GPR85_DANRE
ID GPR85_DANRE Reviewed; 371 AA.
AC Q9I919; A4KUT3; Q1L937;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable G protein-coupled receptor 85;
DE AltName: Full=Super conserved receptor expressed in brain 2;
DE Short=zSREB2;
GN Name=gpr85; Synonyms=sreb2; ORFNames=si:dkey-223l3.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10833454; DOI=10.1006/bbrc.2000.2829;
RA Matsumoto M., Saito T., Takasaki J., Kamohara M., Sugimoto T.,
RA Kobayashi M., Tadokoro M., Matsumoto S., Ohishi T., Furuichi K.;
RT "An evolutionarily conserved G-protein coupled receptor family, SREB,
RT expressed in the central nervous system.";
RL Biochem. Biophys. Res. Commun. 272:576-582(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-346.
RX PubMed=17374158; DOI=10.1186/1471-2148-7-44;
RA Li C., Orti G., Zhang G., Lu G.;
RT "A practical approach to phylogenomics: the phylogeny of ray-finned fish
RT (Actinopterygii) as a case study.";
RL BMC Evol. Biol. 7:44-44(2007).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK05473.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ14025.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB040805; BAA96651.1; -; Genomic_DNA.
DR EMBL; CR388075; CAK05473.1; ALT_INIT; Genomic_DNA.
DR EMBL; CT583719; CAQ14025.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC054645; AAH54645.1; -; mRNA.
DR EMBL; EF033027; ABM22392.1; -; Genomic_DNA.
DR RefSeq; NP_571574.1; NM_131499.2.
DR AlphaFoldDB; Q9I919; -.
DR SMR; Q9I919; -.
DR STRING; 7955.ENSDARP00000090236; -.
DR PaxDb; Q9I919; -.
DR GeneID; 793299; -.
DR KEGG; dre:793299; -.
DR CTD; 54329; -.
DR ZFIN; ZDB-GENE-000710-2; gpr85.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9I919; -.
DR OrthoDB; 1311948at2759; -.
DR PhylomeDB; Q9I919; -.
DR TreeFam; TF331163; -.
DR PRO; PR:Q9I919; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..371
FT /note="Probable G protein-coupled receptor 85"
FT /id="PRO_0000069594"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 288
FT /note="F -> L (in Ref. 3; ABM22392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 41955 MW; F6F6175ED3A348C2 CRC64;
MANYSHAGDH NILQNVSPLA TFLKLTSLGF IIGVGVVGNL LISILLVKDK SLHRAPYYFL
LDLCASDILR SAICFPFVFT SVKNGSAWTY GTLTCKVIAF LGVLSCFHTA FMLFCVSVTR
YLAIAHHRFY TKRLTFWTCL AVICMVWTLS VAMAFPPVLD VGTYSFIREE DQCTFQHRSF
RANDSLGFML LLALILLATQ LVYLKLIFFV HDRRKMKPVQ FVPAVSQNWT FHGPGASGQA
AANWLAGFGR GPTPPTLLGI RQNSNAAGRR RLLVLDEFKT EKRISRMFYI ITFFFLSLWG
PYLVACYWRV FARGPVIPGG YLTAAVWMSF AQAGVNPFIC IFSNRELRRC FSTTLLYCRK
SRLPREPYCV I
