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Database: UniProt
Entry: A0A3B4CX71_PYGNA
LinkDB: A0A3B4CX71_PYGNA
Original site: A0A3B4CX71_PYGNA 
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
//
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