MSHR_MAMPR
ID MSHR_MAMPR Reviewed; 317 AA.
AC Q0Q460;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 54.
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 Mammuthus primigenius (Siberian woolly mammoth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Mammuthus.
OX NCBI_TaxID=37349;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-21; CYS-67 AND SER-301.
RX PubMed=16825562; DOI=10.1126/science.1128994;
RA Roempler H., Rohland N., Lalueza-Fox C., Willerslev E., Kuznetsova T.,
RA Rabeder G., Bertranpetit J., Schoeneberg T., Hofreiter M.;
RT "Nuclear gene indicates coat-color polymorphism in mammoths.";
RL Science 313:62-62(2006).
CC -!- FUNCTION: Receptor for MSH (alpha, beta and gamma) and ACTH. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase. Mediates melanogenesis, the production of eumelanin
CC (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP
CC signaling in melanocytes. {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 -!- POLYMORPHISM: Allele 2 is much less active than allele 1 and would have
CC probably resulted in mammoths with a substantially lighter hair color.
CC {ECO:0000305|PubMed:16825562}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; DQ648860; ABG37012.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0Q460; -.
DR SMR; Q0Q460; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004980; F:melanocyte-stimulating hormone receptor activity; IEA:InterPro.
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; Extinct organism protein; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000286434"
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 REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VARIANT 21
FT /note="T -> A (in allele 2)"
FT /evidence="ECO:0000269|PubMed:16825562"
FT VARIANT 67
FT /note="R -> C (in allele 2)"
FT /evidence="ECO:0000269|PubMed:16825562"
FT VARIANT 301
FT /note="R -> S (in allele 2)"
FT /evidence="ECO:0000269|PubMed:16825562"
SQ SEQUENCE 317 AA; 34944 MW; E95B945790D7A9E4 CRC64;
MPMQGAQGRL RGSLNATPPT TPHSGLAGNQ TGPWCLEVSI PDELFLSLGL VSLVENMLVV
AAIAKNRNLH SPMYYFICCL AVSDLLVSVS NVLETAVMLL LEAGVLAAWA GVVQQLDNAI
DVFICGSMVS SLCFLGAIAV DRYITIFYAL RYHSIVTLPR ARWAIATIWA ASVVCSTLFI
AYYDCTAVLL CLVSFFLALV VLMAVLYMHM LARACLHARS IARLHKRWRP VHQGLGLKGA
ATLSILLGSF FLCWGPFFLH LTLIVLCPQH PTCSCVFKNF KLFLTLIICN SIVDPLIYAF
RSQELRKTLK EVLLCSW
