COLI_RAT
ID COLI_RAT Reviewed; 235 AA.
AC P01194;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 127.
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; Synonyms=Pomc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998878; DOI=10.1016/0014-5793(85)80078-8;
RA Drouin J., Chamberland M., Charron J., Jeannotte L., Nemer M.;
RT "Structure of the rat pro-opiomelanocortin (POMC) gene.";
RL FEBS Lett. 193:54-58(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-235.
RX PubMed=6255341; DOI=10.1038/288610a0;
RA Drouin J., Goodman H.M.;
RT "Most of the coding region of rat ACTH beta-LPH precursor gene lacks
RT intervening sequences.";
RL Nature 288:610-613(1980).
RN [4]
RP PROTEIN SEQUENCE OF 76-100.
RC TISSUE=Pituitary;
RX PubMed=7259753; DOI=10.1016/s0006-291x(81)80101-5;
RA Browne C.A., Bennett H.P., Solomon S.;
RT "The isolation of characterization of gamma 3-melanotropin from the
RT neurointermediary lobe of the rat pituitary.";
RL Biochem. Biophys. Res. Commun. 100:336-343(1981).
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; X03176; CAA26937.1; -; Genomic_DNA.
DR EMBL; K01877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00759; AAA41903.1; -; Genomic_DNA.
DR EMBL; K01878; AAA41903.1; JOINED; Genomic_DNA.
DR PIR; A91353; CTRTP.
DR AlphaFoldDB; P01194; -.
DR SMR; P01194; -.
DR STRING; 10116.ENSRNOP00000016976; -.
DR GlyGen; P01194; 1 site.
DR PaxDb; P01194; -.
DR PRIDE; P01194; -.
DR RGD; 3366; Pomc.
DR eggNOG; ENOG502RZNY; Eukaryota.
DR InParanoid; P01194; -.
DR PhylomeDB; P01194; -.
DR Reactome; R-RNO-111885; Opioid Signalling.
DR Reactome; R-RNO-193048; Androgen biosynthesis.
DR Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-209952; Peptide hormone biosynthesis.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P01194; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0070996; F:type 1 melanocortin receptor binding; ISO:RGD.
DR GO; GO:0031781; F:type 3 melanocortin receptor binding; ISO:RGD.
DR GO; GO:0031782; F:type 4 melanocortin receptor binding; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:0033059; P:cellular pigmentation; ISO:RGD.
DR GO; GO:0007631; P:feeding behavior; NAS:RGD.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
DR GO; GO:0140668; P:positive regulation of oxytocin production; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032098; P:regulation of appetite; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:2000852; P:regulation of corticosterone secretion; ISO:RGD.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; ISO:RGD.
DR GO; GO:1990680; P:response to melanocyte-stimulating hormone; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
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 Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT PEPTIDE 27..100
FT /note="NPP"
FT /id="PRO_0000025029"
FT PEPTIDE 77..87
FT /note="Melanotropin gamma"
FT /id="PRO_0000025030"
FT PEPTIDE 101..123
FT /note="Potential peptide"
FT /id="PRO_0000437245"
FT PEPTIDE 124..162
FT /note="Corticotropin"
FT /id="PRO_0000025031"
FT PEPTIDE 124..136
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025032"
FT PEPTIDE 142..162
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000025033"
FT PEPTIDE 165..235
FT /note="Lipotropin beta"
FT /id="PRO_0000025034"
FT PEPTIDE 165..202
FT /note="Lipotropin gamma"
FT /id="PRO_0000025035"
FT PEPTIDE 185..202
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025036"
FT PEPTIDE 205..235
FT /note="Beta-endorphin"
FT /id="PRO_0000025037"
FT PEPTIDE 205..209
FT /note="Met-enkephalin"
FT /id="PRO_0000025038"
FT REGION 88..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..200
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"
FT MOD_RES 124
FT /note="N-acetylserine; in Corticotropin"
FT /evidence="ECO:0000250|UniProtKB:P01191"
FT MOD_RES 136
FT /note="Valine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01189"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="N -> Y (in Ref. 1; CAA26937/AAA41903)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="E -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 26540 MW; A1AEC6AC9DBF1C13 CRC64;
MPRFCNSRSG ALLLALLLQT SIDVWSWCLE SSQCQDLTTE SNLLACIRAC RLDLSAETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGPR NSSSAGGSAQ RRAEEETAGG DGRPEPSPRE
GKRSYSMEHF RWGKPVGKKR RPVKVYPNVA ENESAEAFPL EFKRELEGEQ PDGLEQVLEP
DTEKADGPYR VEHFRWGNPP KDKRYGGFMT SEKSQTPLVT LFKNAIIKNV HKKGQ
