AGRF2_RAT
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 03-AUG-2022, entry version 57.
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 GlyGen; D4A3T6; 5 sites.
DR PaxDb; D4A3T6; -.
DR UCSC; RGD:1306718; rat.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
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; 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
