AGRG2_HUMAN
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 03-AUG-2022, entry version 160.
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}.
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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 GlyGen; Q8IZP9; 21 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; Q8IZP9; -.
DR PeptideAtlas; Q8IZP9; -.
DR PRIDE; 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 Antibodypedia; 473; 132 antibodies from 25 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 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; NKTMNVC; -.
DR OrthoDB; 148879at2759; -.
DR PhylomeDB; Q8IZP9; -.
DR TreeFam; TF321769; -.
DR PathwayCommons; Q8IZP9; -.
DR BioGRID-ORCS; 10149; 5 hits in 692 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 122 other tissues.
DR Genevisible; Q8IZP9; HS.
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:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
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; unknown pathological significance;
FT 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; AAN33056/
FT AAN33064/AAN33065/AAN38971/AAN38972/AAN38973/AAN38974/
FT AAN75702)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="E -> G (in Ref. 1; CAA57479 and 2; AAN33056/
FT AAN33064/AAN33065/AAN38971/AAN38972/AAN38973/AAN38974/
FT 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
