ID A0A3B1KK79_ASTMX Unreviewed; 780 AA.
AC A0A3B1KK79;
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:ENSAMXP00000055003.1};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSAMXP00000055003.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000055003.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000055003.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 AlphaFoldDB; A0A3B1KK79; -.
DR Ensembl; ENSAMXT00000057075.1; ENSAMXP00000055003.1; ENSAMXG00000007893.2.
DR GeneTree; ENSGT00940000158781; -.
DR InParanoid; A0A3B1KK79; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000007893; Expressed in bone element and 11 other cell types or tissues.
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; IPR013111; EGF_extracell.
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; PF07974; EGF_2; 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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
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..780
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017210051"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 250..447
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 453..538
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 682..719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 510..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 709..718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 780 AA; 86151 MW; BF9DB84A292049AC CRC64;
MWLRFLSHLL VSVLVSGLRS SITTALLVEN EPGGDAVSVR VEQDATAPTH TRNESGQEVE
QAITYPSRLI YFLNENSEST YHNLNTWAKT PGHQGQAVHL AQATFQLEAF GSRFILDLTL
NNDLLSSDYV EIHYEDGKPI LSKGGEHCYY SGQVRGVEAS RVALSTCNGL HGMFDDGVYV
YLIEPLKQTH SFEGAARPHT LRRTPSLLQS NDPQDEGDKV EPLLSELDDM SWLRRRKKRA
IPRNVFEEMK YIELMIVSDH NMFKRHKTKQ QTKNFAKSVV NLVDAVFKEH LNTRVVLVAV
EIWTDKDQIP ITVYPLEMLR NFSRYRQQHI KQHADAVHLF TNVTFHYHQS SIAFVGGMCS
VSHGVGVNEY GSTWTMAVSL SQSLAQNLGI RWDVTSKNKE CGCVDSWVGC IMEDTGVQHP
RKFSKCSISD YKEFLLKGGG SCLFNKPTKL FQTTECGNGY VEVGEECDCG VRAECYKECC
KKCSLSNGAH CSDGPCCNST CLFYPRGYSC RFAVNDCDIS ETCSGDSGQC PPNLHKQDGH
LCHLDQGRCY TGECKTRESQ CKYVWGPKSG SSEKFCYEKL NTEGSEKGNC GENGQKWIQC
SKHDVFCGLL MCTNVGQVPR IGVIKGEITP TTFNHQGNLI ECSGGHVLLD DLTDLGYVED
GTPCGPSMMC LDRKCLSIQS LNMSACPTGP NGRICSNHGV CNNEATCTCD TTWAGTDCSM
ADPPKEPPPS EDDGPKVSVA TNRLIGALAG TVLALGVLFG GTGWGREAVK KGRFNENSAI
//