ID   GPC5C_RAT               Reviewed;         441 AA.
AC   Q3KRC4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=G-protein coupled receptor family C group 5 member C;
DE   Flags: Precursor;
GN   Name=Gprc5c;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI05782.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC105781; AAI05782.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q3KRC4; -.
DR   STRING; 10116.ENSRNOP00000004256; -.
DR   GlyGen; Q3KRC4; 1 site.
DR   iPTMnet; Q3KRC4; -.
DR   PhosphoSitePlus; Q3KRC4; -.
DR   PaxDb; Q3KRC4; -.
DR   PRIDE; Q3KRC4; -.
DR   RGD; 1311408; Gprc5c.
DR   eggNOG; ENOG502QQEH; Eukaryota.
DR   InParanoid; Q3KRC4; -.
DR   PhylomeDB; Q3KRC4; -.
DR   PRO; PR:Q3KRC4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070062; C:extracellular exosome; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; 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   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..441
FT                   /note="G-protein coupled receptor family C group 5 member
FT                   C"
FT                   /id="PRO_0000251136"
FT   TOPO_DOM        23..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..119
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          419..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         413
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         422
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ84"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  48449 MW;  C5185C88E1E4E687 CRC64;
     MATHKTLLMC LGLPLFFPGA LAQNHAPPGC SPDLDPLYYN LCDRSGAWGI VLEAVAGAGI
     ITTFVLTIIL VASLPFVQDT KKRSLLGTQV FFLLGTLGLF CLVFACVVKP DFSTCASRRF
     LFGVLFAICF SCLIAHTLSL NFLARKNHGP RGWVIFTVAL LLTLVEVIIN TEWLIITLVR
     GGGQVSTPGN GSADWTVTSP CAIANMDFVM ALIYVMLLLL AAFLGAWPTL CGRFKRWRKH
     GVFVLLTTAT SIAIWVVWIV MYTYGNKQHH SPTWDDPTLA IALAANAWTF VFFYVIPEVS
     QVTKPSPEQS YQGDMYPTRG VGYETILKEQ TGQSMFVENK AFSMDEPASA KRPVSPYSGY
     NGQLLTSVYQ PTEMALMHKG PSEGAYDVIL PRATANSQVM GSANSTLRAE DMYMVQSHQV
     ATPTKDGKIS QDQSPKNKTR W