COLI_PIG
ID COLI_PIG Reviewed; 267 AA.
AC P01192; Q95246;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Pro-opiomelanocortin;
DE Short=POMC;
DE AltName: Full=Corticotropin-lipotropin;
DE Contains:
DE RecName: Full=NPP;
DE Contains:
DE RecName: Full=Melanotropin gamma;
DE AltName: Full=Gamma-MSH;
DE Contains:
DE RecName: Full=Corticotropin;
DE AltName: Full=Adrenocorticotropic hormone;
DE Short=ACTH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone alpha;
DE Short=Alpha-MSH;
DE AltName: Full=Melanotropin alpha;
DE Contains:
DE RecName: Full=Corticotropin-like intermediary peptide;
DE Short=CLIP;
DE Contains:
DE RecName: Full=Lipotropin beta;
DE AltName: Full=Beta-LPH;
DE Contains:
DE RecName: Full=Lipotropin gamma;
DE AltName: Full=Gamma-LPH;
DE Contains:
DE RecName: Full=Melanocyte-stimulating hormone beta;
DE Short=Beta-MSH;
DE AltName: Full=Melanotropin beta;
DE Contains:
DE RecName: Full=Beta-endorphin;
DE Contains:
DE RecName: Full=Met-enkephalin;
DE Flags: Precursor;
GN Name=POMC;
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=3753882; DOI=10.1016/0167-4781(86)90102-8;
RA Gossard F.J., Chang A.C.Y., Cohen S.N.;
RT "Sequence of the cDNA encoding porcine pro-opiomelanocortin.";
RL Biochim. Biophys. Acta 866:68-74(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6196724; DOI=10.1093/nar/11.22.8063;
RA Boileau G., Barbeau C., Jeannotte L., Chretien M., Drouin J.;
RT "Complete structure of the porcine pro-opiomelanocortin mRNA derived from
RT the nucleotide sequence of cloned cDNA.";
RL Nucleic Acids Res. 11:8063-8071(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7958386; DOI=10.1016/0303-7207(94)90075-2;
RA Gen K., Hirai T., Kato T., Kato Y.;
RT "Presence of the same transcript of pro-opiomelanocortin (POMC) genes in
RT the porcine anterior and intermediate pituitary lobes.";
RL Mol. Cell. Endocrinol. 103:101-108(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6547437; DOI=10.1016/s0021-9258(17)42807-9;
RA Oates E., Herbert E.;
RT "5' sequence of porcine and rat pro-opiomelanocortin mRNA. One porcine and
RT two rat forms.";
RL J. Biol. Chem. 259:7421-7425(1984).
RN [5]
RP PROTEIN SEQUENCE OF 136-174.
RA Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S.,
RA Davis S.B., Eigner E.A., Shakespeare N.E.;
RT "Studies with corticotropin. III. Determination of the structure of beta-
RT corticotropin and its active degradation products.";
RL J. Am. Chem. Soc. 78:5067-5076(1956).
RN [6]
RP SEQUENCE REVISION TO 160 AND 165.
RX PubMed=4334191; DOI=10.1038/newbio235114b0;
RA Riniker B., Sieber P., Rittel W., Zuber H.;
RT "Revised amino-acid sequences for porcine and human adrenocorticotrophic
RT hormone.";
RL Nature New Biol. 235:114-115(1972).
RN [7]
RP SEQUENCE REVISION (CORTICOTROPIN).
RX PubMed=4369114;
RA Graf L.;
RT "Re-examination of the sequence of the C-terminal tryptic fragment from
RT porcine adrenocorticotropic hormone.";
RL Acta Biochim. Biophys. Acad. Sci. Hung. 7:293-297(1972).
RN [8]
RP PROTEIN SEQUENCE OF 136-174.
RX PubMed=2174774; DOI=10.1111/j.1432-1033.1990.tb19447.x;
RA Voigt K., Stegmaier W., McGregor G.P., Roesch H., Seliger H.;
RT "Isolation and full structural characterisation of six adrenocorticotropin-
RT like peptides from porcine pituitary gland. Identification of three novel
RT fragments of adrenocorticotropin and of two forms of a novel
RT adrenocorticotropin-like peptide.";
RL Eur. J. Biochem. 194:225-236(1990).
RN [9]
RP PROTEIN SEQUENCE OF 136-148, AND AMIDATION AT VAL-148.
RX PubMed=13451616; DOI=10.1038/1791346a0;
RA Harris J.I., Lerner A.B.;
RT "Amino-acid sequence of the alpha-melanocyte-stimulating hormone.";
RL Nature 179:1346-1347(1957).
RN [10]
RP PROTEIN SEQUENCE OF 177-267.
RX PubMed=5543613; DOI=10.1016/0005-2795(71)90344-8;
RA Graf L., Barat E., Cseh G., Sajgo M.;
RT "Amino acid sequence of porcine beta-lipotropic hormone.";
RL Biochim. Biophys. Acta 229:276-278(1971).
RN [11]
RP SEQUENCE REVISION (LIPOTROPIN).
RA Gilardeau C., Chretien M.;
RT "Complete amino acid sequence of porcine beta-lipotropic hormone (beta-
RT LPH).";
RL (In) Meienhofer J. (eds.);
RL Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub., Ann
RL Arbor (1972).
RN [12]
RP SEQUENCE REVISION TO 211.
RX PubMed=4673865;
RA Pankov Y.A., Yudaev N.A.;
RT "Complete amino acid sequence in the molecule of porcine beta-lipotropin.";
RL Biokhimiia 37:991-1004(1972).
RN [13]
RP PROTEIN SEQUENCE OF 217-234.
RX PubMed=13348631; DOI=10.1038/178090a0;
RA Harris J.I., Roos P.;
RT "Amino-acid sequence of a melanophore-stimulating peptide.";
RL Nature 178:90-90(1956).
RN [14]
RP PROTEIN SEQUENCE OF 217-234.
RA Geschwind I.I., Li C.H., Barnafi L.;
RT "The structure of the beta-melanocyte-stimulating hormone.";
RL J. Am. Chem. Soc. 79:620-625(1957).
RN [15]
RP PROTEIN SEQUENCE OF 237-241.
RX PubMed=1207728; DOI=10.1038/258577a0;
RA Hughes J., Smith T.W., Kosterlitz H.W., Fothergill L.A., Morgan B.A.,
RA Morris H.R.;
RT "Identification of two related pentapeptides from the brain with potent
RT opiate agonist activity.";
RL Nature 258:577-579(1975).
RN [16]
RP PROTEIN SEQUENCE OF 237-267.
RX PubMed=1007884;
RA Graf L., Barat E., Patthy A.;
RT "Isolation of a COOH-terminal beta-lipotropin fragment (residues 61-91)
RT with morphine-like analgesic activity from porcine pituitary glands.";
RL Acta Biochim. Biophys. Acad. Sci. Hung. 11:121-122(1976).
CC -!- FUNCTION: [Corticotropin]: Stimulates the adrenal glands to release
CC cortisol.
CC -!- FUNCTION: [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide.
CC Increases the pigmentation of skin by increasing melanin production in
CC melanocytes.
CC -!- FUNCTION: [Melanocyte-stimulating hormone beta]: Increases the
CC pigmentation of skin by increasing melanin production in melanocytes.
CC -!- FUNCTION: [Beta-endorphin]: Endogenous orexigenic opiate.
CC -!- FUNCTION: [Met-enkephalin]: Endogenous opiate.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
CC Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored
CC in separate granules in hypothalamic POMC neurons, suggesting that
CC secretion may be under the control of different regulatory mechanisms.
CC {ECO:0000250|UniProtKB:P01193}.
CC -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.
CC -!- PTM: Specific enzymatic cleavages at paired basic residues yield the
CC different active peptides.
CC -!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
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DR EMBL; X03561; CAA27248.1; -; mRNA.
DR EMBL; X00135; CAA24968.1; -; mRNA.
DR EMBL; S73519; AAB32312.1; -; mRNA.
DR PIR; A93496; CTPGP.
DR RefSeq; NP_999023.1; NM_213858.1.
DR AlphaFoldDB; P01192; -.
DR BMRB; P01192; -.
DR SMR; P01192; -.
DR STRING; 9823.ENSSSCP00000024582; -.
DR MetOSite; P01192; -.
DR PaxDb; P01192; -.
DR GeneID; 396863; -.
DR KEGG; ssc:396863; -.
DR CTD; 5443; -.
DR eggNOG; ENOG502RZNY; Eukaryota.
DR InParanoid; P01192; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IMP:AgBase.
DR GO; GO:0043400; P:cortisol secretion; IMP:AgBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:2000852; P:regulation of corticosterone secretion; IBA:GO_Central.
DR InterPro; IPR013531; Mcrtin_ACTH_cent.
DR InterPro; IPR013593; Melanocortin_N.
DR InterPro; IPR013532; Opioid_neuropept.
DR InterPro; IPR001941; PMOC.
DR Pfam; PF00976; ACTH_domain; 3.
DR Pfam; PF08384; NPP; 1.
DR Pfam; PF08035; Op_neuropeptide; 1.
DR PRINTS; PR00383; MELANOCORTIN.
DR SMART; SM01363; ACTH_domain; 2.
DR SMART; SM01364; NPP; 1.
DR SMART; SM01365; Op_neuropeptide; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Endorphin; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT PEPTIDE 27..106
FT /note="NPP"
FT /id="PRO_0000025015"
FT PEPTIDE 77..87
FT /note="Melanotropin gamma"
FT /id="PRO_0000025016"
FT PROPEP 109..133
FT /id="PRO_0000025017"
FT PEPTIDE 136..174
FT /note="Corticotropin"
FT /id="PRO_0000025018"
FT PEPTIDE 136..148
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025019"
FT PEPTIDE 154..174
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000025020"
FT PEPTIDE 177..267
FT /note="Lipotropin beta"
FT /id="PRO_0000025021"
FT PEPTIDE 177..234
FT /note="Lipotropin gamma"
FT /id="PRO_0000025022"
FT PEPTIDE 217..234
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025023"
FT PEPTIDE 237..267
FT /note="Beta-endorphin"
FT /id="PRO_0000025024"
FT PEPTIDE 237..241
FT /note="Met-enkephalin"
FT /id="PRO_0000025025"
FT REGION 88..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:P01190"
FT MOD_RES 136
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000250|UniProtKB:P01191"
FT MOD_RES 148
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:13451616"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 143
FT /note="R -> T"
FT CONFLICT 6
FT /note="G -> S (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="T -> A (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="G -> E (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28895 MW; A6DB487A5032B648 CRC64;
MPRLCGSRSG ALLLTLLLQA SMGVRGWCLE SSQCQDLSTE SNLLACIRAC KPDLSAETPV
FPGNGDAQPL TENPRKYVMG HFRWDRFGRR NGSSSGGGGG GGGAGQKREE EEVAAGEGPG
PRGDGVAPGP RQDKRSYSME HFRWGKPVGK KRRPVKVYPN GAEDELAEAF PLEFRRELAG
APPEPARDPE APAEGAAARA ELEYGLVAEA EAAEKKDEGP YKMEHFRWGS PPKDKRYGGF
MTSEKSQTPL VTLFKNAIVK NAHKKGQ
