ID M3XN11_MUSPF Unreviewed; 727 AA.
AC M3XN11;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=ADAM metallopeptidase domain 23 {ECO:0000313|Ensembl:ENSMPUP00000000461.1};
GN Name=ADAM23 {ECO:0000313|Ensembl:ENSMPUP00000000461.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000461.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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 EMBL; AEYP01060550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01060551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01060552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012917794.1; XM_013062340.1.
DR AlphaFoldDB; M3XN11; -.
DR STRING; 9669.ENSMPUP00000000461; -.
DR Ensembl; ENSMPUT00000000472.1; ENSMPUP00000000461.1; ENSMPUG00000000467.1.
DR GeneID; 101688507; -.
DR CTD; 8745; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158781; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR InParanoid; M3XN11; -.
DR OMA; ECDCTES; -.
DR OrthoDB; 5406290at2759; -.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 688..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 397..483
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 627..664
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 455..475
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 654..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 727 AA; 81223 MW; 7799192AF3318BC1 CRC64;
MQKEITLPSR LIYYINQDSE SPYHVLDTKT RHQQKHNQAV HLAQASFQIE AFGSKFILDL
TLNNGLLSSD YVEIHYENGK PQHSKGGEHC YYHGSIRGVK DSRAALSTCN GLHGMFEDDT
FVYMIEPLEL IHNEKSTGRP HIIQKTLAGQ YSKQMKNLSM ESSGQWPFLS ELQWLKRRRK
RAVNPSRGVF EEMKYLELMI VNDHKTYKKY RSSHAHTNNF AKSVVNLVDS IYKEQLNTRV
VLVAVETWTE KDHIEITTNP VQMLHEFSKY RQRMKQHADA VHLISRMTFH YKRSSLSFFG
GVCSRTRGVG VNEYGLPMAV AQVLSQSLAQ NLGIQWEPSS RKPKCDCTES WGGCIMEETG
VSHSRKFSKC SILEYRDFLQ RGGGACLFNR PTKLFEPTEC GNGYVEAGEE CDCGLHVECY
GLCCKKCSLS NGAHCSDGPC CNNTSCLFQP RGYECRDAVN GCDITEYCTG DSGQCPPNLH
KQDGYACNQN QGRCYNGECK TRDNQCQHVW GTKASGSDKF CYEKLNTEGT EKGNCGRDGD
RWIQCSKHDV FCGFLLCTNL TRAPRIGQLQ GEIIPTSFYH QGRVIDCSGA HVILDDDTDV
GYVEDGTPCG PSMMCLDRKC LQIQALNMSS CPLDSKGKVC SGHGVCSNEA TCICDFTWAG
TDCSIRDPVR NLHPPKDEGP KGPSATNLII GSIAGAILVA AIVLGGTGWG FKNVKKRRFD
PTQQGPI
//
