ID A0A3P8SYF4_AMPPE Unreviewed; 755 AA.
AC A0A3P8SYF4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000017400.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000017400.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000017400.1}
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 -!- 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; A0A3P8SYF4; -.
DR STRING; 161767.ENSAPEP00000017400; -.
DR Ensembl; ENSAPET00000017896.1; ENSAPEP00000017400.1; ENSAPEG00000012421.1.
DR GeneTree; ENSGT00940000164516; -.
DR OMA; KRDSCFV; -.
DR Proteomes; UP000265080; Chromosome 1.
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 InterPro; IPR002870; Peptidase_M12B_N.
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; PF01562; Pep_M12B_propep; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000265080};
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..755
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 10"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018144291"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..458
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 459..553
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 707..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 755 AA; 84754 MW; CCF3C111531BBBEE CRC64;
MIFVKLFLMF CCLQDITGQF GNRLNKYIRH YEGLSYDTEA LHNSHQRAKR ALSPQDRTVQ
LDFHAHGRYF NLQLKRDTNL FSPDLIIEVS GEEIPIDTSH IYSGEIFGEK GTLTHGSVVD
GRFEGFIKTH QGTYYVEPSE RYLRDKNVPF HSVIYHEDDI NYPHKYGSEG GCADHSVFER
MRKYQTSGAE EHGKAENSVL EEDSSHVPFI LRRKRAAGKE KNTCQLFIQT DHLFFKYYGT
REAVIAQISS HVKAIDSIYQ ATDFMGIRNI SFMVKRIRIN TTEDERDRSN PFRFSNIGVE
KFLELNSEQN HDDYCLAYVF TDRDFDDGVL GLAWVGAPSG SSGGICEKSK LYSDGKRKSL
NTGIITVQNY ASHVPPKVSH ITFAHEVGHN FGSPHDSGIE CTPGESKLQD KKEQGNYIMY
ARATSGDKLN NNKFSICSIR NISAVLTKKR DDCFVESGQP ICGNGLVEAG EQCDCGYSDQ
CTDPCCYSAN EAEGKKCKLQ PGKICSPSQG PCCSKECTFK GANDRCRVES ECAQEGRCNG
ATALCPTSAP KENFTSCHAE TQVCLNGVCS GSICEKYGLE VCTCASQDGK DEAAELCHVC
CMEKMSPSTC SSTGSEKWAR FFNKKTTTLQ PGSPCNDFKG YCDVFMRCRL VDADGPLARL
KKAIFNAELY ENIAEWIVAH WWAVLLMGIA LIMLMAGFIK ICSVHTPSSN PKLPPPKPLP
GTLKRRRQQH ANQQPQGQRQ PRQYRENYQM GQMRR
//
