ASIP_PANPA
ID ASIP_PANPA Reviewed; 132 AA.
AC Q1XGV6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Agouti-signaling protein;
DE Short=ASP;
DE AltName: Full=Agouti switch protein;
DE Flags: Precursor;
GN Name=ASIP;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16597585; DOI=10.1101/gr.4763906;
RA Nakayama K., Ishida T.;
RT "Alu-mediated 100-kb deletion in the primate genome: the loss of the agouti
RT signaling protein gene in the lesser apes.";
RL Genome Res. 16:485-490(2006).
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; AB236870; BAE93018.1; -; Genomic_DNA.
DR RefSeq; XP_008955444.1; XM_008957196.1.
DR AlphaFoldDB; Q1XGV6; -.
DR STRING; 9597.XP_008955444.1; -.
DR Ensembl; ENSPPAT00000038463; ENSPPAP00000015772; ENSPPAG00000031015.
DR GeneID; 100974762; -.
DR KEGG; pps:100974762; -.
DR CTD; 434; -.
DR eggNOG; ENOG502S5XF; Eukaryota.
DR GeneTree; ENSGT00940000154258; -.
DR OMA; TICQCLM; -.
DR Proteomes; UP000240080; Chromosome 20.
DR Bgee; ENSPPAG00000031015; Expressed in heart and 5 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:InterPro.
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..132
FT /note="Agouti-signaling protein"
FT /id="PRO_0000235200"
FT DOMAIN 93..132
FT /note="Agouti"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT REGION 61..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
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 93..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 100..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 107..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 111..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT DISULFID 116..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
SQ SEQUENCE 132 AA; 14593 MW; BE8BE65C76344791 CRC64;
MDVTRLLLAT LLVFLCFFTA NSHLPPEEKL RDDRSLRSNS SVNLLDFPSV SIVALNKKSK
QIGRKEAEKK RSSKKEASMK KVARPRTPLS APCVATRNSC KPPAPACCDP CASCQCRFFR
SACSCRVLSL NC