similarity
	Disulfide bond	122 ↔ 131		By similarity
	Disulfide bond	140 ↔ 151		By similarity
	Disulfide bond	147 ↔ 160		By similarity
	Disulfide bond	162 ↔ 175		By similarity
	Disulfide bond	183 ↔ 318		Interchain (between light and heavy chains) By similarity
	Disulfide bond	237 ↔ 253		By similarity
	Disulfide bond	368 ↔ 382		By similarity
	Disulfide bond	393 ↔ 421		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q28278-1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 7AD3A8C1C34E59FF	FASTA	456	50,814
	10 20 30 40 50 60 MWQLASLSLL LTICGTCSTA APPGSVFSSS ESAHQVLRIR KRANSFLEEI RAGSLERECM 70 80 90 100 110 120 EEICDFEEAK EIFQNVDDTL AYWSKYVDGD QCAALPPEHA CDSPCCGHGS CIDGIGAFHC 130 140 150 160 170 180 DCGRGWEGRF CQHEVSYINC SLDNGGCSHY CLEEEGGRHC SCAPGYRLGD DHLQCQPAVK 190 200 210 220 230 240 FPCGRPGKQM EKKRKHLKRD TNQTDQIDPR LVNGKVTRRG ESPWQVVLLD SKKKLACGAV 250 260 270 280 290 300 LIHTSWVLTA AHCMEDSKKL IVRLGEYDLR RWEKGEMDVD IKEVLIHPNY SKSTTDNDIA 310 320 330 340 350 360 LLHLAQPAIF SQTIVPICLP DSGLAERELT QVGQETVVTG WGYRSETKRN RTFVLNFINI 370 380 390 400 410 420 PVAPHNECIQ AMYNMISENM LCAGILGDSR DACEGDSGGP MVTSFRGTWF LVGLVSWGEG 430 440 450 CGRLHNYGIY TKVSRYLDWI HSHIRGEEAS LENQVP

References

[1]	"Molecular characterization and chromosomal assignment of the canine protein C gene." Leeb T., Kopp T., Deppe A., Breen M., Matis U., Brunnberg L., Brenig B. Mamm. Genome 10:134-139(1999) [PubMed: 9922393] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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] OF 273-429.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ001979 Genomic DNA. Translation: CAA05126.1. D43751 Genomic DNA. Translation: BAA07808.1.
RefSeq	NP_001013871.1.
UniGene	Cfa.6331
3D structure databases
HSSP	HSSP built from PDB template 1AUT based on UniProtKB P04070.
SMR	Q28278. Positions 91-186, 211-445.
ModBase	Search...
Protein family/group databases
MEROPS	S01.218.
Genome annotation databases
GeneID	476104.
KEGG	cfa:476104.
Phylogenomic databases
HOVERGEN	Q28278.
Enzyme and pathway databases
BRENDA	3.4.21.69. 463.
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_CANFA

Accession

Primary (citable) accession number: Q28278
Secondary accession number(s): Q9TTR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 7, 2004
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)