ID A0A3B3BGG9_ORYME Unreviewed; 780 AA.
AC A0A3B3BGG9;
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:ENSOMEP00000004302.1};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSOMEP00000004302.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000004302.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000004302.1}
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; A0A3B3BGG9; -.
DR Ensembl; ENSOMET00000009387.1; ENSOMEP00000004302.1; ENSOMEG00000005340.1.
DR GeneTree; ENSGT00940000158781; -.
DR Proteomes; UP000261560; 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};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..780
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017411237"
FT TRANSMEM 743..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..446
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 452..537
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DISULFID 509..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 780 AA; 86436 MW; 2E2FB3E27D81D121 CRC64;
MRLIFLATSL VSILSPWLPP SLASSDFQGA EDKVERDAVV ALLKQQATAA PATSNATHHA
VEHTITYPSR LIYYLNEDSE STYHDLNTQT RNQATEGQTV HLAQASFQLE AFGSRFVLDL
TLNNDLLSSN YVEIHYEGGK PVLSKGGEHC YYHGQVRGND NSHVALSTCN GLQGMFDDGV
HAYLIEPLHL THSVDSAARP HKLKRIASFQ WNNDSTEAVE EEQLFSELDE LSWLKRRKKR
AMPRSVFEEM KYLEVMIVCD HNTYKRHKQH ARNFAKGVVN LVDGIFKEQL HTRVVLVAVE
IWTDKDRIPI SEKPLEMLRD FSKYRQQSIK VHADSVQLFS NLNFQYRRSS AAYFGGLCSL
NRGVGVNEHS GIWSMVPFLS QSLAQNLGIQ WDPASKRKEC GCDIKMIGCI MEDNGVQHPK
KFSKCSISDY KEFLLKGGGS CLFNRPTKLF ETAHCGNGFV EVGEECDCGL RSDCYKECCK
KCSLANGAHC SDGPCCNNTC LFLPRGITCR YAVNDCDISE TCSGDSGQCP PNLHKQDGYL
CQVNQGRCYS GECKTRENQC KYIWGTKAGG SEKFCYEKLN TEGTEKGNCG KDGERWIQCS
KHDVFCGYLL CTNVGKIPRI GTMKEDITTT SFNHQGNVIH CTGAHVLLDD ETDLGYVEDG
TPCGPSMMCL DRKCLPIQSL NMSTCPSGPN GQVCSAHGVC NNEATCTCDT TWAGTDCSMP
DPPKEPEVSE DDEPKVSVAT NRLIGAVAGT ILALGVIFGG TGWGIENVKK RRYDPNAQAI
//