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Database: UniProt
Entry: A0A3Q4G3C8_NEOBR
LinkDB: A0A3Q4G3C8_NEOBR
Original site: A0A3Q4G3C8_NEOBR 
ID   A0A3Q4G3C8_NEOBR        Unreviewed;       414 AA.
AC   A0A3Q4G3C8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE            EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000000448.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000000448.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A3Q4G3C8; -.
DR   STRING; 32507.ENSNBRP00000000448; -.
DR   Ensembl; ENSNBRT00000000485.1; ENSNBRP00000000448.1; ENSNBRG00000000388.1.
DR   GeneTree; ENSGT00940000165061; -.
DR   OMA; LITIQNY; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000000388; Expressed in zone of skin and 1 other cell type or tissue.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
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:SF1; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 10 ISOFORM X1; 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|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   DOMAIN          1..196
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          196..285
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   414 AA;  45479 MW;  35367F924C142FA3 CRC64;
     RAVNDIYDKV DFSGIQLINF QVKSLRVMTE EDKNDPLSPL YIGPEKLLSL YSENNWSNFC
     LSYLLTDRDY SGVLGLAWEG KANWGGVCSK PATLKNGVKC TLNTGLVTIQ NYGQFLPPRR
     VQLTLAHELG HSLGSPHDEG ANCGNLGSNG GKGRYLMFPY ATDGARENND KFSPCSIKHV
     SNILKLKKDD CFTSDQPICG NQIIEEGEEC DVGNKDADLC CYSAKEPVGI QCHLKPRKIC
     QGLCCGQKCE FKPEGQRCNE ETDCQKASVC SGLSPLCPKP AAKENLTVCS QGTRVCLKGH
     HLEKCDCPGD SMRDKCHMCC QKPQPETCAS TTSSVLSDHF HKKVLPLVGG APCSGNRGYC
     DKFHVCRILD ADGPIARLKN SFLHLDDFDD VGEWMKAHWW AILLAILTLS GVMG
//
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