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Agouti-signaling protein (ASP) (Agouti switch protein)

 ASIP_RAT                Reviewed;         131 AA.
Q99JA2;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 92.
RecName: Full=Agouti-signaling protein;
Short=ASP;
AltName: Full=Agouti switch protein;
Flags: Precursor;
Name=Asip {ECO:0000250|UniProtKB:P42127};
Synonyms=A {ECO:0000312|RGD:2003};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:BAB21579.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND POLYMORPHISM.
STRAIN=ACI {ECO:0000269|PubMed:11353396};
TISSUE=Skin {ECO:0000269|PubMed:11353396};
PubMed=11353396; DOI=10.1007/s003350020010;
Kuramoto T., Nomoto T., Sugimura T., Ushijima T.;
"Cloning of the rat agouti gene and identification of the rat
nonagouti mutation.";
Mamm. Genome 12:469-471(2001).
-!- FUNCTION: Involved in the regulation of melanogenesis. The binding
of ASP to MC1R precludes alpha-MSH initiated signaling and thus
blocks production of cAMP, leading to a down-regulation of
eumelanogenesis (brown/black pigment) and thus increasing
synthesis of pheomelanin (yellow/red pigment).
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q03288}.
-!- DOMAIN: The presence of a 'disulfide through disulfide knot'
structurally defines this protein as a knottin. {ECO:0000250}.
-!- POLYMORPHISM: A polymorphism exists that is responsible for the
nonagouti phenotype, characterized by a plain black coat on the
back and belly. This is due to a 19-bp deletion resulting in a
frameshift at position 36 and a premature stop codon at position
48.
-!- POLYMORPHISM: Both strain WKAH (agouti) and strain BN (nonagouti)
contain a substitution at the splice donor site of intron 3,
resulting in a shorter isoform lacking exon 3 which causes reduced
expression levels in strain WKAH and almost undetectable levels in
strain BN. {ECO:0000269|PubMed:11353396}.
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EMBL; AB045587; BAB21564.1; -; mRNA.
EMBL; AB045590; BAB21579.1; -; Genomic_DNA.
RefSeq; NP_443211.1; NM_052979.2.
UniGene; Rn.205372; -.
SMR; Q99JA2; -.
PRIDE; Q99JA2; -.
GeneID; 24152; -.
KEGG; rno:24152; -.
UCSC; RGD:2003; rat.
CTD; 434; -.
RGD; 2003; Asip.
HOGENOM; HOG000111779; -.
HOVERGEN; HBG050593; -.
InParanoid; Q99JA2; -.
KO; K08725; -.
PhylomeDB; Q99JA2; -.
PRO; PR:Q99JA2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
Gene3D; 4.10.760.10; -; 1.
InterPro; IPR007733; Agouti.
InterPro; IPR027300; Agouti_dom.
InterPro; IPR036836; Agouti_dom_sf.
PANTHER; PTHR16551; PTHR16551; 1.
Pfam; PF05039; Agouti; 1.
SMART; SM00792; Agouti; 1.
SUPFAM; SSF57055; SSF57055; 1.
PROSITE; PS60024; AGOUTI_1; 1.
PROSITE; PS51150; AGOUTI_2; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Knottin;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 131 Agouti-signaling protein.
/FTId=PRO_0000001031.
DOMAIN 92 131 Agouti. {ECO:0000255|PROSITE-
ProRule:PRU00494}.
COMPBIAS 57 85 Arg/Lys-rich (basic).
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 92 107 {ECO:0000255|PROSITE-ProRule:PRU00494}.
DISULFID 99 113 {ECO:0000255|PROSITE-ProRule:PRU00494}.
DISULFID 106 124 {ECO:0000255|PROSITE-ProRule:PRU00494}.
DISULFID 110 131 {ECO:0000255|PROSITE-ProRule:PRU00494}.
DISULFID 115 122 {ECO:0000255|PROSITE-ProRule:PRU00494}.
SEQUENCE 131 AA; 14276 MW; 6E45BB22F2075AEB CRC64;
MDVTRLLLAT LVGFLCFLTV HSHLVFEETL GDDRSLKSNS SINSLDFSSV SIVALNKKSK
KISRKEAEKR KRSSKKKASI KKVARPPPPS PCVATRDSCK PPAPACCNPC ASCQCRFFGS
ACTCRVLNPN C


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