ID A0A3B4EC74_PYGNA Unreviewed; 782 AA.
AC A0A3B4EC74;
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:ENSPNAP00000033435.1};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSPNAP00000033435.1};
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:ENSPNAP00000033435.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000033435.1}
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_017547813.1; XM_017692324.1.
DR AlphaFoldDB; A0A3B4EC74; -.
DR STRING; 42514.ENSPNAP00000033435; -.
DR Ensembl; ENSPNAT00000024325.1; ENSPNAP00000033435.1; 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, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..782
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017439606"
FT TRANSMEM 744..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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..741
FT /note="Disordered"
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 782 AA; 86935 MW; D89E2D9828B7E4E2 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 SEDEGPKGPS ATNLIIGSIA GAILVAAIVL GGTGWGFKNV KKRRYDPNAS
AI
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