ID   ASIP_VULVU              Reviewed;         131 AA.
AC   P79407;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 14.
RA   Vage D.I.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-125.
RC   TISSUE=Skin;
RX   PubMed=9054949; DOI=10.1038/ng0397-311;
RA   Vage D.I., Lu D., Klungland J., Lien S., Adalsteinsson S., Cone R.D.;
RT   "A non-epistatic interaction of agouti and extension in the fox, Vulpes
RT   vulpes.";
RL   Nat. Genet. 15:311-315(1997).
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; Y09877; CAA71004.2; -; mRNA.
DR   AlphaFoldDB; P79407; -.
DR   STRING; 9627.ENSVVUP00000005760; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Knottin; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..131
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000001032"
FT   DOMAIN          92..131
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          57..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..80
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   DISULFID        92..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        99..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        106..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        110..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        115..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ   SEQUENCE   131 AA;  14449 MW;  42185147E5B49954 CRC64;
     MNIFRLLLAT LLVSLCFLTA YSHLAEEKPK DDRSLRSNSS VNLLDFPSVS IVALNKKSKK
     ISRKEAEKKR SSKKKASMKN VARPRPPPPN PCVATRNSCK SPAPACCDPC ASCQCRFFRS
     ACTCRVLSPS C