MSHR_BOVIN
ID MSHR_BOVIN Reviewed; 317 AA.
AC P47798; Q28025;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Melanocyte-stimulating hormone receptor;
DE Short=MSH-R;
DE AltName: Full=BDF3;
DE AltName: Full=Melanocortin receptor 1;
DE Short=MC1-R;
GN Name=MC1R; Synonyms=MSHR;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8034052; DOI=10.1016/0014-5793(94)00619-9;
RA Vanetti M., Schoenrock C., Meyerhof W., Hoellt V.;
RT "Molecular cloning of a bovine MSH receptor which is highly expressed in
RT the testis.";
RL FEBS Lett. 348:268-272(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein;
RX PubMed=8661706; DOI=10.1007/s003359900090;
RA Joerg H., Fries H.R., Meijerink E., Stranzinger G.F.;
RT "Red coat color in Holstein cattle is associated with a deletion in the
RT MSHR gene.";
RL Mamm. Genome 7:317-318(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10628296; DOI=10.1111/j.1601-5223.1999.00039.x;
RA Klungland H., Roed K.H., Nesbo C.L., Jakobsen K.S., Vage D.I.;
RT "The melanocyte-stimulating hormone receptor (MC1-R) gene as a tool in
RT evolutionary studies of artiodactyles.";
RL Hereditas 131:39-46(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein;
RA Kriegesmann B., Brenig B., Dierkes B., Jansen S.;
RT "A new melanocortin 1-receptor allele is coupled with Agouti coat colour
RT pattern in Holstein cattle.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for MSH (alpha, beta) and ACTH (PubMed:8034052).
CC Does not seem to be active with gamma-MSH (PubMed:8034052). The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase (PubMed:8034052). Mediates melanogenesis, the
CC production of eumelanin (black/brown) and phaeomelanin (red/yellow),
CC via regulation of cAMP signaling in melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q01726, ECO:0000269|PubMed:8034052}.
CC -!- SUBUNIT: Interacts with MGRN1, but does not undergo MGRN1-mediated
CC ubiquitination; this interaction competes with GNAS-binding and thus
CC inhibits agonist-induced cAMP production. Interacts with OPN3; the
CC interaction results in a decrease in MC1R-mediated cAMP signaling and
CC ultimately a decrease in melanin production in melanocytes.
CC {ECO:0000250|UniProtKB:Q01726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01726};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis.
CC {ECO:0000269|PubMed:8034052}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; S71017; AAB31361.1; -; mRNA.
DR EMBL; U39469; AAC48590.2; -; Genomic_DNA.
DR EMBL; Y13957; CAA74291.1; -; Genomic_DNA.
DR EMBL; Y19103; CAB64818.1; -; Genomic_DNA.
DR PIR; S45708; S45708.
DR AlphaFoldDB; P47798; -.
DR SMR; P47798; -.
DR STRING; 9913.ENSBTAP00000055607; -.
DR PaxDb; P47798; -.
DR PRIDE; P47798; -.
DR Ensembl; ENSBTAT00000032494; ENSBTAP00000055607; ENSBTAG00000023731.
DR VEuPathDB; HostDB:ENSBTAG00000023731; -.
DR VGNC; VGNC:106814; MC1R.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_13_0_1; -.
DR InParanoid; P47798; -.
DR OMA; FFCTTLV; -.
DR TreeFam; TF332646; -.
DR Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000023731; Expressed in spermatid and 47 other tissues.
DR ExpressionAtlas; P47798; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001671; Melcrt_ACTH_rcpt.
DR InterPro; IPR000761; MSH_rcpt.
DR PANTHER; PTHR22750:SF2; PTHR22750:SF2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00534; MCRFAMILY.
DR PRINTS; PR00536; MELNOCYTESHR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000069793"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 40..41
FT /note="IP -> SL (in Ref. 1; AAB31361)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="L -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 34916 MW; 123692614F7FF168 CRC64;
MPALGSQRRL LGSLNCTPPA TLPFTLAPNR TGPQCLEVSI PDGLFLSLGL VSLVENVLVV
AAIAKNRNLH SPMYYFICCL AVSDLLVSVS NVLETAVMLL LEAGVLATQA AVVQQLDNVI
DVLICGSMVS SLCFLGAIAV DRYISIFYAL RYHSVVTLPR AWRIIAAIWV ASILTSLLFI
TYYNHKVILL CLVGLFIAML ALMAVLYVHM LARACQHARG IARLQKRQRP IHQGFGLKGA
ATLTILLGVF FLCWGPFFLH LSLIVLCPQH PTCGCIFKNF NLFLALIICN AIVDPLIYAF
RSQELRKTLQ EVLQCSW
