ID   ASIP_MACMU              Reviewed;         132 AA.
AC   A1YL67; A8CEL9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17143587; DOI=10.1007/s00335-006-0056-0;
RA   Mundy N.I., Kelly J.;
RT   "Investigation of the role of the agouti signaling protein gene (ASIP) in
RT   coat color evolution in primates.";
RL   Mamm. Genome 17:1205-1213(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nakayama K., Shotake T., Takenaka O., Ishida T.;
RT   "Association of the agouti signaling protein gene with coat color variation
RT   in the macaques.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of melanogenesis. The binding of
CC       ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks
CC       production of cAMP, leading to a down-regulation of eumelanogenesis
CC       (brown/black pigment) and thus increasing synthesis of pheomelanin
CC       (yellow/red pigment) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
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DR   EMBL; EF094484; ABL84282.1; -; Genomic_DNA.
DR   EMBL; AB299207; BAF80791.1; -; Genomic_DNA.
DR   RefSeq; XP_015004667.1; XM_015149181.1.
DR   AlphaFoldDB; A1YL67; -.
DR   STRING; 9544.ENSMMUP00000037733; -.
DR   Ensembl; ENSMMUT00000104405; ENSMMUP00000077604; ENSMMUG00000061171.
DR   GeneID; 709156; -.
DR   KEGG; mcc:709156; -.
DR   CTD; 434; -.
DR   VEuPathDB; HostDB:ENSMMUG00000061171; -.
DR   eggNOG; ENOG502S5XF; Eukaryota.
DR   GeneTree; ENSGT00940000154258; -.
DR   HOGENOM; CLU_2746535_0_0_1; -.
DR   InParanoid; A1YL67; -.
DR   Proteomes; UP000006718; Chromosome 10.
DR   Bgee; ENSMMUG00000061171; Expressed in heart and 9 other tissues.
DR   ExpressionAtlas; A1YL67; baseline.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0031779; F:melanocortin receptor binding; IBA:GO_Central.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
DR   GO; GO:0031781; F:type 3 melanocortin receptor binding; IEA:Ensembl.
DR   GO; GO:0031782; F:type 4 melanocortin receptor binding; IEA:Ensembl.
DR   GO; GO:0008343; P:adult feeding behavior; IEA:Ensembl.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
DR   GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR   GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IBA:GO_Central.
DR   Gene3D; 4.10.760.10; -; 1.
DR   InterPro; IPR007733; Agouti.
DR   InterPro; IPR027300; Agouti_dom.
DR   InterPro; IPR036836; Agouti_dom_sf.
DR   PANTHER; PTHR16551; PTHR16551; 1.
DR   Pfam; PF05039; Agouti; 1.
DR   SMART; SM00792; Agouti; 1.
DR   SUPFAM; SSF57055; SSF57055; 1.
DR   PROSITE; PS60024; AGOUTI_1; 1.
DR   PROSITE; PS51150; AGOUTI_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Knottin; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..132
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000285056"
FT   DOMAIN          93..132
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          61..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        100..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        107..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        111..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        116..123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ   SEQUENCE   132 AA;  14692 MW;  1E00D5F449A95D43 CRC64;
     MDVTRLLLAT LLVFLCFFTA YSHLPPEEKL RDDRSLRSNS SVNLLDFPSV SIMALNKNSK
     EISRKEAEKK RSSKKEASMK KVARPRTPLS APCVATRDSC KPPAPACCDP CASCQCRFFR
     SACSCRVLSL NC