AGRD1_MOUSE
ID AGRD1_MOUSE Reviewed; 903 AA.
AC Q80T32; B2RXC3; Q8BW80;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Adhesion G-protein coupled receptor D1;
DE AltName: Full=G-protein coupled receptor 133;
DE AltName: Full=G-protein coupled receptor PGR25;
DE Flags: Precursor;
GN Name=Adgrd1; Synonyms=Gpr133, Pgr25;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 569-698.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-903.
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
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).
CC -!- FUNCTION: Orphan receptor. Signals via G(s)-alpha family of G-proteins.
CC {ECO:0000250|UniProtKB:Q6QNK2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6QNK2};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: A short peptide sequence (termed the Stachel sequence) in the
CC C-terminal part of the extra-cellular domain (ECD) functions as a
CC tethered agonist. Upon structural changes within the ECD, e.g. due to
CC extracellular ligand binding or mechanical movements, this
CC intramolecular agonist is exposed to the 7TM domain, triggering G-
CC protein activation. {ECO:0000250|UniProtKB:Q6QNK2}.
CC -!- MISCELLANEOUS: The N-terminal domain and autocatalytic activity of
CC ADGRD1 at the GPCR proteolysis site (GPS) are not required for G-
CC protein coupling activity. {ECO:0000250|UniProtKB:Q6QNK2}.
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=BAC35624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC115899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151161; AAI51162.1; -; mRNA.
DR EMBL; AY255618; AAO85130.1; -; mRNA.
DR EMBL; AK054021; BAC35624.1; ALT_INIT; mRNA.
DR CCDS; CCDS39289.1; -.
DR RefSeq; NP_001074811.1; NM_001081342.1.
DR AlphaFoldDB; Q80T32; -.
DR STRING; 10090.ENSMUSP00000060307; -.
DR MEROPS; P02.021; -.
DR GlyGen; Q80T32; 13 sites.
DR PhosphoSitePlus; Q80T32; -.
DR PaxDb; Q80T32; -.
DR PRIDE; Q80T32; -.
DR ProteomicsDB; 282031; -.
DR Antibodypedia; 19419; 181 antibodies from 27 providers.
DR DNASU; 243277; -.
DR Ensembl; ENSMUST00000056617; ENSMUSP00000060307; ENSMUSG00000044017.
DR GeneID; 243277; -.
DR KEGG; mmu:243277; -.
DR UCSC; uc008zst.1; mouse.
DR CTD; 283383; -.
DR MGI; MGI:3041203; Adgrd1.
DR VEuPathDB; HostDB:ENSMUSG00000044017; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000159783; -.
DR InParanoid; Q80T32; -.
DR OMA; EGSKHLY; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q80T32; -.
DR TreeFam; TF351999; -.
DR BioGRID-ORCS; 243277; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Adgrd1; mouse.
DR PRO; PR:Q80T32; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80T32; protein.
DR Bgee; ENSMUSG00000044017; Expressed in lumbar dorsal root ganglion and 102 other tissues.
DR ExpressionAtlas; Q80T32; baseline and differential.
DR Genevisible; Q80T32; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001759; Pentraxin-related.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..903
FT /note="Adhesion G-protein coupled receptor D1"
FT /id="PRO_0000307113"
FT TOPO_DOM 27..599
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..620
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 633..653
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 654..662
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 663..683
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 702..722
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..740
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 741..761
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..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..813
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 814..834
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 111..305
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DOMAIN 536..585
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 862..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 575..583
FT /note="Stachel"
FT /evidence="ECO:0000250|UniProtKB:Q6QNK2"
FT COMPBIAS 862..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 903 AA; 99277 MW; FBF67ECFB3B5781B CRC64;
MKDLPAFPCS WVWLLWSFCS VQVCSTQPRA QEHPGFAVLA SASHYWPLEN VDGILELQDT
TGALRTLNLT VPLSHNATFV FTNDSAYSNL SATVDIMEGK VNKGIYLKEE KGVTFLYYGT
YKSSCISNPA QCGPEGVTFS FFWKTQGDQT RPAPYAYGGQ VVSDGFKVCS SGGKGSVELY
TRDNSMTWKA TFNPPGPYWT HVLFTWKSKE GLKVYVNGTL STSDPSGKVS HTYGDPHVNL
VIGSEQDQTK RYENGAFDEF IIWERALTPD EIKMYFTAAI GKHALLSSTP PAMPTAHTVI
PTDAYHPIIT NLTEERKRFQ RPGTVLRYLQ NVSLRLPNKS LSEETALNLT ETFLRTVGEV
LLLPSWTHES EDNAMTLGLV DTIDTVMGHI SSNLQSREPH VTLTGSSSTA EFTVAKVLPP
ALSAPHYRFP AHGHSYIEIP REALHSQAWT TIVGLLYHTM HYYLKNIHPT STEIPEAVNC
RDCLLSVASH LISLEVSPPP TLSQNLSGSP LITVHLRHKL TQKQYSDATN ESNRLFLYCA
FLNFSSGEGV WSSQGCALTE GNLTYSVCHC THLTNFAILM QVVPLKLTHG HQVALSSISY
VGCSLSVLCL AATLVTFAVL SSVSTIRNQR YHIHANLSFA VLVAQVLLLI SFSMEPGTVP
CQVLAVLLHY FFLTAFAWML VEGLHLYSMV IKVFGSEDSK HLYYYGIGWG CPLLICIISI
SSSMDSYGTS DSCWLALGSG AIWAFVGPAL LVIVVNIVIL VAVTRVISHI STDSYKIHGD
PSAFKLTAKA VAVLLPILGT SWVFGVLAVS DRALVFQYMF AILNSLQGLF IFLFHCLLNS
EVRAAFKHKT KVWSLTSSSA RTANTKPFSS DTVNGTRPGT ASTKLSPWDK SSHSAHRVDL
SAV
