ID A0A1L8D683_BOTAT Unreviewed; 409 AA. AC A0A1L8D683; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 08-NOV-2023, entry version 25. DE SubName: Full=BATXSVMPI1 {ECO:0000313|EMBL:JAV01877.1}; OS Bothrops atrox (Barba amarilla) (Fer-de-lance). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops. OX NCBI_TaxID=8725 {ECO:0000313|EMBL:JAV01877.1}; RN [1] {ECO:0000313|EMBL:JAV01877.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tapajos National Forest {ECO:0000313|EMBL:JAV01877.1}; RC TISSUE=Venom gland {ECO:0000313|EMBL:JAV01877.1}; RA Amazonas D.R., Nishiyama M.Y.Jr., Gibbs H.L., Rokyta D.R., RA Junqueira-de-Azevedo I.L., Moura-da-Silva A.M.; RT "Transcriptomic analysis of venom glands from five Bothrops atrox snakes."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. 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; GEDR01000085; JAV01877.1; -; mRNA. DR AlphaFoldDB; A0A1L8D683; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1. DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00276}; Hydrolase {ECO:0000256|ARBA:ARBA00023049}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..409 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5012996123" FT DOMAIN 193..389 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT ACT_SITE 330 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 333 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 339 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT DISULFID 304..384 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT DISULFID 344..368 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" FT DISULFID 346..351 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276" SQ SEQUENCE 409 AA; 46041 MW; F636A91EF4CA894A CRC64; MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK VNGEPVVLHL EKNKGLFSKD YSEIHYSPDG REITTYPPVE DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VFKFENVEKE DEAPKMCGVT QNWESYEPIK KASQSNLTPE QQRYVELFVV VDHGMFMKYN GNSDKIRRRI HQMVNIMKEI YSTMYIDIFL TGVEIWSNKD LINVQPAAPQ TLDSFGEWRK TDLLNRKSHD NAQLLTSTDF NGPTIGLAYV GSMCDPKRST GVIQDHSPIN LMVAVTMAHE LGHNLGISHD TGSCSCGGYS CIMSPVLSHE PSKYFSDCSY IQCWDFIMKE NPQCILNKRL RTDTVSTPVS GNQLLEAGE //