ID   AGRF2_RAT               Reviewed;         638 AA.
AC   D4A3T6;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Adhesion G-protein coupled receptor F2;
DE   AltName: Full=G-protein coupled receptor 111;
DE   AltName: Full=G-protein coupled receptor PGR20;
DE   Flags: Precursor;
GN   Name=Adgrf2; Synonyms=Gpr111, Pgr20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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}.
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DR   EMBL; AABR06058952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; D4A3T6; -.
DR   SMR; D4A3T6; -.
DR   STRING; 10116.ENSRNOP00000035606; -.
DR   GlyCosmos; D4A3T6; 5 sites, No reported glycans.
DR   GlyGen; D4A3T6; 5 sites.
DR   PhosphoSitePlus; D4A3T6; -.
DR   PaxDb; 10116-ENSRNOP00000035606; -.
DR   UCSC; RGD:1306718; rat.
DR   AGR; RGD:1306718; -.
DR   RGD; 1306718; Adgrf2.
DR   eggNOG; KOG4193; Eukaryota.
DR   HOGENOM; CLU_002753_3_6_1; -.
DR   InParanoid; D4A3T6; -.
DR   PhylomeDB; D4A3T6; -.
DR   TreeFam; TF316380; -.
DR   PRO; PR:D4A3T6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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   SMART; SM00303; GPS; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..638
FT                   /note="Adhesion G-protein coupled receptor F2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433229"
FT   TOPO_DOM        26..386
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        387..407
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        408..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        423..443
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..465
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        466..486
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        487..493
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        494..514
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..541
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        542..562
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..586
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        587..607
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        608..610
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        611..631
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        632..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          326..376
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  70830 MW;  8613B71433D5A694 CRC64;
     MISARWLYCL VLLLATESCR LFCQAASKSK ENVMPRPHDV CDGVCKNNAS PCFQSCPPNS
     EGNMKFACKA KRWHKVTETC HTLNAHSIFE EDKELYSVQS SESTIRTHMF NSGLKTITDT
     LMEKCPKDLS CVIRGIEKSP RIPGNIAVVV QLLHNISTTL TKGVDEEKMQ SYSAMANHIL
     NSKSISNWTF IQDRNSSCVL LQSINSFASN LFMKGHLINI SHVFIHTLGT VVPRNSLGKN
     FTFSMRVNDT SDKVTGRILL TTEELQKVPS AFQVISIAFP TLGAILEASL LENMTVNGLV
     LSVILPKELK NISLIFEKIR KSGERKSQCV GWHSLESRWD RRACKMIQEN SRQAICRCQP
     NKFFTSFSIL MSPNTVESPV LTYITYIGLG ISICSLIICL AIEALVWSQV TKTEISYLRH
     LCIANIAVTL LMADVWFIVA SFLSGPIVHH NGCVTATFFV HFFYLSVFFW MLAKALLILY
     GILIVFHTLP KSCLVASLFT VGYGCPLVIA VITLAVTEPG KGYLRPEACW LNWDMTKALL
     AFVVPALAIV VVNLITVTLV IIKTQRAAVG SSMFQEVRAI VRICKNIAIL TPLLGLTWGF
     GIATVVAGHS LAFHIIFSLL NALQVSPDAM IESEWRGC
//