AGRA3_MOUSE
ID AGRA3_MOUSE Reviewed; 1310 AA.
AC Q7TT36; E9QK56; Q6PE67; Q8VE71;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Adhesion G protein-coupled receptor A3;
DE AltName: Full=G-protein coupled receptor 125;
DE Flags: Precursor;
GN Name=Adgra3; Synonyms=Gpr125;
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=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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.
RX PubMed=17882221; DOI=10.1038/nature06129;
RA Seandel M., James D., Shmelkov S.V., Falciatori I., Kim J., Chavala S.,
RA Scherr D.S., Zhang F., Torres R., Gale N.W., Yancopoulos G.D., Murphy A.,
RA Valenzuela D.M., Hobbs R.M., Pandolfi P.P., Rafii S.;
RT "Generation of functional multipotent adult stem cells from GPR125+
RT germline progenitors.";
RL Nature 449:346-350(2007).
CC -!- FUNCTION: Orphan receptor that may have a role in planar cell polarity
CC pathway. {ECO:0000250|UniProtKB:S4X0Q8}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with DLG1.
CC {ECO:0000250|UniProtKB:Q8IWK6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:S4X0Q8}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed by spermatogonial progenitor cells
CC located within the outer cell layer of the seminiferous tubule and by
CC multipotent adult spermatogonial-derived stem cells.
CC {ECO:0000269|PubMed:17882221}.
CC -!- MISCELLANEOUS: Most adhesion GPCRs proteins undergo autoproteolysis at
CC the GPS domain. ADGRA3 is predicted non-cleavable because of the lack
CC of a consensus catalytic triad sequence within GPS domain.
CC {ECO:0000250|UniProtKB:Q8IWK6}.
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=AAH52391.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC102501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019649; AAH19649.1; -; mRNA.
DR EMBL; BC052391; AAH52391.1; ALT_INIT; mRNA.
DR EMBL; BC058251; AAH58251.1; -; mRNA.
DR CCDS; CCDS51500.1; -.
DR RefSeq; NP_598672.1; NM_133911.1.
DR AlphaFoldDB; Q7TT36; -.
DR SMR; Q7TT36; -.
DR BioGRID; 214207; 2.
DR STRING; 10090.ENSMUSP00000030971; -.
DR MEROPS; P02.950; -.
DR GlyConnect; 2107; 2 N-Linked glycans (1 site).
DR GlyGen; Q7TT36; 13 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q7TT36; -.
DR PhosphoSitePlus; Q7TT36; -.
DR MaxQB; Q7TT36; -.
DR PaxDb; Q7TT36; -.
DR PRIDE; Q7TT36; -.
DR ProteomicsDB; 296085; -.
DR Antibodypedia; 1933; 172 antibodies from 31 providers.
DR Ensembl; ENSMUST00000030971; ENSMUSP00000030971; ENSMUSG00000029090.
DR GeneID; 70693; -.
DR KEGG; mmu:70693; -.
DR UCSC; uc008xjz.2; mouse.
DR CTD; 166647; -.
DR MGI; MGI:1917943; Adgra3.
DR VEuPathDB; HostDB:ENSMUSG00000029090; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000157235; -.
DR HOGENOM; CLU_005242_1_0_1; -.
DR InParanoid; Q7TT36; -.
DR OMA; TYIYHHS; -.
DR OrthoDB; 31536at2759; -.
DR PhylomeDB; Q7TT36; -.
DR TreeFam; TF331206; -.
DR BioGRID-ORCS; 70693; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Adgra3; mouse.
DR PRO; PR:Q7TT36; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q7TT36; protein.
DR Bgee; ENSMUSG00000029090; Expressed in placenta labyrinth and 288 other tissues.
DR Genevisible; Q7TT36; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR000203; GPS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 4.
PE 2: Evidence at transcript level;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1310
FT /note="Adhesion G protein-coupled receptor A3"
FT /id="PRO_0000012901"
FT TOPO_DOM 28..747
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 748..768
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 786..806
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..815
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 816..836
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 837..865
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 866..886
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..908
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 909..929
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 930..985
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 986..1006
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1013
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1014..1034
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1035..1310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 28..70
FT /note="LRRNT"
FT REPEAT 71..92
FT /note="LRR 1"
FT REPEAT 95..116
FT /note="LRR 2"
FT REPEAT 119..140
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT DOMAIN 176..226
FT /note="LRRCT"
FT DOMAIN 231..329
FT /note="Ig-like"
FT DOMAIN 687..738
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 1065..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1308..1310
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1187..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
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 321
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 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 30
FT /note="A -> P (in Ref. 2; AAH52391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1070
FT /note="A -> T (in Ref. 2; AAH19649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1310 AA; 144697 MW; 688D8D44059F0142 CRC64;
MEPPPPLLLL PLALLALLWG GERGAAALPA GCKHDGRARG TGRAAAAAEG KVVCSSLELA
QVLPPDTLPN RTVTLILSNN KISELKNGSF SGLSLLERLD LRNNLISRIA PGAFWGLSSL
KRLDLTNNRI GCLNADVFRG LTNLVRLNLS GNLFTSLSQG TFDYLGSLRS LEFQTEYLLC
DCNILWMHRW VKERNITVRD TRCVYPKSLQ AQPVTGVKQE LLTCDPPLEL PSFYMTPSHR
QVVFEGDSLP FQCMASYIDQ DMQVLWYQDG RIVETDESQG IFVEKSMIHN CSLIASALTI
SNIQAGSTGN WGCHVQTKRG NNTRTVDIVV LESSAQYCPP ERVVNNKGDF RWPRTLAGIT
AYLQCTRNTH SSGIYPGSAQ DERKAWRRCD RGGFWADDDY SRCQYANDVT RVLYMFNQMP
LNLTNAVATA RQLLAYTVEA ANFSDKMDVI FVAEMIEKFG RFTREEKSKE LGDVMVDVAS
NIMLADERVL WLAQREAKAC SRIVQCLQRI ATHRLASGAH VYSTYSPNIA LEAYVIKAAG
FTGMTCSVFQ KVAASDRAGL SDYGRRDPDG NLDKQLSFKC NVSSTFSSLA LKNTIMEASI
QLPSSLLSPK HKREARAADD ALYKLQLIAF RNGKLFPATG NSTKLADDGK RRTVVTPVIL
TKIDGATVDT HHIPVNVTLR RIAHGADAVA AQWDFDLLNG QGGWKSDGCC ILYSDENITT
IQCGSLGNYA VLMDLTGTEL YTPAASLLHP VVYTTAITLL LCLLAVIISY MYHHSLIRIS
LKSWHMLVNL CFHILLTCVV FVGGITQTRN ASVCQAVGII LHYSTLATVL WVGVTARNIY
KQVTKKAKRC QDPDEPPAPP RPMLRFYLIG GGIPIIVCGI TAAANIKNYG SRPSAPYCWM
AWEPSLGAFY GPASFITFVN CMYFLSIFIQ LKRHPERKYE LKEPTEEQQR LAANENGEIN
HQDSMSLSLI STSTLENEHS FQSQLLGASL TLLLYVILWM FGAMAVSLYY PLDLVFSFFF
GATCLSFSAF MMVHHCINRE DVRLAWIMMC CPGRSSYSVQ VNVQPPNSSA TNGEAPKCTN
SSAESSCTNK SASSFKNSSQ GCKLTNLQAA AAQYHSNALP VNATPQLDNS LTEHSMDNDI
KMHVAPLDVQ FRTNVHPSRH HKNRSKGHRA SRLTVLREYA YDVPTSVEGS VQNGLPKSRP
GSNEGHSRSR RAYLAYRERQ YNPPQQDSSD ACSTLPKSSR NVEKPVSTSS KKDAPRKPAA
ADLESQQKSY GLNLAVQNGP VKSNGQEGPL LATDVTGNVR TGLWKHETTV
