ID   ASIP_HORSE              Reviewed;         133 AA.
AC   Q95MP2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11353392; DOI=10.1007/s003350020017;
RA   Rieder S., Taourit S., Mariat D., Langlois B., Guerin G.;
RT   "Mutations in the agouti (ASIP), the extension (MC1R), and the brown
RT   (TYRP1) loci and their association to coat color phenotypes in horses
RT   (Equus caballus).";
RL   Mamm. Genome 12:450-455(2001).
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; AF288358; AAK70925.1; -; Genomic_DNA.
DR   RefSeq; NP_001157489.1; NM_001164017.1.
DR   AlphaFoldDB; Q95MP2; -.
DR   STRING; 9796.ENSECAP00000003317; -.
DR   PaxDb; Q95MP2; -.
DR   Ensembl; ENSECAT00000004772; ENSECAP00000003317; ENSECAG00000004241.
DR   GeneID; 100054335; -.
DR   KEGG; ecb:100054335; -.
DR   CTD; 434; -.
DR   VGNC; VGNC:15585; ASIP.
DR   GeneTree; ENSGT00940000154258; -.
DR   HOGENOM; CLU_138633_0_0_1; -.
DR   InParanoid; Q95MP2; -.
DR   OMA; TICQCLM; -.
DR   OrthoDB; 1556484at2759; -.
DR   TreeFam; TF330729; -.
DR   Proteomes; UP000002281; Chromosome 22.
DR   Bgee; ENSECAG00000004241; Expressed in liver and 12 other tissues.
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..133
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000001027"
FT   DOMAIN          94..133
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          26..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        101..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        108..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        112..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        117..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ   SEQUENCE   133 AA;  14780 MW;  332CE78470392507 CRC64;
     MDVIHLFLAT LLVSLCFLTA YSHLSPEEKP KDDRSLRNNS SMNLLDSPSV SIMALNKKSK
     KISRKEAEKK KRSSKKKASM TKVARPRLLQ PAPCVATRDS CKPPAPACCD PCASCQCRFF
     RSACSCRVLT RTC