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   02-SEP-2026, entry version 196.
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 {ECO:0000303|PubMed:9413988};
DE   Contains:
DE     RecName: Full=Corticotropin;
DE     AltName: Full=Adrenocorticotropic hormone {ECO:0000303|PubMed:35926007};
DE              Short=ACTH {ECO:0000303|PubMed:9413988};
DE   Contains:
DE     RecName: Full=Melanocyte-stimulating hormone alpha {ECO:0000303|PubMed:35926007};
DE              Short=Alpha-MSH {ECO:0000303|PubMed:35926007};
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 {ECO:0000303|PubMed:9413988};
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 {ECO:0000312|MGI:MGI:97742}; 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   FUNCTION (ACTH AND ALPHA-MSH).
RX   PubMed=9413988; DOI=10.1016/s0092-8674(00)80467-5;
RA   Chen W., Kelly M.A., Opitz-Araya X., Thomas R.E., Low M.J., Cone R.D.;
RT   "Exocrine gland dysfunction in MC5-R-deficient mice: evidence for
RT   coordinated regulation of exocrine gland function by melanocortin
RT   peptides.";
RL   Cell 91:789-798(1997).
RN   [9]
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).
RN   [10]
RP   FUNCTION (ALPHA-MSH).
RX   PubMed=35926007; DOI=10.1126/science.abj2674;
RA   Xu Y., Yan J., Tao Y., Qian X., Zhang C., Yin L., Gu P., Liu Y., Pan Y.,
RA   Tang R., Jiang W., Zhou R.;
RT   "Pituitary hormone alpha-MSH promotes tumor-induced myelopoiesis and
RT   immunosuppression.";
RL   Science 377:1085-1091(2022).
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]: Functions as a ligand for the melanocortin
CC       receptors MC1R, MC2R, MC3R and MC5R (PubMed:9413988). Activation of
CC       MC1R increases melanogenesis in melanocytes found in the skin and hair.
CC       Binding to MC2R stimulates the adrenal glands to secrete cortisol.
CC       Contributes to the regulation of energy homeostasis through activation
CC       of MC3R (By similarity). Involved in the regulation exocrine gland
CC       function through MC5R activation (PubMed:9413988).
CC       {ECO:0000250|UniProtKB:P01189, ECO:0000269|PubMed:9413988}.
CC   -!- FUNCTION: [Melanocyte-stimulating hormone alpha]: Serves as a ligand
CC       for the melanocortin receptors MC1R, MC3R, MC4R and MC5R
CC       (PubMed:35926007, PubMed:9413988). Activation of MC1R promotes
CC       melanogenesis in melanocytes of the skin and hair. Contributes to the
CC       regulation of energy homeostasis through activation of MC3R. Through
CC       MC4R activation, functions as an anorexigenic peptide (By similarity).
CC       Promotes immunosuppression and involved in the regulation exocrine
CC       gland function through MC5R activation (PubMed:35926007,
CC       PubMed:9413988). {ECO:0000250|UniProtKB:P01189,
CC       ECO:0000269|PubMed:35926007, ECO:0000269|PubMed:9413988}.
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   FunCoup; P01193; 756.
DR   STRING; 10090.ENSMUSP00000151504; -.
DR   GlyConnect; P01193; 5 N-Linked glycans (1 site).
DR   GlyCosmos; P01193; 2 sites, 8 glycans.
DR   GlyGen; P01193; 3 sites, 10 N-linked glycans (3 sites).
DR   iPTMnet; P01193; -.
DR   PhosphoSitePlus; P01193; -.
DR   CPTAC; non-CPTAC-4026; -.
DR   PaxDb; 10090-ENSMUSP00000151504; -.
DR   PeptideAtlas; P01193; -.
DR   ProteomicsDB; 283426; -.
DR   Antibodypedia; 3452; 2442 antibodies from 45 providers.
DR   DNASU; 18976; -.
DR   Ensembl; ENSMUST00000020990.7; ENSMUSP00000020990.6; ENSMUSG00000020660.7.
DR   Ensembl; ENSMUST00000218089.2; ENSMUSP00000151367.2; ENSMUSG00000020660.7.
DR   Ensembl; ENSMUST00000219543.2; ENSMUSP00000151504.2; ENSMUSG00000020660.7.
DR   GeneID; 18976; -.
DR   KEGG; mmu:18976; -.
DR   UCSC; uc007mxe.2; mouse.
DR   AGR; MGI:97742; -.
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; NIRKYVM; -.
DR   OrthoDB; 8962839at2759; -.
DR   PhylomeDB; P01193; -.
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 82 CRISPR screens.
DR   PRO; PR:P01193; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P01193; protein.
DR   Bgee; ENSMUSG00000020660; Expressed in pituitary gland and 128 other cell types or tissues.
DR   ExpressionAtlas; P01193; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0005782; C:peroxisomal matrix; ISO:GO_Central.
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:0048018; F:receptor ligand activity; ISO:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central.
DR   GO; GO:0070996; F:type 1 melanocortin receptor binding; ISS:UniProtKB.
DR   GO; GO:0031781; F:type 3 melanocortin receptor binding; ISO:GO_Central.
DR   GO; GO:0031782; F:type 4 melanocortin receptor binding; ISO:GO_Central.
DR   GO; GO:0031783; F:type 5 melanocortin receptor binding; ISO:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0035821; P:modulation of process of another organism; ISO:GO_Central.
DR   GO; GO:0061744; P:motor behavior; ISO:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:GO_Central.
DR   GO; GO:0032099; P:negative regulation of appetite; ISO:GO_Central.
DR   GO; GO:1903999; P:negative regulation of eating behavior; ISO:GO_Central.
DR   GO; GO:0050777; P:negative regulation of immune response; ISO:GO_Central.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:GO_Central.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:ARUK-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:GO_Central.
DR   GO; GO:0031948; P:positive regulation of glucocorticoid biosynthetic process; ISO:GO_Central.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; ISO:GO_Central.
DR   GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; ISO:GO_Central.
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:0060259; P:regulation of feeding behavior; ISO:GO_Central.
DR   GO; GO:0005981; P:regulation of glycogen catabolic 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   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; 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        90..100
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..205
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
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