Vitamin K-dependent protein C precursor

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P00745 (PROC_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Vitamin K-dependent protein C
EC=3.4.21.69

Alternative name(s):
Anticoagulant protein C
Autoprothrombin IIA
Blood coagulation factor XIV

Cleaved into the following 3 chains:

Vitamin K-dependent protein C light chain
Vitamin K-dependent protein C heavy chain
Activation peptide

Gene names

Name:

PROC

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	456 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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 – 29

›29

Propeptide

30 – 39

PRO_0000028098

Chain

40 – 456

417

Vitamin K-dependent protein C

PRO_0000028099

Chain

40 – 194

155

Vitamin K-dependent protein C light chain

PRO_0000028100

Chain

197 – 456

260

Vitamin K-dependent protein C heavy chain

PRO_0000028101

Peptide

197 – 210

Activation peptide

PRO_0000028102

Regions

Domain

40 – 85

Gla

Domain

94 – 129

EGF-like 1

Domain

133 – 173

EGF-like 2

Domain

211 – 445

235

Peptidase S1

Sites

Active site

252

Charge relay system

Active site

298

Charge relay system

Active site

397

Charge relay system

Amino acid modifications

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

110

(3R)-3-hydroxyaspartate

Glycosylation

136

N-linked (GlcNAc...) Ref.2

Glycosylation

289

N-linked (GlcNAc...) Ref.4

Glycosylation

350

N-linked (GlcNAc...) Ref.4

Glycosylation

366

N-linked (GlcNAc...); partial; atypical Ref.4

Disulfide bond

56 ↔ 61

By similarity

Disulfide bond

89 ↔ 108

By similarity

Disulfide bond

98 ↔ 103

By similarity

Disulfide bond

102 ↔ 117

By similarity

Disulfide bond

119 ↔ 128

By similarity

Disulfide bond

137 ↔ 148

By similarity

Disulfide bond

144 ↔ 157

By similarity

Disulfide bond

159 ↔ 172

By similarity

Disulfide bond

180 ↔ 318

Interchain (between light and heavy chains)

Disulfide bond

237 ↔ 253

Disulfide bond

368 ↔ 382

Disulfide bond

393 ↔ 421

Natural variations

Natural variant

F → K.

Experimental info

Sequence conflict

455 – 456

VP → PV AA sequence Ref.4

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

P00745 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: CAAF6833F894C209
Show »

FASTA

456

51,409

        10         20         30         40         50         60 
XTSLLLFVTI WGISSTPAPP DSVFSSSQRA HQVLRIRKRA NSFLEELRPG NVERECSEEV 

        70         80         90        100        110        120 
CEFEEAREIF QNTEDTMAFW SFYSDGDQCE DRPSGSPCDL PCCGRGKCID GLGGFRCDCA 

       130        140        150        160        170        180 
EGWEGRFCLH EVRFSNCSAE NGGCAHYCME EEGRRHCSCA PGYRLEDDHQ LCVSKVTFPC 

       190        200        210        220        230        240 
GRLGKRMEKK RKTLKRDTNQ VDQKDQLDPR IVDGQEAGWG ESPWQAVLLD SKKKLVCGAV 

       250        260        270        280        290        300 
LIHVSWVLTV AHCLDSRKKL IVRLGEYDMR RWESWEVDLD IKEVIIHPNY TKSTSDNDIA 

       310        320        330        340        350        360 
LLRLAKPATL SQTIVPICLP DSGLSERKLT QVGQETVVTG WGYRDETKRN RTFVLSFIKV 

       370        380        390        400        410        420 
PVVPYNACVH AMENKISENM LCAGILGDPR DACEGDSGGP MVTFFRGTWF LVGLVSWGEG 

       430        440        450 
CGRLYNYGVY TKVSRYLDWI YGHIKAQEAP LESQVP

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References

[1]	"Cloning and sequencing of liver cDNA coding for bovine protein C." Long G.L., Balagaje R.M., McGillivray R.T.A. Proc. Natl. Acad. Sci. U.S.A. 81:5653-5656(1984) [PubMed: 6091100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Amino acid sequence of the light chain of bovine protein C." Fernlund P., Stenflo J. J. Biol. Chem. 257:12170-12179(1982) [PubMed: 6896876] [Abstract] Cited for: PROTEIN SEQUENCE OF 40-194, GLYCOSYLATION AT ASN-136.
[3]	"Beta-hydroxyaspartic acid in vitamin K-dependent protein C." Drakenberg T., Fernlund P., Roepstorff P., Stenflo J. Proc. Natl. Acad. Sci. U.S.A. 80:1802-1806(1983) [PubMed: 6572939] [Abstract] Cited for: SEQUENCE REVISION TO 110.
[4]	"Amino acid sequence of the heavy chain of bovine protein C." Stenflo J., Fernlund P. J. Biol. Chem. 257:12180-12190(1982) [PubMed: 6896877] [Abstract] Cited for: PROTEIN SEQUENCE OF 197-456, GLYCOSYLATION AT ASN-289; ASN-350 AND ASN-366.
[5]	"Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C." Esmon N.L., Debault L.E., Esmon C.T. J. Biol. Chem. 258:5548-5553(1983) [PubMed: 6304092] [Abstract] Cited for: PROTEOLYTIC PROCESSING, CALCIUM-BINDING.
[6]	"Structural changes required for activation of protein C are induced by Ca2+ binding to a high affinity site that does not contain gamma-carboxyglutamic acid." Johnson A.E., Esmon N.L., Laue T.M., Esmon C.T. J. Biol. Chem. 258:5554-5560(1983) [PubMed: 6406503] [Abstract] Cited for: PROTEOLYTIC PROCESSING, CALCIUM-BINDING DATA.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K02435 mRNA. Translation: AAA30685.1.
IPI	IPI00713247.
PIR	KXBO. A26250.
UniGene	Bt.49146.
3D structure databases
ProteinModelPortal	P00745.
SMR	P00745. Positions 41-85, 88-183, 211-445.
ModBase	Search...
Protein-protein interaction databases
STRING	P00745.
Protein family/group databases
MEROPS	S01.218.
Proteomic databases
PRIDE	P00745.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG17466.
GeneTree	ENSGT00560000076714.
HOVERGEN	HBG013304.
InParanoid	P00745.
OrthoDB	EOG43BMNX.
Family and domain databases
InterPro	IPR017857. Coagulation_fac_subgr_Gla_dom. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR000742. EGF_3. IPR018097. EGF_Ca-bd_CS. IPR000294. GLA_domain. IPR009003. Pept_cys/ser_Trypsin-like. IPR012224. Pept_S1A_FX. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
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]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit. SSF57630. VitK_dep_GLA. 1 hit.
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. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P00745.

Entry information

Entry name

PROC_BOVIN

Accession

Primary (citable) accession number: P00745

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	November 16, 2011
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents