ID A0A3B4CX71_PYGNA Unreviewed; 779 AA.
AC A0A3B4CX71;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 23-like {ECO:0000313|Ensembl:ENSPNAP00000015955.1};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSPNAP00000015955.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000015955.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000015955.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_017547815.1; XM_017692326.1.
DR AlphaFoldDB; A0A3B4CX71; -.
DR Ensembl; ENSPNAT00000037932.1; ENSPNAP00000015955.1; ENSPNAG00000022084.1.
DR GeneID; 108424345; -.
DR GeneTree; ENSGT00940000158781; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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:SF13; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 23; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..779
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017229816"
FT DOMAIN 250..448
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 454..539
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 683..720
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 719..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 511..531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 710..719
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 779 AA; 87076 MW; 7FD6CD71208B9C74 CRC64;
MWLRFLSHLI VSVLVSGLRS SISTTSLVEN EPSEDAVSVR VEQDAIAPAH TQNRSGQEVE
HTITYPSRLI YYLNEDSEST YHNLNTWAKT PGQQGQVVHL AQATFQLEAF GYRFILDLTL
NNDLLSSDYV EIHYEDNKTI QSKGGEHCYY RGQVRGVEAS RVAMSTCNGL HGMFDDGVHV
YLIEPLKQTH SIDGAARPHI LRRTPSLLQS HEPEDGGNKE ELLFSELNHM SWLRRRKKRA
MPRNVFEEMK YIELMIVSDH NMFKRQKTKQ QTRNFAKSVV NLVDAIFKEH LNTRVVLVAM
EIWTDKDHIP ISVMPLDMLR DFSKYRQQHI KQHADAVHLF SNVTFHYRQS SAAFFGGMCS
MSRGVGVNEY GSTWTMAVSL SQSLAQNLGI RWDPAARKSK ECGCVDSWVG CIMEDTGVQH
PRKFSKCSIS DYKEFLLKGG GSCLFNRPTK LFEPTECGNG YMEVGEECDC GVRAECYKEC
CKKCSLSNGA HCSDGPCCNN TCLFYPRGYS CRYAVNDCDI SETCSGDSGQ CPPNLHKQDG
YFCHLNQGRC YSGECKTRES QCKYVWGPKS GSSEKFCYEK LNTEGSHKGN CGENGEKYIQ
CSKHDVFCGL LLCTNVGQMP RIGLIKGEIT PTTFNHQGQL IECSGGHVLL DDDTDLGYVE
DGTPCGPSMM CLDRKCLPIQ SLNMSACPTG PSGHICSNHG VCNNEATCTC DVTWAGTDCS
MPDPPKEPPP SEDEGPKEMS KSDGTTRMPV PSSGERRTRP SVASLVYSWT AIIAALFWH
//