MSHR_CANLF
ID MSHR_CANLF Reviewed; 317 AA.
AC O77616;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Melanocyte-stimulating hormone receptor;
DE Short=MSH-R;
DE AltName: Full=Melanocortin receptor 1;
DE Short=MC1-R;
GN Name=MC1R;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT 306-ARG--TRP-317 DEL.
RX PubMed=10895310; DOI=10.1046/j.1365-2052.2000.00639.x;
RA Everts R.E., Rothuizen J., van Oost B.A.;
RT "Identification of a premature stop codon in the melanocyte-stimulating
RT hormone receptor gene (MC1R) in Labrador and Golden retrievers with yellow
RT coat colour.";
RL Anim. Genet. 31:194-199(2000).
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH (By
CC similarity). The activity of this receptor is mediated by G proteins
CC which activate adenylate cyclase (By similarity). Mediates
CC melanogenesis, the production of eumelanin (black/brown) and
CC phaeomelanin (red/yellow), via regulation of cAMP signaling in
CC melanocytes (By similarity). {ECO:0000250|UniProtKB:Q01726}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF064455; AAC33737.2; -; Genomic_DNA.
DR AlphaFoldDB; O77616; -.
DR SMR; O77616; -.
DR InParanoid; O77616; -.
DR Proteomes; UP000002254; Unplaced.
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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
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_0000069798"
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 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 306..317
FT /note="Missing (in Labrador and Golden retriever with
FT yellow coat color)"
FT /evidence="ECO:0000269|PubMed:10895310"
SQ SEQUENCE 317 AA; 34984 MW; F10FDD9552BEF922 CRC64;
MVWQGPQRRL LGSLNGTSPA TPHFELAANQ TGPRCLEVSI PNGLFLSLGL VSVVENVLVV
AAIAKNRNLH SPMYYFIGCL AVSDLLVSVT NVLETAVMLL VEAGALAAQA AVVQQLDDII
DVLICGSMVS SLCFLGAIAV DRYLSIFYAL RYHSIVTLPR AWRAISAIWV ASVLSSTLFI
AYYNHTAVLL CLVSFFVAML VLMAVLYVHM LARARQHARG IARLRKRQHS VHQGFGLKGA
ATLTILLGIF FLCWGPFFLH LSLMVLCPQH PICGCVFQNF NLFLTLIICN SIIDPFIYAF
RSQELRKTLQ EVVLCSW
