AGRD1_BOVIN
ID AGRD1_BOVIN Reviewed; 902 AA.
AC A6QLU6; Q58DJ5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Adhesion G-protein coupled receptor D1;
DE AltName: Full=G-protein coupled receptor 133;
DE Flags: Precursor;
GN Name=ADGRD1; Synonyms=GPR133;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6QLU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6QLU6-2; Sequence=VSP_028570, VSP_028571, VSP_028572;
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}.
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DR EMBL; BT021602; AAX46449.1; -; mRNA.
DR EMBL; BC148090; AAI48091.1; -; mRNA.
DR RefSeq; NP_001029736.2; NM_001034564.2. [A6QLU6-1]
DR AlphaFoldDB; A6QLU6; -.
DR STRING; 9913.ENSBTAP00000027783; -.
DR PaxDb; A6QLU6; -.
DR GeneID; 528174; -.
DR KEGG; bta:528174; -.
DR CTD; 283383; -.
DR eggNOG; KOG4193; Eukaryota.
DR HOGENOM; CLU_008509_0_0_1; -.
DR InParanoid; A6QLU6; -.
DR OrthoDB; 388923at2759; -.
DR TreeFam; TF351999; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 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 Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..902
FT /note="Adhesion G-protein coupled receptor D1"
FT /id="PRO_0000307112"
FT TOPO_DOM 26..598
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 599..619
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 631..651
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..661
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 662..682
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 703..723
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..739
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 740..760
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 789..809
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..812
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 813..833
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 111..304
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT DOMAIN 535..584
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 865..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 574..582
FT /note="Stachel"
FT /evidence="ECO:0000250|UniProtKB:Q6QNK2"
FT COMPBIAS 865..888
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 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
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 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
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 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 63..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_028570"
FT VAR_SEQ 520..521
FT /note="TQ -> VS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_028571"
FT VAR_SEQ 522..902
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_028572"
SQ SEQUENCE 902 AA; 99812 MW; 86F8D35B5509E148 CRC64;
MKKLLPLCCW HSWLLLFYCD FQVRGAHTRS HVHPGFEVLA SASHYWPLEN VDGIHELQET
TGASRTHNLT VLPSHNSTFV YTNDSAYSNF SATVDIVEGK VNKGIYLKEG KGVTFLYYRK
NKTSCISNPA QCGPEGVSFS FFWKTQGEQS TSIPSAYGGQ VISNGFKVCS RGGKGSVELY
THNKSVTWEA SFSPPGHYWT HVLFTWKSEE GLKVYVNGTL RTSDPSGKAS PAYGESNDNL
VLDLTKSYEN RAFDEFIIWE RALTPDEIAM YFTAAIGEQL SLSSTPPSFS VTPTVNTMAP
TNAYHPIITN LTEERKNFRR PGVVLSYLQN MSLSLPNKSL SEETAFNLTK TFLNTVGEVL
RLPSWTAVSE DSAVVPGLID TIDTVMSHIT YNLQASKPQV AIVGSSSMAD FSVAKVLPKT
MNSSHYRFPA RGQNYIEIPH EAFHSQAWTT IVGLLYHSVH YYLSNIQPAS TKIAEAANYK
NCLLSATSYL ISLEVSPTPK LSQNLSGSPL ITVHLRHHLT QRQYTEATNE SNRIFLYCAF
LDFSSGEGIW SNQGCALTEG NLSYSICRCT HLTNFAILMQ VVPLELTRGH QVALSSISYI
GCSLSVLCLA ITLVTFAVLS SVSTIRNQRY HIHANLSCAV LVAQVLLLIS FRFEPGTAPC
QVLAMLLHYF FLSAFAWMLV EGLHLYSMVI KVFGSEDSKH RYYYGIGWGF PLLICIISIV
FAMDSYGTSK NCWLSLGNGA IWAFVAPALF IIVVNIGILI AVTRVISQIS AENYKIHGDP
SAFKLTAKAV AVLLPILGTS WVFGVLAVNN QAMVFQYMFA ILNSLQGFFI FLFHCLLNSE
VRAAFKHKTK VWSLTSSSSR QANVKPFSSD IMNGTRPATG STRLSPWDKS SHSGHRVDLS
AV
