ID B3XZY8_LETCA Unreviewed; 471 AA. AC B3XZY8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-OCT-2015, entry version 51. DE SubName: Full=Coagulation factor X-2 {ECO:0000313|EMBL:BAG66072.1}; GN Name=Factor X-2 {ECO:0000313|EMBL:BAG66072.1}; OS Lethenteron camtschaticum (Japanese lamprey) (Lampetra japonica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Lethenteron. OX NCBI_TaxID=980415 {ECO:0000313|EMBL:BAG66072.1}; RN [1] {ECO:0000313|EMBL:BAG66072.1} RP NUCLEOTIDE SEQUENCE. RA Kimura A., Ikeo K., Nonaka M.; RT "Evolutionary origin of the vertebrate blood complement and RT coagulation systems inferred from liver EST analysis of lamprey."; RL Dev. Comp. Immunol. 33:77-87(2009). CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|RuleBase:RU000360}. CC -!- SIMILARITY: Contains Gla (gamma-carboxy-glutamate) domain. CC {ECO:0000256|SAAS:SAAS00139184}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB377286; BAG66072.1; -; mRNA. DR ProteinModelPortal; B3XZY8; -. DR MEROPS; S01.216; -. DR HOVERGEN; HBG013304; -. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0007596; P:blood coagulation; IEA:InterPro. DR Gene3D; 4.10.740.10; -; 1. DR InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR012224; Pept_S1A_FX. DR InterPro; IPR018114; Peptidase_S1_AS. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR Pfam; PF00008; EGF; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001143; Factor_X; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR SMART; SM00181; EGF; 2. DR SMART; SM00069; GLA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57630; SSF57630; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00145227}; KW EGF-like domain {ECO:0000256|RuleBase:RU000460, KW ECO:0000256|SAAS:SAAS00145385}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 471 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002800769. FT COILED 49 69 {ECO:0000256|SAM:Coils}. FT ACT_SITE 260 260 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001143-1}. FT ACT_SITE 305 305 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001143-1}. FT ACT_SITE 401 401 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001143-1}. SQ SEQUENCE 471 AA; 53044 MW; 3064D96951D698E4 CRC64; MALSSATFVL LIGSIIPMTL CAVFLEKQDA GQVLSRLRRA NSAFEELRAA NLERECNEER CSIEEAMEIF KNKELANDFW NTYVDGNQCD PNQCLNNGIC KDGVKMYTCI CPNGFEGNNC ELTKIGCVFR NGGCNHFCLD QENKAPVCTC VKGYRLQDDG HTCEPVEAFP CGRLHPEEIR AKREENRRDE FSTSHSDENL KTQPHNTSSI KEQREDVKSI AGGMDCPRGD CPWQALVKLE NNLYCGGTIL NLEWILTAAH CVPLKPWNVV VGEHNLRVTE SSEQHVPIKN IVVHSRYDPI TFDNDLALLQ LERPLNFSRL VLPACLPERD FADKVLVEEQ SRISGWGSLH HRGIKATVLQ IAEVPFVDTL RCKESSSSLV TKNMFCAGYS DGTKDACQHD SGGPHVTIFK DTWFATGIIS WGEGCARKGK YGVYTRVSRY LLWMHQVMQR ASIYQLEIPT RGIRFTRNPL A //