ID AGRG2_HUMAN Reviewed; 1017 AA. AC Q8IZP9; B1AWB3; B1AWB4; B1AWB6; B1AWB7; O00406; Q14CE0; Q8IWT2; Q8IZE4; AC Q8IZE5; Q8IZE6; Q8IZE7; Q8IZP3; Q8IZP4; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 24-JAN-2024, entry version 168. DE RecName: Full=Adhesion G-protein coupled receptor G2 {ECO:0000303|PubMed:25713288}; DE AltName: Full=G-protein coupled receptor 64; DE AltName: Full=Human epididymis-specific protein 6; DE Short=He6; DE Flags: Precursor; GN Name=ADGRG2 {ECO:0000312|HGNC:HGNC:4516}; GN Synonyms=GPR64 {ECO:0000303|PubMed:28397838}, HE6, TM7LN2; 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] (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Epididymis; RX PubMed=9150425; DOI=10.1089/dna.1997.16.379; RA Osterhoff C., Ivell R., Kirchhoff C.; RT "Cloning of a human epididymis-specific mRNA, HE6, encoding a novel member RT of the seven transmembrane-domain receptor superfamily."; RL DNA Cell Biol. 16:379-389(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8 AND 9), TISSUE RP SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION. RC TISSUE=Epididymis; RX PubMed=12420295; DOI=10.1002/mrd.10220; RA Obermann H., Samalecos A., Osterhoff C., Schroeder B., Heller R., RA Kirchhoff C.; RT "HE6, a two-subunit heptahelical receptor associated with apical membranes RT of efferent and epididymal duct epithelia."; RL Mol. Reprod. Dev. 64:13-26(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP TISSUE SPECIFICITY. RX PubMed=18469038; DOI=10.1530/rep-08-0078; RA Kirchhoff C., Osterhoff C., Samalecos A.; RT "HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin RT scaffold in male excurrent duct epithelia."; RL Reproduction 136:235-245(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] RP TISSUE SPECIFICITY. RX PubMed=23338946; DOI=10.1002/path.4170; RA Richter G.H., Fasan A., Hauer K., Grunewald T.G., Berns C., Rossler S., RA Naumann I., Staege M.S., Fulda S., Esposito I., Burdach S.; RT "G-Protein coupled receptor 64 promotes invasiveness and metastasis in RT Ewing sarcomas through PGF and MMP1."; RL J. Pathol. 230:70-81(2013). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP NOMENCLATURE. RX PubMed=25713288; DOI=10.1124/pr.114.009647; RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R., RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I., RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S., RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A., RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.; RT "International union of basic and clinical pharmacology. XCIV. Adhesion G RT protein-coupled receptors."; RL Pharmacol. Rev. 67:338-367(2015). RN [11] RP INVOLVEMENT IN CBAVDX, AND TISSUE SPECIFICITY. RX PubMed=27476656; DOI=10.1016/j.ajhg.2016.06.012; RA Patat O., Pagin A., Siegfried A., Mitchell V., Chassaing N., Faguer S., RA Monteil L., Gaston V., Bujan L., Courtade-Saidi M., Marcelli F., Lalau G., RA Rigot J.M., Mieusset R., Bieth E.; RT "Truncating mutations in the adhesion G protein-coupled receptor G2 gene RT ADGRG2 cause an X-Linked congenital bilateral absence of vas deferens."; RL Am. J. Hum. Genet. 99:437-442(2016). RN [12] RP VARIANT SER-224. RX PubMed=23092983; DOI=10.1038/tp.2012.102; RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D., RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A., RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G., RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T., RA Brice A., Depienne C.; RT "Analysis of the chromosome X exome in patients with autism spectrum RT disorders identified novel candidate genes, including TMLHE."; RL Transl. Psychiatry 2:E179-E179(2012). RN [13] RP VARIANT SER-64. RX PubMed=28397838; DOI=10.1038/mp.2017.60; RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K., RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M., RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M., RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R., RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M., RA Vincent J.B.; RT "Mapping autosomal recessive intellectual disability: combined microarray RT and exome sequencing identifies 26 novel candidate genes in 192 RT consanguineous families."; RL Mol. Psychiatry 23:973-984(2018). CC -!- FUNCTION: Orphan receptor. Could be involved in a signal transduction CC pathway controlling epididymal function and male fertility. May CC regulate fluid exchange within epididymis. CC {ECO:0000250|UniProtKB:Q8CJ12}. CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing; CC the large extracellular N-terminal fragment and the membrane-bound C- CC terminal fragment predominantly remain associated and non-covalently CC linked. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Name=1; Synonyms=Long splice variant; CC IsoId=Q8IZP9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IZP9-2; Sequence=VSP_009791; CC Name=3; Synonyms=d1; CC IsoId=Q8IZP9-3; Sequence=VSP_009792; CC Name=4; Synonyms=24; CC IsoId=Q8IZP9-4; Sequence=VSP_009793; CC Name=5; Synonyms=23; CC IsoId=Q8IZP9-5; Sequence=VSP_009794; CC Name=6; Synonyms=d3; CC IsoId=Q8IZP9-6; Sequence=VSP_009795; CC Name=7; Synonyms=d2; CC IsoId=Q8IZP9-7; Sequence=VSP_009796; CC Name=8; Synonyms=21; CC IsoId=Q8IZP9-8; Sequence=VSP_009797; CC Name=9; Synonyms=Delta exon 28; CC IsoId=Q8IZP9-9; Sequence=VSP_009798; CC Name=10; CC IsoId=Q8IZP9-10; Sequence=VSP_009792, VSP_009793, VSP_054522; CC -!- TISSUE SPECIFICITY: Epididymis-specific expression (at protein level). CC Both subunits are associated with apical membranes of efferent ductule CC and proximal epididymal duct epithelia. Mainly expressed in the CC nonciliated principal cells of the proximal excurrent ducts. CC Specifically over-expressed in Ewing sarcomas but also up-regulated in CC a number of carcinomas derived from prostate, kidney or lung. CC {ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:18469038, CC ECO:0000269|PubMed:23338946, ECO:0000269|PubMed:27476656, CC ECO:0000269|PubMed:9150425}. CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit CC and a seven-transmembrane subunit. {ECO:0000305}. CC -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}. CC -!- DISEASE: Congenital bilateral aplasia of the vas deferens, X-linked CC (CBAVDX) [MIM:300985]: A disease characterized by bilateral absence of CC vas deferens, obstructive azoospermia, and infertility. CC {ECO:0000269|PubMed:27476656}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X81892; CAA57479.1; -; mRNA. DR EMBL; AF538954; AAN33056.1; -; mRNA. DR EMBL; AF539455; AAN33064.1; -; mRNA. DR EMBL; AF539456; AAN33065.1; -; mRNA. DR EMBL; AY143364; AAN38971.1; -; mRNA. DR EMBL; AY143365; AAN38972.1; -; mRNA. DR EMBL; AY143366; AAN38973.1; -; mRNA. DR EMBL; AY143367; AAN38974.1; -; mRNA. DR EMBL; AY148343; AAN75702.1; -; mRNA. DR EMBL; AL732509; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL732578; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC113979; AAI13980.1; -; mRNA. DR CCDS; CCDS14191.1; -. [Q8IZP9-2] DR CCDS; CCDS43921.1; -. [Q8IZP9-6] DR CCDS; CCDS43922.1; -. [Q8IZP9-4] DR CCDS; CCDS43923.1; -. [Q8IZP9-1] DR CCDS; CCDS55376.1; -. [Q8IZP9-5] DR CCDS; CCDS55377.1; -. [Q8IZP9-7] DR CCDS; CCDS55378.1; -. [Q8IZP9-3] DR CCDS; CCDS55379.1; -. [Q8IZP9-9] DR RefSeq; NP_001073327.1; NM_001079858.2. [Q8IZP9-1] DR RefSeq; NP_001073328.1; NM_001079859.2. [Q8IZP9-4] DR RefSeq; NP_001073329.1; NM_001079860.2. [Q8IZP9-6] DR RefSeq; NP_001171762.1; NM_001184833.1. [Q8IZP9-3] DR RefSeq; NP_001171763.1; NM_001184834.1. [Q8IZP9-9] DR RefSeq; NP_001171764.1; NM_001184835.1. [Q8IZP9-8] DR RefSeq; NP_001171765.1; NM_001184836.1. [Q8IZP9-5] DR RefSeq; NP_001171766.1; NM_001184837.1. [Q8IZP9-7] DR RefSeq; NP_005747.2; NM_005756.3. [Q8IZP9-2] DR RefSeq; XP_006724518.1; XM_006724455.3. [Q8IZP9-1] DR RefSeq; XP_011543736.1; XM_011545434.1. [Q8IZP9-1] DR RefSeq; XP_011543737.1; XM_011545435.2. [Q8IZP9-1] DR AlphaFoldDB; Q8IZP9; -. DR SMR; Q8IZP9; -. DR BioGRID; 115451; 11. DR STRING; 9606.ENSP00000369198; -. DR ChEMBL; CHEMBL4523893; -. DR MEROPS; P02.007; -. DR TCDB; 9.A.14.6.10; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q8IZP9; 21 sites, No reported glycans. DR GlyGen; Q8IZP9; 25 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q8IZP9; -. DR PhosphoSitePlus; Q8IZP9; -. DR BioMuta; ADGRG2; -. DR DMDM; 229462874; -. DR EPD; Q8IZP9; -. DR jPOST; Q8IZP9; -. DR MassIVE; Q8IZP9; -. DR MaxQB; Q8IZP9; -. DR PaxDb; 9606-ENSP00000369198; -. DR PeptideAtlas; Q8IZP9; -. DR ProteomicsDB; 60325; -. DR ProteomicsDB; 71395; -. [Q8IZP9-1] DR ProteomicsDB; 71396; -. [Q8IZP9-2] DR ProteomicsDB; 71397; -. [Q8IZP9-3] DR ProteomicsDB; 71398; -. [Q8IZP9-4] DR ProteomicsDB; 71399; -. [Q8IZP9-5] DR ProteomicsDB; 71400; -. [Q8IZP9-6] DR ProteomicsDB; 71401; -. [Q8IZP9-7] DR ProteomicsDB; 71402; -. [Q8IZP9-8] DR ProteomicsDB; 71403; -. [Q8IZP9-9] DR Pumba; Q8IZP9; -. DR Antibodypedia; 473; 146 antibodies from 26 providers. DR DNASU; 10149; -. DR Ensembl; ENST00000340581.3; ENSP00000344972.3; ENSG00000173698.18. [Q8IZP9-10] DR Ensembl; ENST00000354791.7; ENSP00000346845.4; ENSG00000173698.18. [Q8IZP9-10] DR Ensembl; ENST00000356606.8; ENSP00000349015.4; ENSG00000173698.18. [Q8IZP9-4] DR Ensembl; ENST00000357544.7; ENSP00000350152.3; ENSG00000173698.18. [Q8IZP9-7] DR Ensembl; ENST00000357991.7; ENSP00000350680.3; ENSG00000173698.18. [Q8IZP9-2] DR Ensembl; ENST00000360279.8; ENSP00000353421.4; ENSG00000173698.18. [Q8IZP9-6] DR Ensembl; ENST00000379869.8; ENSP00000369198.3; ENSG00000173698.18. [Q8IZP9-1] DR Ensembl; ENST00000379873.6; ENSP00000369202.2; ENSG00000173698.18. [Q8IZP9-9] DR Ensembl; ENST00000379876.5; ENSP00000369205.1; ENSG00000173698.18. [Q8IZP9-5] DR Ensembl; ENST00000379878.7; ENSP00000369207.3; ENSG00000173698.18. [Q8IZP9-3] DR GeneID; 10149; -. DR KEGG; hsa:10149; -. DR MANE-Select; ENST00000379869.8; ENSP00000369198.3; NM_001079858.3; NP_001073327.1. DR UCSC; uc004cyx.4; human. [Q8IZP9-1] DR AGR; HGNC:4516; -. DR CTD; 10149; -. DR DisGeNET; 10149; -. DR GeneCards; ADGRG2; -. DR HGNC; HGNC:4516; ADGRG2. DR HPA; ENSG00000173698; Tissue enriched (epididymis). DR MalaCards; ADGRG2; -. DR MIM; 300572; gene. DR MIM; 300985; phenotype. DR neXtProt; NX_Q8IZP9; -. DR OpenTargets; ENSG00000173698; -. DR Orphanet; 48; Congenital bilateral absence of vas deferens. DR PharmGKB; PA28908; -. DR VEuPathDB; HostDB:ENSG00000173698; -. DR eggNOG; KOG4193; Eukaryota. DR GeneTree; ENSGT00940000156341; -. DR HOGENOM; CLU_002753_3_3_1; -. DR InParanoid; Q8IZP9; -. DR OMA; RIWLFGN; -. DR OrthoDB; 4370914at2759; -. DR PhylomeDB; Q8IZP9; -. DR TreeFam; TF321769; -. DR PathwayCommons; Q8IZP9; -. DR BioGRID-ORCS; 10149; 6 hits in 766 CRISPR screens. DR ChiTaRS; ADGRG2; human. DR GeneWiki; GPR64; -. DR GenomeRNAi; 10149; -. DR Pharos; Q8IZP9; Tbio. DR PRO; PR:Q8IZP9; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8IZP9; Protein. DR Bgee; ENSG00000173698; Expressed in corpus epididymis and 124 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:GDB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc. DR CDD; cd15444; 7tmB2_GPR64; 1. DR Gene3D; 2.60.220.50; -; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR046338; GAIN_dom_sf. DR InterPro; IPR017981; GPCR_2-like_7TM. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017983; GPCR_2_secretin-like_CS. DR InterPro; IPR000203; GPS. DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR12011:SF264; ADHESION G-PROTEIN COUPLED RECEPTOR G2; 1. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF01825; GPS; 1. DR PRINTS; PR00249; GPCRSECRETIN. DR SMART; SM00303; GPS; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR PROSITE; PS50221; GPS; 1. DR Genevisible; Q8IZP9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome; KW Signal; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1..37 FT /evidence="ECO:0000255" FT CHAIN 38..1017 FT /note="Adhesion G-protein coupled receptor G2" FT /id="PRO_0000012886" FT TOPO_DOM 38..627 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 628..648 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 649..667 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 668..688 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 689..693 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 694..714 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 715..737 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 738..758 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 759..789 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 790..810 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 811..834 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 835..855 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 856..857 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 858..878 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 879..1017 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 567..618 FT /note="GPS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098" FT REGION 301..366 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 918..939 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 317..366 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1010 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 85 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 117 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 144 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 162 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 194 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 357 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 438 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 461 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 542 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 547 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 551 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 597 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 857 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 51..66 FT /note="Missing (in isoform 3 and isoform 10)" FT /evidence="ECO:0000303|PubMed:12420295, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009792" FT VAR_SEQ 52..101 FT /note="AKLSVVSFAPSSNGTPEVETTSLNDVTLSLLPSNETEKTKITIVKTFNAS FT -> EVETTSLNDVTLSLLPSNET (in isoform 7)" FT /evidence="ECO:0000303|PubMed:12420295" FT /id="VSP_009796" FT VAR_SEQ 52..101 FT /note="AKLSVVSFAPSSNGTPEVETTSLNDVTLSLLPSNETEKTKITIVKTFNAS FT -> DVTLSLLPSNET (in isoform 8)" FT /evidence="ECO:0000303|PubMed:12420295" FT /id="VSP_009797" FT VAR_SEQ 52..75 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:12420295" FT /id="VSP_009794" FT VAR_SEQ 65..67 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9150425" FT /id="VSP_009791" FT VAR_SEQ 68..101 FT /note="EVETTSLNDVTLSLLPSNETEKTKITIVKTFNAS -> DVTLSLLPSNET FT (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12420295" FT /id="VSP_009795" FT VAR_SEQ 88..101 FT /note="Missing (in isoform 4 and isoform 10)" FT /evidence="ECO:0000303|PubMed:12420295, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009793" FT VAR_SEQ 474..562 FT /note="Missing (in isoform 10)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054522" FT VAR_SEQ 906..956 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:12420295" FT /id="VSP_009798" FT VARIANT 64 FT /note="N -> S (found in a family with intellectual FT disability; uncertain significance; dbSNP:rs746638813)" FT /evidence="ECO:0000269|PubMed:28397838" FT /id="VAR_080773" FT VARIANT 224 FT /note="P -> S (in dbSNP:rs140334931)" FT /evidence="ECO:0000269|PubMed:23092983" FT /id="VAR_076259" FT VARIANT 290 FT /note="H -> Q (in dbSNP:rs35974297)" FT /id="VAR_055289" FT VARIANT 771 FT /note="N -> S (in dbSNP:rs3924227)" FT /id="VAR_055290" FT CONFLICT 202 FT /note="V -> A (in Ref. 1; CAA57479 and 2; FT AAN33056/AAN33064/AAN33065/AAN38971/AAN38972/AAN38973/AAN38974/AAN75702)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="E -> G (in Ref. 1; CAA57479 and 2; FT AAN33056/AAN33064/AAN33065/AAN38971/AAN38972/AAN38973/AAN38974/AAN75702)" FT /evidence="ECO:0000305" SQ SEQUENCE 1017 AA; 111593 MW; 2E0839DB45B6C553 CRC64; MVFSVRQCGH VGRTEEVLLT FKIFLVIICL HVVLVTSLEE DTDNSSLSPP PAKLSVVSFA PSSNGTPEVE TTSLNDVTLS LLPSNETEKT KITIVKTFNA SGVKPQRNIC NLSSICNDSA FFRGEIMFQY DKESTVPQNQ HITNGTLTGV LSLSELKRSE LNKTLQTLSE TYFIMCATAE AQSTLNCTFT IKLNNTMNAC AVIAALERVK IRPMEHCCCS VRIPCPSSPE ELEKLQCDLQ DPIVCLADHP RGPPFSSSQS IPVVPRATVL SQVPKATSFA EPPDYSPVTH NVPSPIGEIQ PLSPQPSAPI ASSPAIDMPP QSETISSPMP QTHVSGTPPP VKASFSSPTV SAPANVNTTS APPVQTDIVN TSSISDLENQ VLQMEKALSL GSLEPNLAGE MINQVSRLLH SPPDMLAPLA QRLLKVVDDI GLQLNFSNTT ISLTSPSLAL AVIRVNASSF NTTTFVAQDP ANLQVSLETQ APENSIGTIT LPSSLMNNLP AHDMELASRV QFNFFETPAL FQDPSLENLS LISYVISSSV ANLTVRNLTR NVTVTLKHIN PSQDELTVRC VFWDLGRNGG RGGWSDNGCS VKDRRLNETI CTCSHLTSFG VLLDLSRTSV LPAQMMALTF ITYIGCGLSS IFLSVTLVTY IAFEKIRRDY PSKILIQLCA ALLLLNLVFL LDSWIALYKM QGLCISVAVF LHYFLLVSFT WMGLEAFHMY LALVKVFNTY IRKYILKFCI VGWGVPAVVV TIILTISPDN YGLGSYGKFP NGSPDDFCWI NNNAVFYITV VGYFCVIFLL NVSMFIVVLV QLCRIKKKKQ LGAQRKTSIQ DLRSIAGLTF LLGITWGFAF FAWGPVNVTF MYLFAIFNTL QGFFIFIFYC VAKENVRKQW RRYLCCGKLR LAENSDWSKT ATNGLKKQTV NQGVSSSSNS LQSSSNSTNS TTLLVNNDCS VHASGNGNAS TERNGVSFSV QNGDVCLHDF TGKQHMFNEK EDSCNGKGRM ALRRTSKRGS LHFIEQM //