ID   AGRF2_HUMAN             Reviewed;         708 AA.
AC   Q8IZF7; Q2PNZ1; Q86SL6; Q8NGU5; Q8TDT5;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Putative adhesion G protein-coupled receptor F2P;
DE   AltName: Full=Adhesion G-protein coupled receptor F2;
DE   AltName: Full=G-protein coupled receptor 111;
DE   AltName: Full=G-protein coupled receptor PGR20;
GN   Name=ADGRF2P {ECO:0000312|HGNC:HGNC:18991};
GN   Synonyms=ADGRF2, GPR111, PGR20;
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 1).
RX   PubMed=12565841; DOI=10.1016/s0006-291x(03)00026-3;
RA   Fredriksson R., Gloriam D.E.I., Hoeglund P.J., Lagerstroem M.C.,
RA   Schioeth H.B.;
RT   "There exist at least 30 human G-protein-coupled receptors with long
RT   Ser/Thr-rich N-termini.";
RL   Biochem. Biophys. Res. Commun. 301:725-734(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-467.
RC   TISSUE=Testis;
RA   Bonner T.I., Kauffman D., Nagle J.W.;
RT   "Complete coding sequence of GPR111.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 293-708.
RX   PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA   Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT   "Identification of G protein-coupled receptor genes from the human genome
RT   sequence.";
RL   FEBS Lett. 520:97-101(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-487 (ISOFORM 1).
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=20149256; DOI=10.1186/1471-2407-10-40;
RA   Lum A.M., Wang B.B., Beck-Engeser G.B., Li L., Channa N., Wabl M.;
RT   "Orphan receptor GPR110, an oncogene overexpressed in lung and prostate
RT   cancer.";
RL   BMC Cancer 10:40-40(2010).
RN   [8]
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).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IZF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IZF7-2; Sequence=VSP_040379, VSP_040380, VSP_040381;
CC   -!- TISSUE SPECIFICITY: High expression in kidney. Up-regulated in lung
CC       adenocarcinomas and prostate cancers. {ECO:0000269|PubMed:20149256}.
CC   -!- MISCELLANEOUS: Most adhesion GPCRs undergo autoproteolysis at the GPS
CC       domain. ADGRF2 is not autoproteolyzed at the GPS motif because of the
CC       lack of a consensus catalytic triad sequence within GPS domain.
CC       {ECO:0000250|UniProtKB:E9Q4J9}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. Protein coding orthologs
CC       in other vertebrate species. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC05907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY140953; AAN46667.1; -; mRNA.
DR   EMBL; AB065684; BAC05907.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DQ315369; ABC41928.1; -; mRNA.
DR   EMBL; AL356421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB083617; BAB89330.1; -; Genomic_DNA.
DR   EMBL; AY255612; AAO85124.1; -; mRNA.
DR   RefSeq; NP_722581.4; NM_153839.6.
DR   AlphaFoldDB; Q8IZF7; -.
DR   SMR; Q8IZF7; -.
DR   BioGRID; 128806; 1.
DR   IntAct; Q8IZF7; 1.
DR   STRING; 9606.ENSP00000296862; -.
DR   ChEMBL; CHEMBL4523892; -.
DR   GlyCosmos; Q8IZF7; 7 sites, No reported glycans.
DR   GlyGen; Q8IZF7; 7 sites.
DR   iPTMnet; Q8IZF7; -.
DR   PhosphoSitePlus; Q8IZF7; -.
DR   BioMuta; ADGRF2; -.
DR   DMDM; 59797952; -.
DR   MassIVE; Q8IZF7; -.
DR   PaxDb; 9606-ENSP00000296862; -.
DR   PeptideAtlas; Q8IZF7; -.
DR   ProteomicsDB; 71348; -. [Q8IZF7-1]
DR   Antibodypedia; 30795; 107 antibodies from 22 providers.
DR   DNASU; 222611; -.
DR   UCSC; uc003oyy.3; human. [Q8IZF7-1]
DR   AGR; HGNC:18991; -.
DR   DisGeNET; 222611; -.
DR   GeneCards; ADGRF2P; -.
DR   HGNC; HGNC:18991; ADGRF2P.
DR   neXtProt; NX_Q8IZF7; -.
DR   PharmGKB; PA134984088; -.
DR   VEuPathDB; HostDB:ENSG00000164393; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_002753_3_6_1; -.
DR   InParanoid; Q8IZF7; -.
DR   OMA; MLMQKCP; -.
DR   OrthoDB; 3876300at2759; -.
DR   PhylomeDB; Q8IZF7; -.
DR   TreeFam; TF316380; -.
DR   PathwayCommons; Q8IZF7; -.
DR   SignaLink; Q8IZF7; -.
DR   BioGRID-ORCS; 222611; 4 hits in 261 CRISPR screens.
DR   ChiTaRS; ADGRF2; human.
DR   GeneWiki; GPR111; -.
DR   GenomeRNAi; 222611; -.
DR   Pharos; Q8IZF7; Tdark.
DR   PRO; PR:Q8IZF7; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q8IZF7; Protein.
DR   Bgee; ENSG00000164393; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 45 other cell types or tissues.
DR   ExpressionAtlas; Q8IZF7; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS:GDB.
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:GDB.
DR   CDD; cd15994; 7tmB2_GPR111_115; 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; IPR000203; GPS.
DR   PANTHER; PTHR45813:SF6; ADHESION G-PROTEIN COUPLED RECEPTOR F2; 1.
DR   PANTHER; PTHR45813; EF-HAND DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   Genevisible; Q8IZF7; HS.
PE   5: Uncertain;
KW   Alternative splicing; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..708
FT                   /note="Putative adhesion G protein-coupled receptor F2P"
FT                   /id="PRO_0000070334"
FT   TOPO_DOM        1..451
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        452..472
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        473..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        488..508
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..530
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        531..551
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        552..557
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        558..578
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        579..606
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        607..627
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        628..650
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        651..671
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..674
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        675..695
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        696..708
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          391..441
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..68
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_040379"
FT   VAR_SEQ         69..92
FT                   /note="PSPNAVSSDQVHCSAGCTHRKCGW -> MTHILLLYYLVFLLPTESCRTLYQ
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_040380"
FT   VAR_SEQ         690..708
FT                   /note="VSPDASDQVQSERIHEDVL -> GFFILVFGTILDPKIREALKG (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_040381"
FT   VARIANT         148
FT                   /note="Q -> R (in dbSNP:rs6907125)"
FT                   /id="VAR_024473"
FT   VARIANT         467
FT                   /note="I -> V (in dbSNP:rs9381594)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_024474"
FT   CONFLICT        427
FT                   /note="K -> E (in Ref. 3; ABC41928)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   708 AA;  78569 MW;  3DE541DD1D723966 CRC64;
     MGLTAYGNRR VQPGELPFGA NLTLIHTRAQ PVICSKLLLT KRVSPISFFL SKFQNSWGED
     GWVQLDQLPS PNAVSSDQVH CSAGCTHRKC GWAASKSKEK VPARPHGVCD GVCTDYSQCT
     QPCPPDTQGN MGFSCRQKTW HKITDTCQTL NALNIFEEDS RLVQPFEDNI KISVYTGKSE
     TITDMLLQKC PTDLSCVIRN IQQSPWIPGN IAVIVQLLHN ISTAIWTGVD EAKMQSYSTI
     ANHILNSKSI SNWTFIPDRN SSYILLHSVN SFARRLFIDK HPVDISDVFI HTMGTTISGD
     NIGKNFTFSM RINDTSNEVT GRVLISRDEL RKVPSPSQVI SIAFPTIGAI LEASLLENVT
     VNGLVLSAIL PKELKRISLI FEKISKSEER RTQCVGWHSV ENRWDQQACK MIQENSQQAV
     CKCRPSKLFT SFSILMSPHI LESLILTYIT YVGLGISICS LILCLSIEVL VWSQVTKTEI
     TYLRHVCIVN IAATLLMADV WFIVASFLSG PITHHKGCVA ATFFVHFFYL SVFFWMLAKA
     LLILYGIMIV FHTLPKSVLV ASLFSVGYGC PLAIAAITVA ATEPGKGYLR PEICWLNWDM
     TKALLAFVIP ALAIVVVNLI TVTLVIVKTQ RAAIGNSMFQ EVRAIVRISK NIAILTPLLG
     LTWGFGVATV IDDRSLAFHI IFSLLNAFQV SPDASDQVQS ERIHEDVL
//