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GPR85_HUMAN
ID   GPR85_HUMAN             Reviewed;         370 AA.
AC   P60893; Q9JHI6; Q9NPD1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Probable G-protein coupled receptor 85;
DE   AltName: Full=Super conserved receptor expressed in brain 2;
GN   Name=GPR85; Synonyms=SREB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10978537; DOI=10.1016/s0167-4781(00)00182-2;
RA   Hellebrand S., Schaller H.C., Wittenberger T.;
RT   "The brain-specific G-protein coupled receptor GPR85 with identical protein
RT   sequence in man and mouse maps to human chromosome 7q31.";
RL   Biochim. Biophys. Acta 1493:269-272(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   VARIANTS THR-152 AND LEU-221, CHARACTERIZATION OF VARIANTS THR-152 AND
RP   LEU-221, SUBCELLULAR LOCATION, AND INTERACTION WITH DLG4 AND DLG3.
RX   PubMed=25780553; DOI=10.1186/s13229-015-0012-5;
RA   Fujita-Jimbo E., Tanabe Y., Yu Z., Kojima K., Mori M., Li H., Iwamoto S.,
RA   Yamagata T., Momoi M.Y., Momoi T.;
RT   "The association of GPR85 with PSD-95-neuroligin complex and autism
RT   spectrum disorder: a molecular analysis.";
RL   Mol. Autism 6:17-17(2015).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBUNIT: Interacts with DLG4 AND DLG3. {ECO:0000269|PubMed:25780553}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:25780553}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis. Lower levels
CC       in small intestine, placenta and spleen. In brain regions, detected in
CC       all regions tested, but somewhat lower levels in the corpus callosum,
CC       medulla and spinal cord. {ECO:0000269|PubMed:10833454,
CC       ECO:0000269|PubMed:10978537}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF250237; AAF79956.1; -; mRNA.
DR   EMBL; AB040800; BAA96646.1; -; mRNA.
DR   EMBL; AB065688; BAC05911.1; -; Genomic_DNA.
DR   EMBL; AL161959; CAB82307.1; -; mRNA.
DR   EMBL; AC073346; AAQ93365.1; -; Genomic_DNA.
DR   CCDS; CCDS5758.1; -.
DR   PIR; T47131; T47131.
DR   RefSeq; NP_001139737.1; NM_001146265.1.
DR   RefSeq; NP_001139738.1; NM_001146266.1.
DR   RefSeq; NP_001139739.1; NM_001146267.1.
DR   RefSeq; NP_061843.3; NM_018970.6.
DR   RefSeq; XP_005250508.1; XM_005250451.2.
DR   RefSeq; XP_016867841.1; XM_017012352.1.
DR   AlphaFoldDB; P60893; -.
DR   SMR; P60893; -.
DR   BioGRID; 119932; 11.
DR   IntAct; P60893; 1.
DR   STRING; 9606.ENSP00000297146; -.
DR   ChEMBL; CHEMBL4523868; -.
DR   GlyGen; P60893; 3 sites.
DR   iPTMnet; P60893; -.
DR   PhosphoSitePlus; P60893; -.
DR   BioMuta; GPR85; -.
DR   DMDM; 46397442; -.
DR   MassIVE; P60893; -.
DR   PaxDb; P60893; -.
DR   PRIDE; P60893; -.
DR   Antibodypedia; 17381; 171 antibodies from 26 providers.
DR   DNASU; 54329; -.
DR   Ensembl; ENST00000297146.7; ENSP00000297146.2; ENSG00000164604.14.
DR   Ensembl; ENST00000424100.2; ENSP00000396763.1; ENSG00000164604.14.
DR   Ensembl; ENST00000449591.2; ENSP00000401178.1; ENSG00000164604.14.
DR   Ensembl; ENST00000610164.1; ENSP00000476863.1; ENSG00000164604.14.
DR   GeneID; 54329; -.
DR   KEGG; hsa:54329; -.
DR   MANE-Select; ENST00000424100.2; ENSP00000396763.1; NM_001146267.2; NP_001139739.1.
DR   UCSC; uc003vgp.2; human.
DR   CTD; 54329; -.
DR   DisGeNET; 54329; -.
DR   GeneCards; GPR85; -.
DR   HGNC; HGNC:4536; GPR85.
DR   HPA; ENSG00000164604; Group enriched (brain, choroid plexus, retina, skeletal muscle).
DR   MIM; 605188; gene.
DR   neXtProt; NX_P60893; -.
DR   OpenTargets; ENSG00000164604; -.
DR   PharmGKB; PA28929; -.
DR   VEuPathDB; HostDB:ENSG00000164604; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00890000139436; -.
DR   HOGENOM; CLU_055518_0_0_1; -.
DR   InParanoid; P60893; -.
DR   OMA; ARGPIVP; -.
DR   OrthoDB; 1311948at2759; -.
DR   PhylomeDB; P60893; -.
DR   TreeFam; TF331163; -.
DR   PathwayCommons; P60893; -.
DR   SignaLink; P60893; -.
DR   BioGRID-ORCS; 54329; 12 hits in 1071 CRISPR screens.
DR   GenomeRNAi; 54329; -.
DR   Pharos; P60893; Tbio.
DR   PRO; PR:P60893; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P60893; protein.
DR   Bgee; ENSG00000164604; Expressed in cortical plate and 126 other tissues.
DR   ExpressionAtlas; P60893; baseline and differential.
DR   Genevisible; P60893; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..370
FT                   /note="Probable G-protein coupled receptor 85"
FT                   /id="PRO_0000069591"
FT   TOPO_DOM        1..25
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..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..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..313
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         152
FT                   /note="M -> T (found in a patient with autism spectrum
FT                   disorder; unknown pathological significance; induces
FT                   response to endoplasmic reticulum stress; negative
FT                   regulation of dendrite morphogenesis)"
FT                   /evidence="ECO:0000269|PubMed:25780553"
FT                   /id="VAR_074204"
FT   VARIANT         221
FT                   /note="V -> L (found in a patient with autism spectrum
FT                   disorder; unknown pathological significance; induces
FT                   response to endoplasmic reticulum stress; negative
FT                   regulation of dendrite morphogenesis)"
FT                   /evidence="ECO:0000269|PubMed:25780553"
FT                   /id="VAR_074205"
SQ   SEQUENCE   370 AA;  41995 MW;  7B67A39F6166AAEB CRC64;
     MANYSHAADN ILQNLSPLTA FLKLTSLGFI IGVSVVGNLL ISILLVKDKT LHRAPYYFLL
     DLCCSDILRS AICFPFVFNS VKNGSTWTYG TLTCKVIAFL GVLSCFHTAF MLFCISVTRY
     LAIAHHRFYT KRLTFWTCLA VICMVWTLSV AMAFPPVLDV GTYSFIREED QCTFQHRSFR
     ANDSLGFMLL LALILLATQL VYLKLIFFVH DRRKMKPVQF VAAVSQNWTF HGPGASGQAA
     ANWLAGFGRG PTPPTLLGIR QNANTTGRRR LLVLDEFKME KRISRMFYIM TFLFLTLWGP
     YLVACYWRVF ARGPVVPGGF LTAAVWMSFA QAGINPFVCI FSNRELRRCF STTLLYCRKS
     RLPREPYCVI
 
 
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