ASIP_BOVIN
ID ASIP_BOVIN Reviewed; 133 AA.
AC Q29414; Q3T0R3; Q53Z62;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Agouti-signaling protein;
DE Short=ASP;
DE AltName: Full=Agouti switch protein;
DE Flags: Precursor;
GN Name=ASIP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Kidney;
RX PubMed=15649150; DOI=10.1111/j.1600-0749.2004.00195.x;
RA Girardot M., Martin J., Guibert S., Leveziel H., Julien R., Oulmouden A.;
RT "Widespread expression of the bovine Agouti gene results from at least
RT three alternative promoters.";
RL Pigment Cell Res. 18:34-41(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Royo L.J., Alvarez I., Fernandez I., Arranz J.J., Gomez E., Goyache F.;
RT "Agouti variation within wild-type coat color in cattle is not dependent on
RT changes in the coding sequence of the ASIP gene.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; X99692; CAA68004.1; -; mRNA.
DR EMBL; X99691; CAA68003.1; -; Genomic_DNA.
DR EMBL; AY352659; AAQ56605.2; -; Genomic_DNA.
DR EMBL; AY348953; AAQ56605.2; JOINED; Genomic_DNA.
DR EMBL; AY348954; AAQ56605.2; JOINED; Genomic_DNA.
DR EMBL; BC102291; AAI02292.1; -; mRNA.
DR RefSeq; NP_996674.1; NM_206843.2.
DR AlphaFoldDB; Q29414; -.
DR SMR; Q29414; -.
DR STRING; 9913.ENSBTAP00000045382; -.
DR PaxDb; Q29414; -.
DR Ensembl; ENSBTAT00000048322; ENSBTAP00000045382; ENSBTAG00000034077.
DR GeneID; 404192; -.
DR KEGG; bta:404192; -.
DR CTD; 434; -.
DR VEuPathDB; HostDB:ENSBTAG00000034077; -.
DR VGNC; VGNC:26214; ASIP.
DR eggNOG; ENOG502S5XF; Eukaryota.
DR GeneTree; ENSGT00940000154258; -.
DR HOGENOM; CLU_138633_0_0_1; -.
DR InParanoid; Q29414; -.
DR OMA; TICQCLM; -.
DR OrthoDB; 1556484at2759; -.
DR TreeFam; TF330729; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000034077; Expressed in caput epididymis and 99 other tissues.
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:0031781; F:type 3 melanocortin receptor binding; IEA:Ensembl.
DR GO; GO:0031782; F:type 4 melanocortin receptor binding; IEA:Ensembl.
DR GO; GO:0008343; P:adult feeding behavior; IEA:Ensembl.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
DR GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
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..133
FT /note="Agouti-signaling protein"
FT /id="PRO_0000001024"
FT DOMAIN 94..133
FT /note="Agouti"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT REGION 56..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 101..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 108..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 112..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 117..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ SEQUENCE 133 AA; 14841 MW; 241759680412CE07 CRC64;
MDVSRLLLAT LLVCLCFLTA YSHLAPEEKP RDERNLKNNS SMNLLDFPSV SIVALNKKSK
KISRNEAEKK KRPSKRKAPM KNVARTRPPP PTPCVATRDS CKPPAPACCD PCAFCQCRFF
RSACSCRVLN PTC
