COLI_MOUSE
ID COLI_MOUSE Reviewed; 235 AA.
AC P01193; P01200; Q544U4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 177.
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; Synonyms=Pomc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6303853; DOI=10.1016/0014-5793(83)80250-6;
RA Notake M., Tobimatsu T., Watanabe Y., Takahashi H., Mishina M., Numa S.;
RT "Isolation and characterization of the mouse corticotropin-beta-lipotropin
RT precursor gene and a related pseudogene.";
RL FEBS Lett. 156:67-71(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6308009; DOI=10.1016/s0021-9258(17)44688-6;
RA Uhler M., Herbert E., D'Eustachio P., Ruddle F.D.;
RT "The mouse genome contains two nonallelic pro-opiomelanocortin genes.";
RL J. Biol. Chem. 258:9444-9453(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-36.
RX PubMed=2536749; DOI=10.1016/s0021-9258(18)94100-1;
RA Thorne B.A., Caton L.W., Thomas G.;
RT "Expression of mouse proopiomelanocortin in an insulinoma cell line.
RT Requirements for beta-endorphin processing.";
RL J. Biol. Chem. 264:3545-3552(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-162.
RC STRAIN=C3H/HeJ; TISSUE=Lymphocyte;
RX PubMed=1689057; DOI=10.1073/pnas.87.3.1057;
RA Smith E.M., Galin F.S., Leboeuf R.D., Coppenhaver D.H., Harbour D.V.,
RA Blalock E.J.;
RT "Nucleotide and amino acid sequence of lymphocyte-derived corticotropin:
RT endotoxin induction of a truncated peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1057-1060(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-234.
RX PubMed=221916; DOI=10.1073/pnas.76.5.2153;
RA Roberts J.L., Seeburg P.H., Shine J., Herbert E., Baxter J.D.,
RA Goodman H.M.;
RT "Corticotropin and beta-endorphin: construction and analysis of recombinant
RT DNA complementary to mRNA for the common precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:2153-2157(1979).
RN [8]
RP SUBCELLULAR LOCATION, AND INDUCTION BY CANNABINOID.
RX PubMed=25707796; DOI=10.1038/nature14260;
RA Koch M., Varela L., Kim J.G., Kim J.D., Hernandez-Nuno F., Simonds S.E.,
RA Castorena C.M., Vianna C.R., Elmquist J.K., Morozov Y.M., Rakic P.,
RA Bechmann I., Cowley M.A., Szigeti-Buck K., Dietrich M.O., Gao X.B.,
RA Diano S., Horvath T.L.;
RT "Hypothalamic POMC neurons promote cannabinoid-induced feeding.";
RL Nature 519:45-50(2015).
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:0000269|PubMed:25707796}.
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:0000269|PubMed:25707796}.
CC -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland.
CC -!- INDUCTION: [Beta-endorphin]: In hypothalamic paraventricular nucleus
CC (PVN), up-regulated by cannabinoids, including the CNR1/CB1R agonist
CC arachidonyl-29-chloroethylamide (ACEA) (at protein level).
CC {ECO:0000269|PubMed:25707796}.
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; J00612; AAB59729.1; -; Genomic_DNA.
DR EMBL; J00611; AAB59729.1; JOINED; Genomic_DNA.
DR EMBL; V01528; CAA24769.1; -; Genomic_DNA.
DR EMBL; V01529; CAA24770.1; -; Genomic_DNA.
DR EMBL; AK017492; BAB30771.1; -; mRNA.
DR EMBL; AK017581; BAB30818.1; -; mRNA.
DR EMBL; AK030714; BAC27095.1; -; mRNA.
DR EMBL; AK077426; BAC36795.1; -; mRNA.
DR EMBL; AK133592; BAE21739.1; -; mRNA.
DR EMBL; AK133646; BAE21764.1; -; mRNA.
DR EMBL; AK133740; BAE21815.1; -; mRNA.
DR EMBL; AK133776; BAE21833.1; -; mRNA.
DR EMBL; AK133800; BAE21850.1; -; mRNA.
DR EMBL; BC061215; AAH61215.1; -; mRNA.
DR EMBL; M30489; AAA37169.1; -; mRNA.
DR EMBL; V00831; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25785.1; -.
DR PIR; A91312; CTMSP.
DR RefSeq; NP_001265510.1; NM_001278581.1.
DR RefSeq; NP_001265511.1; NM_001278582.1.
DR RefSeq; NP_001265512.1; NM_001278583.1.
DR RefSeq; NP_001265513.1; NM_001278584.1.
DR RefSeq; NP_032921.1; NM_008895.4.
DR AlphaFoldDB; P01193; -.
DR BMRB; P01193; -.
DR SMR; P01193; -.
DR BioGRID; 202295; 1.
DR ELM; P01193; -.
DR STRING; 10090.ENSMUSP00000020990; -.
DR GlyConnect; 112; 5 N-Linked glycans (1 site).
DR GlyGen; P01193; 3 sites, 8 N-linked glycans (2 sites).
DR PhosphoSitePlus; P01193; -.
DR CPTAC; non-CPTAC-4026; -.
DR PaxDb; P01193; -.
DR PeptideAtlas; P01193; -.
DR PRIDE; P01193; -.
DR ProteomicsDB; 283426; -.
DR Antibodypedia; 3452; 2389 antibodies from 43 providers.
DR DNASU; 18976; -.
DR Ensembl; ENSMUST00000020990; ENSMUSP00000020990; ENSMUSG00000020660.
DR Ensembl; ENSMUST00000218089; ENSMUSP00000151367; ENSMUSG00000020660.
DR Ensembl; ENSMUST00000219543; ENSMUSP00000151504; ENSMUSG00000020660.
DR GeneID; 18976; -.
DR KEGG; mmu:18976; -.
DR UCSC; uc007mxe.2; mouse.
DR CTD; 5443; -.
DR MGI; MGI:97742; Pomc.
DR VEuPathDB; HostDB:ENSMUSG00000020660; -.
DR eggNOG; ENOG502RZNY; Eukaryota.
DR GeneTree; ENSGT00390000016811; -.
DR HOGENOM; CLU_094632_0_0_1; -.
DR InParanoid; P01193; -.
DR OMA; KMHHFRW; -.
DR OrthoDB; 1168862at2759; -.
DR PhylomeDB; P01193; -.
DR TreeFam; TF333215; -.
DR Reactome; R-MMU-111885; Opioid Signalling.
DR Reactome; R-MMU-193048; Androgen biosynthesis.
DR Reactome; R-MMU-194002; Glucocorticoid biosynthesis.
DR Reactome; R-MMU-202040; G-protein activation.
DR Reactome; R-MMU-209952; Peptide hormone biosynthesis.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 18976; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Pomc; mouse.
DR PRO; PR:P01193; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P01193; protein.
DR Bgee; ENSMUSG00000020660; Expressed in pituitary gland and 125 other tissues.
DR ExpressionAtlas; P01193; baseline and differential.
DR Genevisible; P01193; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0070996; F:type 1 melanocortin receptor binding; ISS:UniProtKB.
DR GO; GO:0031781; F:type 3 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0031782; F:type 4 melanocortin receptor binding; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:ARUK-UCL.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:0033059; P:cellular pigmentation; ISS:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0035821; P:modulation of process of another organism; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:ARUK-UCL.
DR GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; ISO:MGI.
DR GO; GO:0140668; P:positive regulation of oxytocin production; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032098; P:regulation of appetite; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR GO; GO:2000852; P:regulation of corticosterone secretion; IMP:MGI.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IMP:MGI.
DR GO; GO:1990680; P:response to melanocyte-stimulating hormone; IDA:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
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; Endorphin;
KW Glycoprotein; Hormone; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT PEPTIDE 27..100
FT /note="NPP"
FT /id="PRO_0000024996"
FT PEPTIDE 77..87
FT /note="Melanotropin gamma"
FT /id="PRO_0000024997"
FT PROPEP 103..121
FT /id="PRO_0000024998"
FT PEPTIDE 124..162
FT /note="Corticotropin"
FT /id="PRO_0000024999"
FT PEPTIDE 124..136
FT /note="Melanocyte-stimulating hormone alpha"
FT /id="PRO_0000025000"
FT PEPTIDE 142..162
FT /note="Corticotropin-like intermediary peptide"
FT /id="PRO_0000025001"
FT PEPTIDE 165..235
FT /note="Lipotropin beta"
FT /id="PRO_0000025002"
FT PEPTIDE 165..202
FT /note="Lipotropin gamma"
FT /id="PRO_0000025003"
FT PEPTIDE 185..202
FT /note="Melanocyte-stimulating hormone beta"
FT /id="PRO_0000025004"
FT PEPTIDE 205..235
FT /note="Beta-endorphin"
FT /id="PRO_0000025005"
FT PEPTIDE 205..209
FT /note="Met-enkephalin"
FT /id="PRO_0000025006"
FT REGION 88..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..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 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 176
FT /note="Q -> H (in Ref. 2; CAA24770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 26707 MW; EF98C0A95D6B4991 CRC64;
MPRFCYSRSG ALLLALLLQT SIDVWSWCLE SSQCQDLTTE SNLLACIRAC KLDLSLETPV
FPGNGDEQPL TENPRKYVMG HFRWDRFGPR NSSSAGSAAQ RRAEEEAVWG DGSPEPSPRE
GKRSYSMEHF RWGKPVGKKR RPVKVYPNVA ENESAEAFPL EFKRELEGER PLGLEQVLES
DAEKDDGPYR VEHFRWSNPP KDKRYGGFMT SEKSQTPLVT LFKNAIIKNA HKKGQ
