ID W5N834_LEPOC Unreviewed; 756 AA.
AC W5N834;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016793.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016793.1}
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 EMBL; AHAT01024871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N834; -.
DR Ensembl; ENSLOCT00000016823.1; ENSLOCP00000016793.1; ENSLOCG00000013609.1.
DR GeneTree; ENSGT00940000164516; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013609; Expressed in camera-type eye and 13 other cell types or tissues.
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:UP000018468};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..756
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 10"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867195"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 227..463
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 464..558
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 193..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
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 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 756 AA; 85118 MW; EE7C19566F0E0092 CRC64;
LLPSISSPLV VVLHYCLSLW NCHYGNPLNK YIRHYEGLSY DTDVLHQKHQ RAKRALSHEE
RFVHLDFHAH GRHFNLRMKR DASMFTQDFK VEFAGEELDY DTSHIYTGEL YGEKGTMSHG
SIVDGKFEGF IQTHQGTFYV EPSERYIKDN AVPFHSVIYH EDDIDYPHKY GAEGGCADHT
VFERMKKYQA SAVEKTPKDD HIEEEEEGQS SGPVLLRSRR AAGADKNTCQ LFIQTDHLFY
KYYGTREAVI AQISSHVKAI DSIYQTTDFQ GIRNISFMVK RIKINTTEAE RDKSNPFRFA
NIGVEKFLEL NSEQNHDDYC LAYVFTDRDF DDGVLGLAWV GAPSGSSGGI CEKSKLYSDG
KKKSLNTGII TVQNYASHVP PKVSHITFAH EVGHNFGSPH DSGTECTPGE SKSQDLKEKG
NYIMYARATS GDKLNNNKFS ICSIRNISQV LEKKRGNCFV ESGQPICGNG LVENGEQCDC
GYSDQCNDSC CYHANEPDHL KCKLKPNKKC SPSQGPCCNP DCTFRSNIQK CREESECAHQ
GFCNGNTAQC PTSEPKANFT ACHGETQVCL NGQCTGSICE KYGLEVCTCA SGDGKDDTEL
CHVCCMEKMR PDTCSSTGSD QWSKFFNKKV TTLQPGSPCN DFRGYCDVFM KCRLVDADGP
LARLKKAIFN PELYENIAEW IVAHWWAVLL MGIALIMLMA GFIKICSVHT PSSNPKLPPP
KPLPGTLKRR RPQQANPQPQ RQRQPRENYQ MGQMRR
//
