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Q9GLP2 (PROC_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. Vitamin K-dependent protein C light chain
  2. Vitamin K-dependent protein C heavy chain
  3. Activation peptide
Gene names
Name:PROC
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Propeptide19 – 4123 By similarity
PRO_0000028117
Chain42 – 459418Vitamin K-dependent protein C
PRO_0000028118
Chain42 – 196155Vitamin K-dependent protein C light chain By similarity
PRO_0000028119
Chain199 – 459261Vitamin K-dependent protein C heavy chain By similarity
PRO_0000028120
Peptide199 – 21315Activation peptide By similarity
PRO_0000028121

Regions

Domain42 – 8746Gla
Domain96 – 13136EGF-like 1
Domain135 – 17541EGF-like 2
Domain214 – 448235Peptidase S1

Sites

Active site2551Charge relay system
Active site3011Charge relay system
Active site4001Charge relay system
Site213 – 2142Cleavage; by thrombin By similarity

Amino acid modifications

Modified residue4714-carboxyglutamate By similarity
Modified residue4814-carboxyglutamate By similarity
Modified residue5514-carboxyglutamate By similarity
Modified residue5714-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6114-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6714-carboxyglutamate By similarity
Modified residue7014-carboxyglutamate By similarity
Modified residue1121(3R)-3-hydroxyaspartate By similarity
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 63 By similarity
Disulfide bond91 ↔ 110 By similarity
Disulfide bond100 ↔ 105 By similarity
Disulfide bond104 ↔ 119 By similarity
Disulfide bond121 ↔ 130 By similarity
Disulfide bond139 ↔ 150 By similarity
Disulfide bond146 ↔ 159 By similarity
Disulfide bond161 ↔ 174 By similarity
Disulfide bond182 ↔ 321Interchain (between light and heavy chains) By similarity
Disulfide bond240 ↔ 256 By similarity
Disulfide bond371 ↔ 385 By similarity
Disulfide bond396 ↔ 424 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GLP2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8541AAC14CC16D09

FASTA45951,867
        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

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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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF191307 mRNA. Translation: AAG28380.1.
RefSeqNP_999083.1. NM_213918.1.
UniGeneSsc.2763.

3D structure databases

ProteinModelPortalQ9GLP2.
SMRQ9GLP2. Positions 43-87, 90-185, 214-448.
ModBaseSearch...

Protein family/group databases

MEROPSS01.218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396954.
KEGGssc:396954.

Organism-specific databases

CTD5624.

Phylogenomic databases

HOVERGENHBG013304.

Family and domain databases

InterProIPR017857. 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]
Gene3DG3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
KOK01344.
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 2 hits.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Entry information

Entry namePROC_PIG
AccessionPrimary (citable) accession number: Q9GLP2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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