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P33587 (PROC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:Proc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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 Potential
Propeptide19 – 4123 By similarity
PRO_0000028112
Chain42 – 460419Vitamin K-dependent protein C
PRO_0000028113
Chain42 – 196155Vitamin K-dependent protein C light chain By similarity
PRO_0000028114
Chain199 – 460262Vitamin K-dependent protein C heavy chain By similarity
PRO_0000028115
Peptide199 – 21214Activation peptide By similarity
PRO_0000028116

Regions

Domain42 – 8746Gla
Domain96 – 13136EGF-like 1
Domain135 – 17541EGF-like 2
Domain213 – 449237Peptidase S1

Sites

Active site2531Charge relay system
Active site2991Charge relay system
Active site4011Charge relay system
Site212 – 2132Cleavage; 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 residue7614-carboxyglutamate By similarity
Modified residue1121(3R)-3-hydroxyaspartate By similarity
Glycosylation2141N-linked (GlcNAc...) Ref.6
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3541N-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 ↔ 319Interchain (between light and heavy chains) By similarity
Disulfide bond238 ↔ 254 By similarity
Disulfide bond372 ↔ 386 By similarity
Disulfide bond397 ↔ 425 By similarity

Natural variations

Natural variant3271Q → QQ in strain: BALB/c.
Natural variant3921D → N in strain: BALB/c.

Experimental info

Sequence conflict651F → L in AAK07918. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P33587 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 0117F26E68FCC274

FASTA46051,818
        10         20         30         40         50         60 
MWQFRVFLLL MSTWGISSIP AHPDPVFSSS EHAHQVLRVR RANSFLEEMR PGSLERECME 

        70         80         90        100        110        120 
EICDFEEAQE IFQNVEDTLA FWIKYFDGDQ CSAPPLDHQC DSPCCGHGTC IDGIGSFSCS 

       130        140        150        160        170        180 
CDKGWEGKFC QQELRFQDCR VNNGGCLHYC LEESNGRRCA CAPGYELADD HMRCKSTVNF 

       190        200        210        220        230        240 
PCGKLGRWIE KKRKILKRDT DLEDELEPDP RIVNGTLTKQ GDSPWQAILL DSKKKLACGG 

       250        260        270        280        290        300 
VLIHTSWVLT AAHCVEGTKK LTVRLGEYDL RRRDHWELDL DIKEILVHPN YTRSSSDNDI 

       310        320        330        340        350        360 
ALLRLAQPAT LSKTIVPICL PNNGLAQELT QAGQETVVTG WGYQSDRIKD GRRNRTFILT 

       370        380        390        400        410        420 
FIRIPLVARN ECVEVMKNVV SENMLCAGII GDTRDACDGD SGGPMVVFFR GTWFLVGLVS 

       430        440        450        460 
WGEGCGHTNN YGIYTKVGSY LKWIHSYIGE KGVSLKSQKL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a mouse protein C cDNA."
Tada N., Sato M., Tsujimura A., Iwase R., Hashimoto-Gotoh T.
J. Biochem. 111:491-495(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Nucleotide structure and characterization of the murine gene encoding anticoagulant protein C."
Jalbert L.R., Rosen E.D., Lissens A., Carmeliet P., Collen D., Castellino F.J.
Thromb. Haemost. 79:310-316(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[3]"Complete sequence of UC72A01."
Korf I.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 274-433.
Strain: BALB/c.
[6]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-214.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10445 mRNA. Translation: BAA01235.1.
AF034569 Genomic DNA. Translation: AAC33795.1.
AF318182 mRNA. Translation: AAK07918.1.
BC013896 mRNA. Translation: AAH13896.1.
D43755 Genomic DNA. Translation: BAA07812.1.
CCDSCCDS29116.1.
PIRJX0210.
RefSeqNP_001036232.1. NM_001042767.2.
NP_001036233.2. NM_001042768.2.
NP_032960.3. NM_008934.3.
UniGeneMm.2786.
Mm.489734.

3D structure databases

ProteinModelPortalP33587.
SMRP33587. Positions 46-87, 90-184, 212-448.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.218.

PTM databases

PhosphoSiteP33587.

Proteomic databases

PaxDbP33587.
PRIDEP33587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000171765; ENSMUSP00000132226; ENSMUSG00000024386.
GeneID19123.
KEGGmmu:19123.
UCSCuc008eiz.1. mouse.

Organism-specific databases

CTD5624.
MGIMGI:97771. Proc.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00750000117249.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidP33587.
KOK01344.
OMAPNYSKST.
OrthoDBEOG75B84T.
PhylomeDBP33587.
TreeFamTF327329.

Gene expression databases

BgeeP33587.
CleanExMM_PROC.
GenevestigatorP33587.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 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...

Other

ChiTaRSPROC. mouse.
NextBio295718.
PROP33587.
SOURCESearch...

Entry information

Entry namePROC_MOUSE
AccessionPrimary (citable) accession number: P33587
Secondary accession number(s): O35498, Q91WN8, Q99PC6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot