ID   A0A3B4T4X5_SERDU        Unreviewed;       759 AA.
AC   A0A3B4T4X5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=ADAM metallopeptidase domain 23 {ECO:0000313|Ensembl:ENSSDUP00000001094.1};
GN   Name=ADAM23 {ECO:0000313|Ensembl:ENSSDUP00000001094.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000001094.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000001094.1}
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:PRU00276}.
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DR   AlphaFoldDB; A0A3B4T4X5; -.
DR   Ensembl; ENSSDUT00000001141.1; ENSSDUP00000001094.1; ENSSDUG00000000744.1.
DR   GeneTree; ENSGT00940000158781; -.
DR   Proteomes; UP000261420; 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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00068}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..759
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017221982"
FT   DOMAIN          251..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   DISULFID        511..531
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   759 AA;  84258 MW;  11D5DF7E6B1F9A16 CRC64;
     MHLIFLATLL VSTLSPWLHP SLASFVSPGV EDKVERDAVA ALLKQQATAA PATDNTTHHA
     VEHEITYPSR LIYYLNEDSE STYHDLDTRA KNQATEGQAI HLAQASFQLE AFGSRFVLDL
     MLNNDLLSSD YVEIHYEGGK PVLSKGGEHC YYHGQVRGND NSHVALSTCN GLHGMFDDGV
     YVYLIEPLEQ THSIDTAARP HKLRRAASLH WNNDSEEQVE EEQLFSELDD LSWLKRRKKR
     AIPRSVFEEM KYLEIMIVSD HNMYKRHKTK QHTRNFAKSV VNLVDAIFKE QLHTRVVLVA
     VEVWTDKDQI PISVRPLEIL RDFSKYRQQS IKHHADAVHL FSNVTFHYRR SNAAYFGGAC
     SLSRGVGVNE YGTTGSMAVS LSQSLAQNLG IQWDPASRRK ECGCADSWTG CIMEDTGVQH
     PRRFSKCSIS DYKEFLLKGG GSCLFNRPTK LFETTECGNG FVEVGEECDC GGRSECYKEC
     CKKCSLANGA HCSDGPCCNN TCLFLPRGCT CRFAVNDCDI SETCSGDSGQ CPPNLHKQDG
     YLCQVNQGRC YSGECKTREN QCKYIWGSKA GGSEKFCYEK LNTEGTEKGN CGKDGEKWIQ
     CSKHDVFCGY LLCTNIGSSP RIGIMKGEST TTYFNYKNGK IDCSGGHVLL DDDTDLGYVE
     DGTPCGPSMM CLDRKCLPIQ SLNMSTCPTG PNGQVCSAHG VCNNEATCTC DTTWAGTDCS
     MPDPPKEPEA TPDEGPKVSL LELSQHRFLD LSFTGVLVP
//