ID A0A3Q3KP24_9TELE Unreviewed; 792 AA.
AC A0A3Q3KP24;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 10 {ECO:0000256|ARBA:ARBA00020518};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
DE AltName: Full=Kuzbanian protein homolog {ECO:0000256|ARBA:ARBA00032724};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000002813.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000002813.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001809};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; A0A3Q3KP24; -.
DR STRING; 205130.ENSMAMP00000002813; -.
DR Ensembl; ENSMAMT00000002869.2; ENSMAMP00000002813.1; ENSMAMG00000001924.2.
DR GeneTree; ENSGT00940000164516; -.
DR InParanoid; A0A3Q3KP24; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR049038; ADAM10_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF4; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13574; Reprolysin_2; 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.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..792
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 10"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018781362"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 223..459
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 460..554
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 395..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 792 AA; 89552 MW; B766B8975C2AE17C CRC64;
MDLSDMLLKV FLFVYLLNYT QGHYRNPLNE YIRHYEGLSY DTELVHSKHQ RAKRALSHED
KFLHLEFHSH GRHFNLRMKR DTTLFAQDLK VEVSGEEIPY DTSHIYTGEI YGEKGTLTHG
SIVDGKFEGF IQSYHGTYYV EPAERYLEDK DVPFHSVIYH EDDIHYPHKY GPEGGCADSS
VFERMWKYQA TAMEKPPKEL HTEVESNDPV LLRKKRMAQA EKNTCQLFIQ TDHLFYKYYK
TREAVIAQIS SHVKAIDAIY QGTDFMGIRN ISFMVKRIRI NTTNDERDRS NPFRFANIGV
EKFLELNSEQ NHDDYCLAYV FTDRDFDDGV LGLAWVGAPS GSSGGICEKS KLYSDGKKKS
LNTGIITVQN YASHVPPKVS HITFAHEVGH NFGSPHDSGS ECTPGESKSQ DKKEKGNYIM
YARATSGDKL NNNKFSNCSI RNISQVLEKK RSNCFVESGQ PICGNGLVEP GEECDCGYSD
QCRDQCCYDA NQADNKKCKL KPNKVCSPSQ GPCCTPECNY KSRHEKCREE SECAHQGMCN
GISAQCPTSE PKANFTACHG ETQVCLNGGC SGSICEKYGL EACTCASQDG KDETELCHVC
CMEKMNPNTC SSTGSERLAR FFNKKVTTLP AGSPCNDFKG YCDVFMKCRL VDADGPLARL
KKAIFNPELY ENIAEWIVAH WWAVLLMGIA LIMLMAGFIK ICSVHTPSSN PKLPPPKPLP
GTLKRRRAQQ HASSQVQQSQ HPHSHQHGHS GHGGHGGHGG QRQPQRQPQR QAQPQRHHRQ
PRENYQMGQM RR
//
