ID B3XZY8_LETCA Unreviewed; 471 AA. AC B3XZY8; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 24-JUL-2024, entry version 87. DE RecName: Full=coagulation factor Xa {ECO:0000256|ARBA:ARBA00012181}; DE EC=3.4.21.6 {ECO:0000256|ARBA:ARBA00012181}; 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 coagulation RT systems inferred from liver EST analysis of lamprey."; RL Dev. Comp. Immunol. 33:77-87(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in CC prothrombin to form thrombin.; EC=3.4.21.6; CC Evidence={ECO:0000256|ARBA:ARBA00001239}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. 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 AlphaFoldDB; B3XZY8; -. DR MEROPS; S01.216; -. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. 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 GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IEA:TreeGrafter. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1. DR Gene3D; 2.10.25.10; Laminin; 2. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR012224; Pept_S1A_FX. DR InterPro; IPR050442; Peptidase_S1_coag_factors. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR PANTHER; PTHR24278; COAGULATION FACTOR; 1. DR PANTHER; PTHR24278:SF28; COAGULATION FACTOR X; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF14670; FXa_inhibition; 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; SM00179; EGF_CA; 1. DR SMART; SM00069; GLA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF57630; GLA-domain; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00076}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE- KW ProRule:PRU00076}; KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..471 FT /note="coagulation factor Xa" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002800769" FT DOMAIN 39..85 FT /note="Gla" FT /evidence="ECO:0000259|PROSITE:PS50998" FT DOMAIN 85..121 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 220..449 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" FT REGION 182..214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..196 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 260 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1" FT ACT_SITE 305 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1" FT ACT_SITE 401 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1" FT DISULFID 111..120 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" 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 //