ID   ASIP_FELCA              Reviewed;         135 AA.
AC   Q865F0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate Fca273;
RX   PubMed=12620197; DOI=10.1016/s0960-9822(03)00128-3;
RA   Eizirik E., Yuhki N., Johnson W.E., Menotti-Raymond M., Hannah S.S.,
RA   O'Brien S.J.;
RT   "Molecular genetics and evolution of melanism in the cat family.";
RL   Curr. Biol. 13:448-453(2003).
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; AY237394; AAO62411.1; -; Genomic_DNA.
DR   RefSeq; NP_001009190.1; NM_001009190.1.
DR   RefSeq; XP_006929845.1; XM_006929783.2.
DR   RefSeq; XP_019681722.1; XM_019826163.1.
DR   RefSeq; XP_019681723.1; XM_019826164.1.
DR   RefSeq; XP_019681724.1; XM_019826165.1.
DR   RefSeq; XP_019681725.1; XM_019826166.1.
DR   RefSeq; XP_019681726.1; XM_019826167.1.
DR   RefSeq; XP_019681727.1; XM_019826168.1.
DR   RefSeq; XP_019681728.1; XM_019826169.1.
DR   AlphaFoldDB; Q865F0; -.
DR   STRING; 9685.ENSFCAP00000010252; -.
DR   GeneID; 492297; -.
DR   KEGG; fca:492297; -.
DR   CTD; 434; -.
DR   eggNOG; ENOG502S5XF; Eukaryota.
DR   HOGENOM; CLU_138633_0_0_1; -.
DR   InParanoid; Q865F0; -.
DR   OMA; TICQCLM; -.
DR   TreeFam; TF330729; -.
DR   Proteomes; UP000011712; Unplaced.
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:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
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..135
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000001026"
FT   DOMAIN          96..135
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          56..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..82
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..99
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        103..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        110..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        114..135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   DISULFID        119..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ   SEQUENCE   135 AA;  14948 MW;  FF748AE9C862E489 CRC64;
     MNILRLLLAT LLVCLCLLTA YSHLAPEEKP RDDRNLRSNS SMNMLDLSSV SIVALNKKSK
     KISRKEAEKK RSSKKKASMK NVAQPRRPRP PPPAPCVATR DSCKPPAPAC CDPCASCQCR
     FFRSSCSCRV LNPTC