AGRF4_MOUSE
ID AGRF4_MOUSE Reviewed; 698 AA.
AC Q9D2L6; Q5FW81;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Adhesion G protein-coupled receptor F4;
DE AltName: Full=G-protein coupled receptor 115;
DE Flags: Precursor;
GN Name=Adgrf4; Synonyms=Gpr115;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Molar;
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: Expressed in squamous epithelia.
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; AK019508; BAB31767.1; -; mRNA.
DR EMBL; BC089564; AAH89564.1; -; mRNA.
DR CCDS; CCDS50113.1; -.
DR RefSeq; NP_001276428.1; NM_001289499.1.
DR RefSeq; NP_001276429.1; NM_001289500.1.
DR RefSeq; NP_001276430.1; NM_001289501.1.
DR RefSeq; NP_084343.1; NM_030067.2.
DR RefSeq; XP_017173214.1; XM_017317725.1.
DR AlphaFoldDB; Q9D2L6; -.
DR SMR; Q9D2L6; -.
DR STRING; 10090.ENSMUSP00000024711; -.
DR MEROPS; P02.034; -.
DR GlyGen; Q9D2L6; 9 sites.
DR iPTMnet; Q9D2L6; -.
DR PhosphoSitePlus; Q9D2L6; -.
DR MaxQB; Q9D2L6; -.
DR PaxDb; Q9D2L6; -.
DR PRIDE; Q9D2L6; -.
DR ProteomicsDB; 282033; -.
DR DNASU; 78249; -.
DR GeneID; 78249; -.
DR KEGG; mmu:78249; -.
DR UCSC; uc008cor.2; mouse.
DR CTD; 221393; -.
DR MGI; MGI:1925499; Adgrf4.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; Q9D2L6; -.
DR OrthoDB; 611778at2759; -.
DR PhylomeDB; Q9D2L6; -.
DR TreeFam; TF316380; -.
DR BioGRID-ORCS; 78249; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9D2L6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D2L6; protein.
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 GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR GO; GO:0003094; P:glomerular filtration; IGI:MGI.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IGI: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 Pfam; PF00002; 7tm_2; 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.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..698
FT /note="Adhesion G protein-coupled receptor F4"
FT /id="PRO_0000012895"
FT TOPO_DOM 20..409
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 445..465
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..486
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 487..507
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 519..539
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..566
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 567..587
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..635
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 636..656
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 350..400
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 170
FT /note="S -> P (in Ref. 2; AAH89564)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> Q (in Ref. 2; AAH89564)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="S -> N (in Ref. 1; BAB31767)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="A -> V (in Ref. 2; AAH89564)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="F -> L (in Ref. 2; AAH89564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 77331 MW; ECC1E777C88E69BB CRC64;
MKPWIAMVCC LVFFLTTECS HSKPKTHRKD EDKFQISLQK HEFRPRQGKC DGLCSSSSSC
NQSCPWNFRG EIVFTCNQNK WQKTIETCTS LSVDTLFQRI HPAASLSLAS SSVFPMSLIG
NAAPVHIGNV FQGIQKYCPE DYVCIVDAVK SSAVTSGNIA FIVELLKNIS SNLQTSGIHD
NVNWKKMKNY GKVANHILGP TAISNWAFIA NKNASSDLLE SVNSFAKKLQ IQGKSESIVD
ELFIQTKGSR ISHSSSEHSL SLSVPRYNAT EDVLVVIEIP RQALQELSFN ASQAIVVAFP
TLGAILKEVH RPNTSLQKPI DDLILSLVLP EGLNEIILTF DKINKSQSTS SQCVSWDPAT
GQWDESPCTV MSDINSTVKC RCRHTKAVTS FSILMSSKPV KNTILNHITF IGLSISIFSL
VLCLVIEAIV WSRVVVTEIS YMRHVCIVNI AVSLLTANVW FIIGSNFSAN VQEDHKWCVA
VTFLCHFFFL SLFFWMLFKA LLIVYGILVV FRRMMKSRMM AIGFAIGYGC PLVIAVITVT
VTEPGEGYTR KDACWLNWNQ TKALFAFAIP ALAIVAVNLL VVLAVAINTQ RPLIGSSKSQ
DMAIVFRISK NVAILTPLLG LTWGFGLTTL LEGVHLVFHI IFALLNAFQG FFILLFGTIM
DHKIRDALRM RVSSLKGKSR AAEKVSLSPA NGSRILNR
