ID   ASIP_PAPAN              Reviewed;         132 AA.
AC   A1YL70;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
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).
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; EF094487; ABL84285.1; -; Genomic_DNA.
DR   RefSeq; NP_001157803.1; NM_001164331.1.
DR   RefSeq; XP_009214555.1; XM_009216291.1.
DR   RefSeq; XP_009214556.1; XM_009216292.2.
DR   RefSeq; XP_009214557.1; XM_009216293.2.
DR   RefSeq; XP_009214559.1; XM_009216295.2.
DR   RefSeq; XP_009214560.1; XM_009216296.2.
DR   RefSeq; XP_009214561.1; XM_009216297.2.
DR   RefSeq; XP_009214562.1; XM_009216298.2.
DR   AlphaFoldDB; A1YL70; -.
DR   STRING; 9555.ENSPANP00000016805; -.
DR   Ensembl; ENSPANT00000013706; ENSPANP00000016805; ENSPANG00000022711.
DR   GeneID; 100302661; -.
DR   KEGG; panu:100302661; -.
DR   CTD; 434; -.
DR   eggNOG; ENOG502S5XF; Eukaryota.
DR   GeneTree; ENSGT00940000154258; -.
DR   HOGENOM; CLU_138633_0_0_1; -.
DR   OMA; TICQCLM; -.
DR   Proteomes; UP000028761; Chromosome 16.
DR   Bgee; ENSPANG00000022711; Expressed in thyroid gland and 27 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR   GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IEA:Ensembl.
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_0000285060"
FT   DOMAIN          93..132
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          62..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..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;  14673 MW;  5B55C1E44DBD0812 CRC64;
     MDVTRLLLAT LLVFLCFFTA YSHLPPEEKL RDDRSLRSNS SVNLLDFPSV SIVALNKKSK
     QISRKEAEKK RSSKKEASMK KVARPRTPLS APCVATRDSC KPPAPACCDP CASCQCRFFR
     SACSCRVLSL NC