AGRF3_MOUSE
ID AGRF3_MOUSE Reviewed; 991 AA.
AC Q58Y75; F8VPU1; Q80T50;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Adhesion G-protein coupled receptor F3;
DE AltName: Full=G-protein coupled receptor 113;
DE AltName: Full=G-protein coupled receptor PGR23;
DE Flags: Precursor;
GN Name=ADGRF3; Synonyms=Gm1041, Gpr113, Pcr113, Pgr23;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15780750; DOI=10.1016/j.ygeno.2004.12.005;
RA LopezJimenez N.D., Sainz E.S., Cavenagh M.M., Cruz-Ithier M.A.,
RA Blackwood C.A., Battey J.F., Sullivan S.L.;
RT "Two novel genes, Gpr113, which encodes a family 2 G-protein-coupled
RT receptor, and Trcg1, are selectively expressed in taste receptor cells.";
RL Genomics 85:472-482(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 726-810.
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).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to testis and
CC circumvallate papillae. {ECO:0000269|PubMed:15780750}.
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; AY701869; AAW23327.1; -; mRNA.
DR EMBL; AC158757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY255593; AAO85105.1; -; mRNA.
DR CCDS; CCDS51450.1; -.
DR RefSeq; NP_001014416.2; NM_001014394.2.
DR AlphaFoldDB; Q58Y75; -.
DR SMR; Q58Y75; -.
DR STRING; 10090.ENSMUSP00000085440; -.
DR MEROPS; P02.035; -.
DR GlyGen; Q58Y75; 10 sites.
DR PhosphoSitePlus; Q58Y75; -.
DR PaxDb; Q58Y75; -.
DR PRIDE; Q58Y75; -.
DR ProteomicsDB; 296132; -.
DR Antibodypedia; 52007; 76 antibodies from 21 providers.
DR DNASU; 381628; -.
DR Ensembl; ENSMUST00000088117; ENSMUSP00000085440; ENSMUSG00000067642.
DR GeneID; 381628; -.
DR KEGG; mmu:381628; -.
DR UCSC; uc008wvg.1; mouse.
DR CTD; 165082; -.
DR MGI; MGI:2685887; Adgrf3.
DR VEuPathDB; HostDB:ENSMUSG00000067642; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161541; -.
DR HOGENOM; CLU_010357_0_0_1; -.
DR InParanoid; Q58Y75; -.
DR OMA; YQWNASV; -.
DR OrthoDB; 311123at2759; -.
DR BioGRID-ORCS; 381628; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adgrf3; mouse.
DR PRO; PR:Q58Y75; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q58Y75; protein.
DR Bgee; ENSMUSG00000067642; Expressed in spermatid and 20 other tissues.
DR ExpressionAtlas; Q58Y75; baseline and differential.
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 Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
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 SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 2: Evidence at transcript level;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..991
FT /note="Adhesion G-protein coupled receptor F3"
FT /id="PRO_0000305305"
FT TOPO_DOM 21..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..715
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 731..751
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..757
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 758..778
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 779..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 800..820
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..850
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 851..871
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..892
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 893..913
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..916
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 917..937
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 938..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 632..683
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 964..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 201
FT /note="S -> G (in Ref. 1; AAW23327)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="A -> T (in Ref. 1; AAW23327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 108975 MW; 42D708F49225A4F8 CRC64;
MSSLALSQLL LAVTLPLLEL EPTFVPTAQS ELSPYGGKSG QQLNQYSGEG ESVLVSSYVH
LEFSSTAWPQ ELSKNFTLPT ALAVLPPKTL TGLGLTTECR ANHSGTSLCT CHPGYQWNAT
LCSLYPHCWG RRSERDSCMC RSFHGPVTGY CQLLPPVPAN LILDSQLQMH GNTLNLILLK
KEEATNLRWF LRHSKNHTPI SLWPGTNVLQ TSSEGQSGLR VARMSRHWAG EYESIFEAQG
FRWRLRQLVK VPLQEEEVVR LPDALSISCT ASTGFQLSCC IPLTTDYTAT WSPGEDSQAS
LQKMSDSQCF VLAVPHCPAT NTTYTCTLQS QNLPPLVAPV SITIIQDGDT TCPEDFSVVS
WNVTKAGFVA QAPCPVNKKG VVKRLCGTDG IWRPVQNTCT EAKILTLCLK AKLLEGQGKP
YEEVPWILSE LQEQVGVAST PSDLWEMLHT VTLLAKVVAE TSTELTGSAL KDLLTTTDKI
LDANISALWT LAQAQEPSMG SDFLKAVETL VHSLRPQQHP FSFSSANVLL QSQLLRHSSP
PGYQMSFSTW PLLQARIPWH SLAPLVHSGT NVSITSLVLQ KLDYRLPSNY TQGLWNTPYT
TPGLILVVSI TADGQAFTQA EVIMDYEDMN GTLHCVFWDH RVFQGQGGWS DEGCEVHAAN
ASITQCICQH LTAFSILMSQ HTVPENPTLD LLSQVGTGAS VLALLVCLAI YGLVWRVVVR
NKVAFFRHTT LFNMVICLLV ADTCFLGSPF LPSGYHSLIC LVTAFLCHFF YLATFFWMLA
QALVLAHQLL FVFHQLSKHV VLSLMVMLGY LCPLGFAGVT LGLYLPQRKY LWEGKCFLNG
GGVMLYSFSE PVLAIVGVNG LVLVIAVLKL LRPSLSEGPT VEKRQALVGV LKALLILTPI
FGLTWGLGVA TLFDGSIVSH YAFSILNSLQ GVFILVFGCL TDKKVLEALR KRLRGSRSSN
SAISMVTNET YTSEHSKERS EPASYEERMT D
