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Q28278 (PROC_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. 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 2 chains:

  1. Vitamin K-dependent protein C light chain
  2. Vitamin K-dependent protein C heavy chain
Gene names
Name:PROC
OrganismCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length456 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4222 By similarity
PRO_0000028103
Chain43 – 456414Vitamin K-dependent protein C
PRO_0000028104
Chain43 – 197155Vitamin K-dependent protein C light chain
PRO_0000028105
Chain200 – 456257Vitamin K-dependent protein C heavy chain
PRO_0000028106

Regions

Domain47 – 8842Gla
Domain97 – 13236EGF-like 1
Domain136 – 17641EGF-like 2
Domain211 – 445235Peptidase S1

Sites

Active site2521Charge relay system By similarity
Active site2981Charge relay system By similarity
Active site3971Charge relay system By similarity

Amino acid modifications

Modified residue4814-carboxyglutamate By similarity
Modified residue4914-carboxyglutamate By similarity
Modified residue5614-carboxyglutamate By similarity
Modified residue5814-carboxyglutamate By similarity
Modified residue6114-carboxyglutamate By similarity
Modified residue6214-carboxyglutamate By similarity
Modified residue6714-carboxyglutamate By similarity
Modified residue6814-carboxyglutamate By similarity
Modified residue7114-carboxyglutamate By similarity
Modified residue1131(3R)-3-hydroxyaspartate By similarity
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 64 By similarity
Disulfide bond92 ↔ 111 By similarity
Disulfide bond101 ↔ 106 By similarity
Disulfide bond105 ↔ 120 By similarity
Disulfide bond122 ↔ 131 By similarity
Disulfide bond140 ↔ 151 By similarity
Disulfide bond147 ↔ 160 By similarity
Disulfide bond162 ↔ 175 By similarity
Disulfide bond183 ↔ 318Interchain (between light and heavy chains) By similarity
Disulfide bond237 ↔ 253 By similarity
Disulfide bond368 ↔ 382 By similarity
Disulfide bond393 ↔ 421 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28278 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 7AD3A8C1C34E59FF

FASTA45650,814
        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

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ001979 Genomic DNA. Translation: CAA05126.1.
D43751 Genomic DNA. Translation: BAA07808.1.
RefSeqNP_001013871.1. NM_001013849.1.
UniGeneCfa.6331.

3D structure databases

ProteinModelPortalQ28278.
SMRQ28278. Positions 44-88, 91-186, 211-445.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28278.

Protein family/group databases

MEROPSS01.218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID476104.
KEGGcfa:476104.

Organism-specific databases

CTD5624.

Phylogenomic databases

eggNOGmaNOG17466.
HOVERGENHBG013304.
PhylomeDBQ28278.

Family and domain databases

InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
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.
PfamPF00594. 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_CANFA
AccessionPrimary (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: November 16, 2011
This is version 93 of the entry and version 2 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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