ID   ASIP_CALGO              Reviewed;         132 AA.
AC   A1YL80;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Callimico goeldii (Goeldi's marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callimico.
OX   NCBI_TaxID=9495;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF094497; ABL84295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YL80; -.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Knottin; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..132
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000285051"
FT   DOMAIN          93..132
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          61..93
FT                   /note="Disordered"
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;  14627 MW;  D3DBC8964AABC220 CRC64;
     MDVTRLLLAT LLVFLCFFAA YSHLPPEEKL RDDRSLRSNS SVNLLDLPSV SIVALNKKSK
     KISRKEAEKK RSSKKEASKQ KVARPRTPLS VPCVSTRGSC KPPAPACCHP CASCQCRFFR
     SACSCRVLNV NC