MSHR_CHICK
ID MSHR_CHICK Reviewed; 314 AA.
AC P55167;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rock-Cornish breed;
RX PubMed=8634326; DOI=10.1016/0167-4781(96)00026-7;
RA Takeuchi S., Suzuki H., Hirose S., Yabuuchi M., Sato C., Yamamoto H.,
RA Takahashi S.;
RT "Molecular cloning and sequence analysis of the chick melanocortin 1-
RT receptor gene.";
RL Biochim. Biophys. Acta 1306:122-126(1996).
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 via regulation of cAMP signaling in melanocytes (By
CC similarity). {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; D78272; BAA11336.1; -; Genomic_DNA.
DR PIR; S70005; S70005.
DR PIR; S71420; S71420.
DR AlphaFoldDB; P55167; -.
DR SMR; P55167; -.
DR STRING; 9031.ENSGALP00000038021; -.
DR VEuPathDB; HostDB:geneid_427562; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P55167; -.
DR PhylomeDB; P55167; -.
DR Proteomes; UP000000539; 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; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Melanocyte-stimulating hormone receptor"
FT /id="PRO_0000069859"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 312
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 35297 MW; 10C64A57B0C75EB0 CRC64;
MSMLAPLRLV REPWNASEGN QSNATAGAGG AWCQGLDIPN ELFLTLGLVS LVENLLVVAA
ILKNRNLHSP TYYFICCLAV SDMLVSVSNL AKTLFMLLME HGVLVIRASI VRHMDNVIDM
LICSSVVSSL SFLGVIAVDR YITIFYALRY HSIMTLQRAV VTMASVWLAS TVSSTVLITY
YRNNAILLCL IGFFLFMLVL MLVLYIHMFA LACHHVRSIS SQQKQPTIYR TSSLKGAVTL
TILLGVFFIC WGPFFFHLIL IVTCPTNPFC TCFFSYFNLF LILIICNSVV DPLIYAFRSQ
ELRRTLREVV LCSW
