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ASIP_CANLF
ID   ASIP_CANLF              Reviewed;         131 AA.
AC   Q5UK76;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CYS-96.
RX   PubMed=15520882; DOI=10.1007/s00335-004-2377-1;
RA   Kerns J.A., Newton J., Berryere T.G., Rubin E.M., Cheng J.F., Schmutz S.M.,
RA   Barsh G.S.;
RT   "Characterization of the dog Agouti gene and a nonagoutimutation in German
RT   Shepherd dogs.";
RL   Mamm. Genome 15:798-808(2004).
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).
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; AY714374; AAV48541.1; -; mRNA.
DR   RefSeq; NP_001007264.1; NM_001007263.1.
DR   AlphaFoldDB; Q5UK76; -.
DR   STRING; 9612.ENSCAFP00000034367; -.
DR   PaxDb; Q5UK76; -.
DR   GeneID; 492296; -.
DR   KEGG; cfa:492296; -.
DR   CTD; 434; -.
DR   eggNOG; ENOG502S5XF; Eukaryota.
DR   InParanoid; Q5UK76; -.
DR   Proteomes; UP000002254; 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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Knottin; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..131
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000001025"
FT   DOMAIN          92..131
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          57..93
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"
FT   VARIANT         96
FT                   /note="R -> C (in strain: Black German Shepherd)"
FT                   /evidence="ECO:0000269|PubMed:15520882"
SQ   SEQUENCE   131 AA;  14505 MW;  4204DDB437B49954 CRC64;
     MNIFRLLLAT LLVSLCFLTA YSHLAEEKPK DDRSLRSNSS VNLLDFPSVS IVALNKKSKK
     ISRKEAEKKR SSKKKASMKN VARPRPPPPT PCVATRNSCK SPAPACCDPC ASCQCRFFRS
     ACTCRVLSPR C
 
 
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