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  Coagulation factor II

SourceMus musculus (house mouse)
Taxonomy Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Keywords3D-structure; Acute phase; Blood coagulation; Calcium; Cleavage on pair of basic residues; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Kringle; Protease; Repeat; Serine protease; Signal; Zymogen.
Details
Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).

Post-translational modification: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.

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

Sequence length: 618 AA.

Sequence
MSHVRGLGLPGCLALAALVSLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERE
CVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGVNYLGT
VNVTHTGIQCQLWRSRYPHKPEINSTTHPGADLKENFCRNPDSSTTGPWCYTTDPTVRRE
ECSVPVCGQEGRTTVVMTPRSGGSKDNLSPPLGQCLTERGRLYQGNLAVTTLGSPCLPWN
SLPAKTLSKYQDFDPEVKLVENFCRNPDWDEEGAWCYVAGQPGDFEYCNLNYCEEAVGEE
NYDVDESIAGRTTDAEFHTFFNEKTFGLGEADCGLRPLFEKKSLKDTTEKELLDSYIDGR
IVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLL
VRIGKHSRTRYERNVEKISMLEKIYVHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCL
PDKQTVTSLLRAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIR
ITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRKGKYGFY
THVFRLKRWIQKVIDQFG
Accession NumberP19221 
PubMed ID2222810, 15489334, 1557383, 17330941, 17428793, 17606903 
CEX DBMM_F2
CTD DB14061
Ensembl DBENSMUST00000028681
CATHG3DSA:2.40.20.10, G3DSA:4.10.140.10
GeneID DB14061
GermOnline DBENSMUSG00000027249
GO DB0005576, 0005509, 0006953, 0030168, 0006508
HOGENOM DBHBG446798
InterPro DBIPR002383, IPR000294, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR012051, IPR003966, IPR009003, IPR018992
IPI DBIPI00114206
KEGGmmu:14061
NCBIX52308, CAA36548, BC013662, AAH13662, M81394, AAA40435, NP_034298
OMAGIECQLW
OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367
OrthoDBEOG90044C
PDB2OCV_A, 2OCV_B, 2PUX_A, 2PUX_B, 2PV9_A, 2PV9_B, 3EDX_A, 3EDX_C, 3EDX_E, 3EDX_B, 3EDX_D, 3EDX_F, 3HK3_A, 3HK3_B, 3HK6_A, 3HK6_C, 3HK6_B, 3HK6_D, 3HKI_A, 3HKI_D, 3HKI_B, 3HKI_E
PfamPF00594, PF00051, PF09396, PF00089
PROSITE DBPS00011, PS50998, PS00021, PS50070, PS50240, PS00134, PS00135
SMART DBSM00069, SM00130, SM00020
UCSCuc008kwg.1
UniGeneMm.89048



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