ID   ASIP_PIG                Reviewed;         131 AA.
AC   Q6ZYM3; Q4R1H8; Q5QJU6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Agouti-signaling protein;
DE            Short=ASP;
DE   AltName: Full=Agouti switch protein;
DE   Flags: Precursor;
GN   Name=ASIP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11105218; DOI=10.1046/j.1365-2052.2000.00656.x;
RA   Leeb T., Deppe A., Kriegesmann B., Brenig B.;
RT   "Genomic structure and nucleotide polymorphisms of the porcine agouti
RT   signalling protein gene (ASIP).";
RL   Anim. Genet. 31:335-336(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16416091; DOI=10.1007/s00335-005-0104-1;
RA   Droegemueller C., Giese A., Martins-Wess F., Wiedemann S., Andersson L.,
RA   Brenig B., Fries R., Leeb T.;
RT   "The mutation causing the black-and-tan pigmentation phenotype of
RT   Mangalitza pigs maps to the porcine ASIP locus but does not affect its
RT   coding sequence.";
RL   Mamm. Genome 17:58-66(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-68.
RA   Shi K., Deng X., Wang A., Li N.;
RT   "Single nucleotide polymorphism analysis on the exons of porcine Agouti
RT   signaling protein.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shi K., Wang A., Li N.;
RT   "Single nucleotide polymorphisms (SNPs) analysis on the extension (MC1R),
RT   the white (KIT) and the agouti (ASIP) loci and their association with coat
RT   color phenotypes of pigs.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Okumura N., Nii M., Hamasima N.;
RT   "Expression of agouti signaling protein gene (ASIP) in pig.";
RL   Submitted (MAR-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; AJ634673; CAG25494.1; -; mRNA.
DR   EMBL; AJ634674; CAG25495.1; -; mRNA.
DR   EMBL; AJ634675; CAG25496.1; -; mRNA.
DR   EMBL; AJ634676; CAG25497.1; -; mRNA.
DR   EMBL; AJ634677; CAG25498.1; -; mRNA.
DR   EMBL; AJ427478; CAD20602.1; -; Genomic_DNA.
DR   EMBL; AY308996; AAQ84057.1; -; mRNA.
DR   EMBL; AY308997; AAQ84058.1; -; mRNA.
DR   EMBL; AY308998; AAQ84059.1; -; mRNA.
DR   EMBL; AY916525; AAX18261.1; -; Genomic_DNA.
DR   EMBL; AB206998; BAD99575.1; -; Genomic_DNA.
DR   RefSeq; NP_001001648.1; NM_001001648.4.
DR   RefSeq; NP_001011646.1; NM_001011646.1.
DR   RefSeq; NP_001011647.1; NM_001011647.1.
DR   RefSeq; NP_001011648.1; NM_001011648.1.
DR   RefSeq; XP_005672916.1; XM_005672859.2.
DR   RefSeq; XP_005672917.1; XM_005672860.2.
DR   RefSeq; XP_013840735.1; XM_013985281.1.
DR   RefSeq; XP_013840736.1; XM_013985282.1.
DR   AlphaFoldDB; Q6ZYM3; -.
DR   STRING; 9823.ENSSSCP00000007749; -.
DR   PaxDb; Q6ZYM3; -.
DR   PRIDE; Q6ZYM3; -.
DR   Ensembl; ENSSSCT00015008116; ENSSSCP00015003271; ENSSSCG00015006092.
DR   Ensembl; ENSSSCT00055035573; ENSSSCP00055028261; ENSSSCG00055018086.
DR   Ensembl; ENSSSCT00055035616; ENSSSCP00055028291; ENSSSCG00055018086.
DR   Ensembl; ENSSSCT00055035668; ENSSSCP00055028325; ENSSSCG00055018086.
DR   Ensembl; ENSSSCT00065059549; ENSSSCP00065025835; ENSSSCG00065043527.
DR   Ensembl; ENSSSCT00065059553; ENSSSCP00065025839; ENSSSCG00065043527.
DR   Ensembl; ENSSSCT00065059557; ENSSSCP00065025841; ENSSSCG00065043527.
DR   Ensembl; ENSSSCT00070011962; ENSSSCP00070009858; ENSSSCG00070006270.
DR   Ensembl; ENSSSCT00070011967; ENSSSCP00070009860; ENSSSCG00070006270.
DR   Ensembl; ENSSSCT00070011970; ENSSSCP00070009863; ENSSSCG00070006270.
DR   Ensembl; ENSSSCT00070011986; ENSSSCP00070009874; ENSSSCG00070006270.
DR   Ensembl; ENSSSCT00070011994; ENSSSCP00070009881; ENSSSCG00070006270.
DR   GeneID; 414439; -.
DR   KEGG; ssc:414439; -.
DR   CTD; 434; -.
DR   eggNOG; ENOG502S5XF; Eukaryota.
DR   HOGENOM; CLU_138633_0_0_1; -.
DR   InParanoid; Q6ZYM3; -.
DR   OMA; TICQCLM; -.
DR   TreeFam; TF330729; -.
DR   ChiTaRS; ASIP; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 17.
DR   Genevisible; Q6ZYM3; SS.
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..131
FT                   /note="Agouti-signaling protein"
FT                   /id="PRO_0000001030"
FT   DOMAIN          92..131
FT                   /note="Agouti"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00494"
FT   REGION          58..92
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        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         68
FT                   /note="E -> K"
FT                   /evidence="ECO:0000269|Ref.3"
SQ   SEQUENCE   131 AA;  14498 MW;  05BBBAB9E765B68D CRC64;
     MDVTRLLLAT LLVCLCFFTA SSHLAPEEKS KDERSLRSNS SMNLLDFPSV SIVALNKKSK
     KISRKEAEKR SSKKKASMKK VAQPRPPRPA PCVANRDSCK PPALACCDPC AFCQCRFFRS
     ACSCRVLNPT C