ID   GPC5C_BOVIN             Reviewed;         442 AA.
AC   Q2YDG0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=G-protein coupled receptor family C group 5 member C;
DE   Flags: Precursor;
GN   Name=GPRC5C;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This retinoic acid-inducible G-protein coupled receptor
CC       provide evidence for a possible interaction between retinoid and G-
CC       protein signaling pathways. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
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DR   EMBL; BC110241; AAI10242.2; -; mRNA.
DR   RefSeq; NP_001258939.1; NM_001272010.1.
DR   AlphaFoldDB; Q2YDG0; -.
DR   STRING; 9913.ENSBTAP00000024834; -.
DR   PaxDb; Q2YDG0; -.
DR   PRIDE; Q2YDG0; -.
DR   GeneID; 535664; -.
DR   KEGG; bta:535664; -.
DR   CTD; 55890; -.
DR   eggNOG; ENOG502QQEH; Eukaryota.
DR   InParanoid; Q2YDG0; -.
DR   OrthoDB; 807909at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR017978; GPCR_3_C.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..442
FT                   /note="G-protein coupled receptor family C group 5 member
FT                   C"
FT                   /id="PRO_0000251135"
FT   TOPO_DOM        24..50
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..209
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   MOD_RES         404
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         415
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         424
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  48459 MW;  B2A5434AA562DF31 CRC64;
     MAIHRTVLMC LGLPLFLLPG ARAQEQAPPG CSPDLNPLYY NLCDRSEAWG IILEAVAGAG
     VVTTFVLTII LVASLPFVQD TKKRSLLGTQ VFFLLGTLGL FCLVFACVVK PSFSTCASRR
     FLFGVLFAIC FSCLVAHVLA LHFLVRKNHG PRGWVIFLVA LLLSLVEVII NTEWLIITLV
     RGAGTEGDAL GNGSAGWVAV SPCAIANADF VMALIYVMLL LLCAFSGAWS ALCGRFKRWR
     KHGVFILLTT TASIAVWVVW IVMYTYGNRQ HNSPTWDDPT LAIALATNAW AFVLFYVIPE
     VSQVTRSSPE QSYQGDLYPT RGVGYETILK EQKGQSMFVE NKAFSMDEPA SAKRPVSPYS
     GYNGQLLTSM YQPTEMTLMH KAPSDGAYDV ILPRATANSQ VTGSANSTLR AEDIYAAQGR
     QEATLPKEGK NSQVFRNPYV WD