AGRF2_MOUSE
ID AGRF2_MOUSE Reviewed; 644 AA.
AC E9Q4J9; B9EJ67;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 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 TISSUE=Brain;
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 TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in skin and heart, and very weakly
CC in lung and spleen. Detected in all epidermal layers of skin.
CC {ECO:0000269|PubMed:22837050}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development in the skin
CC starting at embryonic day 12 with the formation of the basal layer of
CC the skin. {ECO:0000269|PubMed:22837050}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22837050}.
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:0000269|PubMed:22837050}.
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; AC117257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141353; AAI41354.1; -; mRNA.
DR CCDS; CCDS28792.2; -.
DR RefSeq; NP_001028665.2; NM_001033493.2.
DR AlphaFoldDB; E9Q4J9; -.
DR SMR; E9Q4J9; -.
DR STRING; 10090.ENSMUSP00000109244; -.
DR GlyGen; E9Q4J9; 4 sites.
DR iPTMnet; E9Q4J9; -.
DR PhosphoSitePlus; E9Q4J9; -.
DR jPOST; E9Q4J9; -.
DR PaxDb; E9Q4J9; -.
DR PRIDE; E9Q4J9; -.
DR ProteomicsDB; 296131; -.
DR Antibodypedia; 30795; 103 antibodies from 22 providers.
DR DNASU; 435529; -.
DR Ensembl; ENSMUST00000113614; ENSMUSP00000109244; ENSMUSG00000057899.
DR GeneID; 435529; -.
DR KEGG; mmu:435529; -.
DR UCSC; uc008cos.1; mouse.
DR CTD; 222611; -.
DR MGI; MGI:2182728; Adgrf2.
DR VEuPathDB; HostDB:ENSMUSG00000057899; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000162401; -.
DR HOGENOM; CLU_002753_3_6_1; -.
DR InParanoid; E9Q4J9; -.
DR OrthoDB; 611778at2759; -.
DR PhylomeDB; E9Q4J9; -.
DR TreeFam; TF316380; -.
DR BioGRID-ORCS; 435529; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adgrf2; mouse.
DR PRO; PR:E9Q4J9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9Q4J9; protein.
DR Bgee; ENSMUSG00000057899; Expressed in esophagus and 16 other tissues.
DR ExpressionAtlas; E9Q4J9; 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 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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..644
FT /note="Adhesion G-protein coupled receptor F2"
FT /id="PRO_0000433228"
FT TOPO_DOM 19..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..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 586..606
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..610
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 611..631
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
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 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 341
FT /note="W -> R (in Ref. 2; AAI41354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 644 AA; 71764 MW; 37F13B998F5FAA66 CRC64;
MIPAHWLYCL MLLLPIESCR ILCQASSKSK EKVTSRPHDV CDGVCNNNGT PCFQSCPPDS
EGNMKFACKA KKWHKVTETC HTLNTHSIFE EDKELYSVQS SDSTIRTHMF HRELKTIMDT
LMEKCPKDLS CVIKGIERSP RMPGNIAVVV QLLHNISTTL TKDVNEEKMQ SYSAMANHIL
NSKSISNWTF IQDRNSSCVL LQSIHSFASK LFMKEHLINI SHVFIHTLGT VVSRGSLGKN
FTFSMRINET SDKVTGRLLL SPEELQKVPS AFQVISIAFP TLGAILEASL LENVTVNGLV
LSVILPEELK NISLIFEKIR KSGERKSQCV GWHSLESRWD WRACKTIQEN SRQAVCRCRP
NKLYTSFSIL MSPNTLESPV LTYITYIGLG ISICSLIICL AIEVLVWSQV TKTEISYLRH
LCIANIAATL LMADAWFIVA SFLSGPVLHH NGCVAATFFV HFFYLSVFFW MLAKALLILY
GILIVFHTLP KSCLVASLFS VGYGCPLVIA IITLAVTEPG KGYLRPEACW LNWDMTKALL
AFVVPALAIV VVNLITVTMV IIKTQRAAIG SSMFQEVRAI VRICKNIAIL TPLLGLTWGF
GIATVINGHS LAFHIIFSLL NALQVSPDAA VDSELRECVH RFCG
