AGRF1_MOUSE
ID AGRF1_MOUSE Reviewed; 908 AA.
AC Q8VEC3; B0V2Q5; Q8BMV8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Adhesion G-protein coupled receptor F1;
DE AltName: Full=G protein-coupled receptor 110;
DE Flags: Precursor;
GN Name=Adgrf1; Synonyms=Gpr110;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-733.
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22837050; DOI=10.1002/dvdy.23841;
RA Promel S., Waller-Evans H., Dixon J., Zahn D., Colledge W.H., Doran J.,
RA Carlton M.B., Grosse J., Schoneberg T., Russ A.P., Langenhan T.;
RT "Characterization and functional study of a cluster of four highly
RT conserved orphan adhesion-GPCR in mouse.";
RL Dev. Dyn. 241:1591-1602(2012).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T601};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney and adrenal gland. In
CC kidney strong expression in the renal pelvis and the ureter.
CC {ECO:0000269|PubMed:22837050}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q5T601}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Adgrf1 show no visible phenotype.
CC {ECO:0000269|PubMed:16141072}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25606.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CT025700; CAQ12617.1; -; Genomic_DNA.
DR EMBL; BC019217; AAH19217.1; -; mRNA.
DR EMBL; AK019869; BAC25606.1; ALT_FRAME; mRNA.
DR CCDS; CCDS28795.1; -.
DR RefSeq; NP_598537.2; NM_133776.2.
DR AlphaFoldDB; Q8VEC3; -.
DR SMR; Q8VEC3; -.
DR STRING; 10090.ENSMUSP00000049380; -.
DR MEROPS; P02.026; -.
DR GlyGen; Q8VEC3; 13 sites.
DR iPTMnet; Q8VEC3; -.
DR PhosphoSitePlus; Q8VEC3; -.
DR PaxDb; Q8VEC3; -.
DR PRIDE; Q8VEC3; -.
DR ProteomicsDB; 296130; -.
DR Antibodypedia; 30773; 195 antibodies from 26 providers.
DR DNASU; 77596; -.
DR Ensembl; ENSMUST00000047399; ENSMUSP00000049380; ENSMUSG00000041293.
DR GeneID; 77596; -.
DR KEGG; mmu:77596; -.
DR UCSC; uc008coz.2; mouse.
DR CTD; 266977; -.
DR MGI; MGI:1924846; Adgrf1.
DR VEuPathDB; HostDB:ENSMUSG00000041293; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161228; -.
DR HOGENOM; CLU_002753_3_6_1; -.
DR InParanoid; Q8VEC3; -.
DR OMA; TQFLSTE; -.
DR OrthoDB; 611778at2759; -.
DR PhylomeDB; Q8VEC3; -.
DR TreeFam; TF316380; -.
DR BioGRID-ORCS; 77596; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Adgrf1; mouse.
DR PRO; PR:Q8VEC3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VEC3; protein.
DR Bgee; ENSMUSG00000041293; Expressed in conjunctival fornix and 24 other tissues.
DR Genevisible; Q8VEC3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004949; F:cannabinoid receptor activity; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR008078; GPCR_2_Ig-hepta-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000082; SEA_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF01390; SEA; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01695; IGHEPTARCPTR.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50024; SEA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..908
FT /note="Adhesion G-protein coupled receptor F1"
FT /id="PRO_0000012892"
FT TOPO_DOM 21..588
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 589..609
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 623..643
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..658
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 659..679
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 698..718
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..742
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 743..763
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 764..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 790..810
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..818
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 819..839
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 147..255
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 529..576
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
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 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 72
FT /note="K -> R (in Ref. 2; AAH19217)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="I -> V (in Ref. 2; AAH19217)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="K -> N (in Ref. 2; AAH19217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 101469 MW; F5ECDE31B96BC0B0 CRC64;
MRIGLLWLVP LFTLTEGTDG FLQQKNDGRR TKEIVSMVEE RHPVHEYEVL LQVTYRDPEE
KRELKRFLKL LKSPSPSLRG PSKIIRVKAT TYCRSRKGFL ECACEDSYTW FPPSCLDPQN
CCLHTTGPVP SCNCSLRGLR QSINFCERAK VWGTFEIDEK FPEDLWNSSS DVYAHYTVGI
ENQLKEAYRR VHGFESVRVT QFRKGSIVVG YEVTGSTSPP ELLFAIEQEA EKAQEALRRQ
FPVKYGSFRV FGKAPCNSIS FGFGSENDEY TVPCSSGFTG SMTVRCQSSG WQITRESCVL
SQLEELKKEL RMIAGKITEA GVASLVQNLS TILLQSPSTT VGNLGSVVSL LSNISSLSLA
NSLTVSNLTL MNVINIADHI LDSASITNWT ILLQDAKDAS SQLLKTLESI SSLIPSMALP
LNFSGKFIDW KGTPVTQIQS TRGYNYQMEM RQNASLPIRG HVFIEPDQFQ KSHPKTIISM
ASLTFGDILP ITQRGNAWVN GPVISTLIQN YSISEIFLNF SKIKGNLTQP RCVFWDFSQL
QWSNAGCQLV NETLDTVLCR CSHLTSFSML MSPFVPSSVV PVVKWITYIG LSISIASLIL
CLIIESLFWK QTKRSQTSYT RNICLVNIAV SLLIADVWFI IAATVDPSVS PSGVCVAAVF
FTHFFYLAVF FWMLVLGILL AYRIILVFHH MALTTMMAIG FCLGYGCPLL ISIITLAVTQ
PSNSYKRNDV CWLNWSDKSK PLLAFVVPAL TIVAVNLVVV LLVLRKLWRP AVGERLNQDD
KATAIRMGKS LLVLTPLLGL TWGFGIGTMA NSHNLAWHVL FALLNAFQGF FIFCFGILLD
TKLRQLLSNK LTTLSSWKQT SKRNASDTVT QPKCLRTFNI LQHRGMYALS HTGDSSSDIT
LTQFLSTE
