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  Protein C

SourceMus musculus (house mouse)
Taxonomy Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
KeywordsBlood coagulation; Calcium; Cleavage on pair of basic residues; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Serine protease; Signal; Zymogen.
Details
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.

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).

Similarity: Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain.

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.

Sequence length: 460 AA.

Sequence
MWQFRVFLLLMSTWGISSIPAHPDPVFSSSEHAHQVLRVRRANSFLEEMRPGSLERECME
EICDFEEAQEIFQNVEDTLAFWIKYFDGDQCSAPPLDHQCDSPCCGHGTCIDGIGSFSCS
CDKGWEGKFCQQELRFQDCRVNNGGCLHYCLEESNGRRCACAPGYELADDHMRCKSTVNF
PCGKLGRWIEKKRKILKRDTDLEDELEPDPRIVNGTLTKQGDSPWQAILLDSKKKLACGG
VLIHTSWVLTAAHCVEGTKKLTVRLGEYDLRRRDHWELDLDIKEILVHPNYTRSSSDNDI
ALLRLAQPATLSKTIVPICLPNNGLAQELTQAGQETVVTGWGYQSDRIKDGRRNRTFILT
FIRIPLVARNECVEVMKNVVSENMLCAGIIGDTRDACDGDSGGPMVVFFRGTWFLVGLVS
WGEGCGHTNNYGIYTKVGSYLKWIHSYIGEKGVSLKSQKL
Accession NumberP33587 
PubMed ID1618739, 9493582, 15489334, 8043441, 16944957 
CEX DBMM_PROC
CTD DB19123
eggNOG DBroNOG10647
Ensembl DBENSMUST00000025245
GeneID DB19123
GermOnline DBENSMUSG00000024386
GO DB0005509, 0004252, 0007596, 0043066, 0030195, 0006508
HOGENOM DBHBG715028
InterPro DBIPR002383, IPR006210, IPR013032, IPR000152, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003
IPI DBIPI00113750
KEGGmmu:19123
NCBID10445, BAA01235, AF034569, AAC33795, AF318182, AAK07918, BC013896, AAH13896, D43755, BAA07812, NP_032960.2
NMPDR fig|10090.3.peg.3736
OMAEICDFEE
OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600, 176860, 188050, 612283, 612304
OrthoDBEOG9QRKPC
PfamPF00594, PF00089
PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135
SMART DBSM00181, SM00179, SM00069, SM00020
UCSCuc008eiz.1
UniGeneMm.2786



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