ID COLI_MACNE Reviewed; 264 AA. AC P01201; P19403; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 2. DT 02-SEP-2026, entry version 98. 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=Potential peptide; 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 Macaca nemestrina (Pig-tailed macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9545; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-87; GLU-131 AND VAL-147. RX PubMed=3229286; DOI=10.1089/dna.1988.7.627; RA Patel P.D., Sherman T.G., Watson S.J.; RT "Characterization of pro-opiomelanocortin cDNA from the Old World monkey, RT Macaca nemestrina."; RL DNA 7:627-635(1988). RN [2] RP PROTEIN SEQUENCE OF 135-147 AND 214-231, AND AMIDATION AT VAL-147. RX PubMed=13760276; DOI=10.1016/s0021-9258(18)64183-3; RA Lee T.H., Lerner A.B., Buettner-Janusch V.; RT "The isolation and structure of alpha- and beta-melanocyte-stimulating RT hormones from monkey pituitary glands."; RL J. Biol. Chem. 236:1390-1394(1961). CC -!- FUNCTION: Precursor protein of pituitary hormones that are involved in CC diverse physiological processes, including the regulation of energy CC balance, stress response, immune function and skin pigmentation. CC {ECO:0000250|UniProtKB:P01189}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M19658; AAA66022.1; -; mRNA. DR PIR; A31855; CTMKP. DR AlphaFoldDB; P01201; -. DR BMRB; P01201; -. DR SMR; P01201; -. DR STRING; 9545.ENSMNEP00000005588; -. DR GlyCosmos; P01201; 1 site, No reported glycans. DR Proteomes; UP000233120; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. DR GO; GO:0030141; C:secretory granule; IEA:TreeGrafter. DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:TreeGrafter. DR GO; GO:0005179; F:hormone activity; IEA:InterPro. DR GO; GO:2000852; P:regulation of corticosterone secretion; IEA:TreeGrafter. DR InterPro; IPR013531; Mcrtin_ACTH_cent. DR InterPro; IPR013593; Melanocortin_N. DR InterPro; IPR013532; Opioid_neuropept. DR InterPro; IPR001941; PMOC. DR InterPro; IPR050878; POMC-derived_peptides. DR PANTHER; PTHR11416; PRO-OPIOMELANOCORTIN; 1. DR PANTHER; PTHR11416:SF7; PRO-OPIOMELANOCORTIN; 1. 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; 3. 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 Phosphoprotein; Reference proteome; Secreted; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000250" FT PEPTIDE 27..99 FT /note="NPP" FT /id="PRO_0000024985" FT PEPTIDE 77..87 FT /note="Melanotropin gamma" FT /id="PRO_0000024986" FT PEPTIDE 91..131 FT /note="Potential peptide" FT /id="PRO_0000024987" FT PEPTIDE 135..173 FT /note="Corticotropin" FT /id="PRO_0000024988" FT PEPTIDE 135..147 FT /note="Melanocyte-stimulating hormone alpha" FT /id="PRO_0000024989" FT PEPTIDE 153..173 FT /note="Corticotropin-like intermediary peptide" FT /id="PRO_0000024990" FT PEPTIDE 176..264 FT /note="Lipotropin beta" FT /id="PRO_0000024991" FT PEPTIDE 176..231 FT /note="Lipotropin gamma" FT /id="PRO_0000024992" FT PEPTIDE 214..231 FT /note="Melanocyte-stimulating hormone beta" FT /id="PRO_0000024993" FT PEPTIDE 234..264 FT /note="Beta-endorphin" FT /id="PRO_0000024994" FT PEPTIDE 234..238 FT /note="Met-enkephalin" FT /id="PRO_0000024995" FT REGION 88..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..238 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 99..122 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..142 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..186 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 189..199 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 219..234 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 87 FT /note="Phenylalanine amide" FT /evidence="ECO:0000269|PubMed:3229286" FT MOD_RES 131 FT /note="Glutamic acid 1-amide" FT /evidence="ECO:0000269|PubMed:3229286" FT MOD_RES 135 FT /note="N-acetylserine; in Corticotropin" FT /evidence="ECO:0000250|UniProtKB:P01191" FT MOD_RES 147 FT /note="Valine amide" FT /evidence="ECO:0000269|PubMed:13760276, FT ECO:0000269|PubMed:3229286" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01189" FT CARBOHYD 91 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 264 AA; 29172 MW; BC73B100D9BAD052 CRC64; MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC KPDLSAETPV FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSGSAHQK REDVAAGEDR GLLPEGGPEP RGDGAGPGPR EGKRSYSMEH FRWGKPVGKK RRPVKVYPNG AEDESAEAFP LEFKRELTGQ RPRAGDGPDG PADDGAGPRA DLEHSLLVAA EKKDEGPYRM EHFRWGSPPK DKRYGGFMTS EKSQTPLVTL FKNAIIKNAY KKGQ //