Result Untitled Document Coagulation factor XSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Blood coagulation; Calcium; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.DetailsFunction: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. N- and O-glycosylated. The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Similarity: Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain. Subcellular location: Secreted. Subunit structure: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Tissue specificity: Plasma; synthesized in the liver. Interaction: Q16938:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646299; Q964Q0:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646347; P04133:PII (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646019. Sequence length: 488 AA. SequenceMGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLKAccession NumberP00742 PubMed ID1902434, 3768336, 15489334, 2582420, 3011603, 6871167, 6587384, 8243461, 2612918, 8355279, 9618463, 17227710, 10391209 CEX DBHS_F10CTD DB2159DIP DBDIP-29896NeggNOG DBprNOG09450Ensembl DBENST00000375559Genecard DBGC13P112825GeneID DB2159GermOnline DBENSG00000126218GO DB0005576, 0031233, 0005509, 0005543, 0005515, 0004252, 0007598, 0030335, 0051897, 0006508HGNC DB3528HOGENOM DBHBG715028InterPro DBIPR002383, IPR006209, IPR006210, IPR013032, IPR000152, IPR000742, IPR001881, IPR018097, IPR000294, IPR012224, IPR018114, IPR001254, IPR001314, IPR009003H-InvDBHIX0026566IPI DBIPI00019576KEGGhsa:2159NCBIK03194, AAA52490, M57285, AAA52421, AF503510, AAM19347, BC046125, AAH46125, N00045, AAA52764, L00390, L00391, L00392, L00393, L00394, L00395, L00396, M22613, AAA51984, K01886, AAA52486, M33297, AAA52636, NP_000495OMAPACLPQKOMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600Orphanet DB328OrthoDBEOG9QRKPCPDB1C5M_D, 1C5M_F, 1EZQ_A, 1EZQ_B, 1F0R_A, 1F0R_B, 1F0S_A, 1F0S_B, 1FAX_A, 1FAX_L, 1FJS_A, 1FJS_L, 1FXY_A, 1G2L_A, 1G2L_B, 1G2M_A, 1G2M_B, 1HCG_A, 1HCG_B, 1IOE_A, 1IOE_L, 1IQE_A, 1IQE_L, 1IQF_A, 1IQF_L, 1IQG_A, 1IQG_L, 1IQH_A, 1IQH_L, 1IQI_A, 1IQI_L, 1IQJ_A, 1IQJ_L, 1IQK_A, 1IQK_L, 1IQL_A, 1IQL_L, 1IQM_A, 1IQM_L, 1IQN_A, 1IQN_L, 1KSN_A, 1KSN_B, 1KYE_A, 1KYE_B, 1LPG_A, 1LPG_B, 1LPK_A, 1LPK_B, 1LPZ_A, 1LPZ_B, 1LQD_A, 1LQD_B, 1MQ5_A, 1MQ5_L, 1MQ6_A, 1MQ6_L, 1MSX_A, 1NFU_A, 1NFU_B, 1NFW_A, 1NFW_B, 1NFX_A, 1NFX_B, 1NFY_A, 1NFY_B, 1NL8_F, 1NL8_L, 1P0S_H, 1P0S_L, 1V3X_A, 1V3X_B, 1WU1_A, 1WU1_B, 1XKA_C, 1XKA_L, 1XKB_A, 1XKB_B, 1XKB_C, 1XKB_D, 1Z6E_A, 1Z6E_B, 2BMG_A, 2BMG_B, 2BOH_A, 2BOH_B, 2BOK_A, 2BOK_L, 2BQ6_A, 2BQ6_B, 2BQ7_A, 2BQ7_B, 2BQW_A, 2BQW_B, 2CJI_A, 2CJI_B, 2D1J_A, 2D1J_B, 2EI6_A, 2EI6_B, 2EI7_A, 2EI7_B, 2EI8_A, 2EI8_B, 2FZZ_A, 2FZZ_L, 2G00_A, 2G00_L, 2GD4_A, 2GD4_L, 2GD4_B, 2GD4_H, 2H9E_H, 2H9E_L, 2J2U_A, 2J2U_B, 2J34_A, 2J34_B, 2J38_A, 2J38_B, 2J4I_A, 2J4I_B, 2J94_A, 2J94_B, 2J95_A, 2J95_B, 2JKH_A, 2JKH_L, 2P16_A, 2P16_L, 2P3F_H, 2P3F_L, 2P3T_A, 2P3T_B, 2P3U_A, 2P3U_B, 2P93_A, 2P93_L, 2P94_A, 2P94_L, 2P95_A, 2P95_L, 2PHB_A, 2PHB_B, 2PR3_A, 2PR3_B, 2Q1J_A, 2Q1J_B, 2RA0_A, 2RA0_L, 2UWL_A, 2UWL_B, 2UWO_A, 2UWO_B, 2UWP_A, 2UWP_B, 2VH0_A, 2VH0_B, 2VH6_A, 2VH6_B, 2VVC_A, 2VVC_B, 2VVC_K, 2VVC_L, 2VVU_A, 2VVU_L, 2VVV_A, 2VVV_L, 2VWL_A, 2VWL_L, 2VWM_A, 2VWM_B, 2VWM_K, 2VWM_L, 2VWN_A, 2VWN_L, 2VWO_A, 2VWO_L, 2W26_A, 2W26_B, 2W3I_A, 2W3I_B, 2W3K_A, 2W3K_B, 3CEN_A, 3CEN_L, 3CS7_A, 3CS7_L, 3ENS_A, 3ENS_C, 3ENS_B, 3ENS_D, 3HPT_A, 3HPT_C, 3HPT_B, 3HPT_D, 3KL6_A, 3KL6_BPfamPF00008, PF00594, PF00089PharmaGKBPA24967PROSITE DBPS00010, PS00022, PS01186, PS50026, PS01187, PS00011, PS50998, PS50240, PS00134, PS00135SMART DBSM00181, SM00179, SM00069, SM00020UCSCuc001vsx.1UniGeneHs.361463
Result
Coagulation factor X
Function: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. Post-translational modification: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. N- and O-glycosylated. The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Similarity: Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain. Subcellular location: Secreted. Subunit structure: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Tissue specificity: Plasma; synthesized in the liver. Interaction: Q16938:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646299; Q964Q0:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646347; P04133:PII (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646019. Sequence length: 488 AA.
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
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