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