ID A0A3P9QD77_POERE Unreviewed; 888 AA.
AC A0A3P9QD77;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 8-like {ECO:0000313|Ensembl:ENSPREP00000032055.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000032055.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000032055.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000032055.1};
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_008427975.1; XM_008429753.2.
DR AlphaFoldDB; A0A3P9QD77; -.
DR Ensembl; ENSPRET00000032417.1; ENSPREP00000032055.1; ENSPREG00000021705.1.
DR GeneID; 103476973; -.
DR KEGG; pret:103476973; -.
DR CTD; 368917; -.
DR GeneTree; ENSGT00940000158585; -.
DR OMA; HGQDHCL; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000021705; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
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:SF20; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..423
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 431..517
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 651..683
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 822..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 489..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 655..665
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 673..682
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 888 AA; 96922 MW; E2A7AEA43A20EEA0 CRC64;
MTESVRQSNM THSGYFIWIF ISSWGIIAGN VKNLPHVIKY QTATPQRLQG MPLPNDVAAA
HKKYPDVVQY SVSIAGKNHT LHLEKNKGLV GKSLTVTYNS DQGTQVSTTS NHEVHCYYHG
HVVGVEDSSA SIGLCSGMKG FIALQDQMYL IEPLPGETTG QQDKAHSDDD LHAVYNYKHL
RRKRSSCSHG NTTTFYDHGA RPSGLFQLGS LKSRAQTKDH KAKPKTVELA VVVDNTEYKK
FGSTKAVEAR VLEVANHVDK LYRPVGVRVM LVGLHVWSYK DEIEVSTNPE VTLGRFLEWR
QRHLLPRTKH DNAQFITGVD FEGSTVGLAN TNAMCTSNSG AVNEDHNTNS IGVASTIAHE
MGHNLGLSHD TENCVCGSLA SKKGCIMAES VGLVYPKQFS SCSQQQLSRF LEEINPACLL
DIPSADRIYG GPVCGNAFLE PGEECDCGTV EECKNPCCNA TTCKLNAGAQ CAEGQCCHKC
QLKPTGSICR PKAGDCDLAE YCTGLSAACP TDAFTQNGRP CNRGRGYCYN GQCPSRQDHC
KRLWGPDGEV AVDACFYQYG TCRRTLFNQK CSSRDQSCGK LFCSGGWDFP ITSRKSLYKV
GNRINCNEAT MNPEDNYPSD LGMVPTGTKC GNNMVCYNQK CEDIKSIKAY GTNDCSSKCN
NHGVCNHESK CHCDPGWALP FCAVQQSELT EESGLAIVIV SVIVGLILLL VILIGSLTCF
IRKRTPTKRF LPVTSGQSNP VFQSSTRRGS SRLGSTHISQ PTFVESSVSQ PCKPLFSAAV
KPQTAALKPC RAAPAPPEKE PVASHLSKVH QVARTFMQPP NVSKLPIYSE NKPLPPSRPL
PPLASKPNMK PKPPMPPLKP KPSPVQSALP HSQLLGRRAP LMPPSRPR
//
