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Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Potential peptide; Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanocyte-stimulating hormone beta (Beta-MSH) (Melanotropin beta); Beta-endorphin; Met-enkephalin]

 COLI_HUMAN              Reviewed;         267 AA.
P01189; P78442; Q53T23; Q9UD39; Q9UD40;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
25-OCT-2017, entry version 189.
RecName: Full=Pro-opiomelanocortin;
Short=POMC;
AltName: Full=Corticotropin-lipotropin;
Contains:
RecName: Full=NPP;
Contains:
RecName: Full=Melanotropin gamma;
AltName: Full=Gamma-MSH;
Contains:
RecName: Full=Potential peptide;
Contains:
RecName: Full=Corticotropin;
AltName: Full=Adrenocorticotropic hormone;
Short=ACTH;
Contains:
RecName: Full=Melanocyte-stimulating hormone alpha;
Short=Alpha-MSH;
AltName: Full=Melanotropin alpha;
Contains:
RecName: Full=Corticotropin-like intermediary peptide;
Short=CLIP;
Contains:
RecName: Full=Lipotropin beta;
AltName: Full=Beta-LPH;
Contains:
RecName: Full=Lipotropin gamma;
AltName: Full=Gamma-LPH;
Contains:
RecName: Full=Melanocyte-stimulating hormone beta;
Short=Beta-MSH;
AltName: Full=Melanotropin beta;
Contains:
RecName: Full=Beta-endorphin;
Contains:
RecName: Full=Met-enkephalin;
Flags: Precursor;
Name=POMC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6274691; DOI=10.1016/0014-5793(81)80952-0;
Takahashi H., Teranishi Y., Nakanishi S., Numa S.;
"Isolation and structural organization of the human corticotropin-
beta-lipotropin precursor gene.";
FEBS Lett. 135:97-102(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6299668; DOI=10.1089/dna.1.1982.1.133;
Whitfeld P.L., Seeburg P.H., Shine J.;
"The human pro-opiomelanocortin gene: organization, sequence, and
interspersion with repetitive DNA.";
DNA 1:133-143(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6314261; DOI=10.1093/nar/11.19.6847;
Takahashi H., Hakamata Y., Watanabe Y., Kikuno R., Miyata T., Numa S.;
"Complete nucleotide sequence of the human corticotropin-beta-
lipotropin precursor gene.";
Nucleic Acids Res. 11:6847-6858(1983).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-267.
PubMed=3606677;
Golovin S.Y., Karginov V.A., Bondar A.A., Beklemishev A.B.,
Chekhranova M.K., Mertvetsov N.P., Pankov Y.A.;
"Synthesis, cloning and primary structure of DNA complementary to mRNA
for human pituitary pro-opiomelanocortin.";
Bioorg. Khim. 13:562-564(1987).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-267.
PubMed=6254047; DOI=10.1073/pnas.77.8.4890;
Chang A.C.Y., Cochet M., Cohen S.N.;
"Structural organization of human genomic DNA encoding the pro-
opiomelanocortin peptide.";
Proc. Natl. Acad. Sci. U.S.A. 77:4890-4894(1980).
[9]
PROTEIN SEQUENCE OF 27-102.
PubMed=6945581; DOI=10.1073/pnas.78.7.4236;
Seidah N.G., Chretien M.;
"Complete amino acid sequence of a human pituitary glycopeptide: an
important maturation product of pro-opiomelanocortin.";
Proc. Natl. Acad. Sci. U.S.A. 78:4236-4240(1981).
[10]
PROTEIN SEQUENCE OF 27-102.
PubMed=6267033;
Seidah N.G., Rochemont J., Hamelin J., Lis M., Chretien M.;
"Primary structure of the major human pituitary pro-opiomelanocortin
NH2-terminal glycopeptide. Evidence for an aldosterone-stimulating
activity.";
J. Biol. Chem. 256:7977-7984(1981).
[11]
PROTEIN SEQUENCE OF 105-134, AND AMIDATION AT GLU-134.
PubMed=6272808; DOI=10.1016/S0006-291X(81)80190-8;
Seidah N.G., Rochemont J., Hamelin J., Benjannet S., Chretien M.;
"The missing fragment of the pro-sequence of human pro-
opiomelanocortin: sequence and evidence for C-terminal amidation.";
Biochem. Biophys. Res. Commun. 102:710-716(1981).
[12]
PROTEIN SEQUENCE OF 138-176.
PubMed=4352834; DOI=10.1042/bj1330011;
Bennett H.P.J., Lowry P.J., McMartin C.;
"Confirmation of the 1-20 amino acid sequence of human
adrenocorticotrophin.";
Biochem. J. 133:11-13(1973).
[13]
PROTEIN SEQUENCE OF 138-176.
PubMed=14463577;
Lee T.H., Lerner A.B., Buettner-Janusch V.;
"On the structure of human corticotropin (adrenocorticotropic
hormone).";
J. Biol. Chem. 236:2970-2974(1961).
[14]
PROTEIN SEQUENCE OF 27-41.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[15]
SEQUENCE REVISION (CORTICOTROPIN).
PubMed=4334191;
Riniker B., Sieber P., Rittel W., Zuber H.;
"Revised amino-acid sequences for porcine and human
adrenocorticotrophic hormone.";
Nature New Biol. 235:114-115(1972).
[16]
SYNTHESIS OF CORTICOTROPIN.
PubMed=4338630; DOI=10.1002/hlca.19720550420;
Sieber P., Rittel W., Riniker B.;
"Synthesis of the human adrenal cortex hormone (alpha-h-ACTH) with a
revised amino-acid sequence.";
Helv. Chim. Acta 55:1243-1266(1972).
[17]
SYNTHESIS OF CORTICOTROPIN.
PubMed=4347148; DOI=10.1021/ja00785a049;
Yamashiro D., Li C.H.;
"Adrenocorticotropins. 44. Total synthesis of the human hormone by the
solid-phase method.";
J. Am. Chem. Soc. 95:1310-1315(1973).
[18]
PROTEIN SEQUENCE OF 179-267.
PubMed=1264228; DOI=10.1038/260622a0;
Li C.H., Chung D.;
"Primary structure of human beta-lipotropin.";
Nature 260:622-624(1976).
[19]
PROTEIN SEQUENCE OF 217-234.
Harris J.I.;
"Structure of a melanocyte-stimulating hormone from the human
pituitary gland.";
Nature 184:167-169(1959).
[20]
PROTEIN SEQUENCE OF 237-267.
PubMed=195688;
Dragon N., Seidah N.G., Lis M., Routhier R., Chretien M.;
"Primary structure and morphine-like activity of human beta-
endorphin.";
Can. J. Biochem. 55:666-670(1977).
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 235-256.
PubMed=2424570; DOI=10.1016/0006-8993(86)90896-6;
Bovenberg R.A.L., Burbach J.P.H., Wiegant V.M., Veeneman G.H.,
van Boom J.H., Baas P.D., Jansz H.S., de Wied D.;
"Gamma-endorphin and schizophrenia: amino acid composition of gamma-
endorphin and nucleotide sequence of gamma-endorphin cDNA from
pituitary glands of schizophrenic patients.";
Brain Res. 376:29-37(1986).
[22]
PROTEOLYTIC PROCESSING.
PubMed=2839146; DOI=10.1042/bj2500781;
Fenger M., Johnsen A.H.;
"Alpha-amidated peptides derived from pro-opiomelanocortin in normal
human pituitary.";
Biochem. J. 250:781-788(1988).
[23]
NUCLEOTIDE SEQUENCE OF 75-104, AND VARIANT 97-SER--GLY-99 DEL.
TISSUE=Pituitary;
PubMed=7828531; DOI=10.1210/endo.136.1.7828531;
Morris J.C., Savva D., Lowry P.J.;
"Reduced expression of a naturally deleted form of human
proopiomelanocortin complementary deoxyribonucleic acid after
transfection into Chinese hamster ovary cells.";
Endocrinology 136:195-201(1995).
[24]
INVOLVEMENT IN POMCD.
PubMed=9620771; DOI=10.1038/509;
Krude H., Biebermann H., Luck W., Horn R., Brabant G., Grueters A.;
"Severe early-onset obesity, adrenal insufficiency and red hair
pigmentation caused by POMC mutations in humans.";
Nat. Genet. 19:155-157(1998).
[25]
INVOLVEMENT IN ABDOMINAL BODY FAT DISTRIBUTION.
PubMed=16046320; DOI=10.2337/diabetes.54.8.2492;
Baker M., Gaukrodger N., Mayosi B.M., Imrie H., Farrall M.,
Watkins H., Connell J.M.C., Avery P.J., Keavney B.;
"Association between common polymorphisms of the proopiomelanocortin
gene and body fat distribution: a family study.";
Diabetes 54:2492-2496(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[27]
VARIANTS ASN-106; GLY-214 AND 97-SER--GLY-99 DEL.
PubMed=9768693; DOI=10.1210/jcem.83.10.5298;
Hinney A., Becker I., Heibult O., Nottebom K., Schmidt A., Ziegler A.,
Mayer H., Siegfried W., Blum W.F., Remschmidt H., Hebebrand J.;
"Systematic mutation screening of the pro-opiomelanocortin gene:
identification of several genetic variants including three different
insertions, one nonsense and two missense point mutations in probands
of different weight extremes.";
J. Clin. Endocrinol. Metab. 83:3737-3741(1998).
[28]
VARIANT GLN-236.
PubMed=10193875; DOI=10.1038/sj.ijo.0800814;
Echwald S.M., Sorensen T.I., Andersen T., Tybjaerg-Hansen A.,
Clausen J.O., Pedersen O.;
"Mutational analysis of the proopiomelanocortin gene in Caucasians
with early onset obesity.";
Int. J. Obes. Relat. Metab. Disord. 23:293-298(1999).
[29]
VARIANTS THR-7; LEU-9; GLY-236 AND 97-SER--GLY-99 DEL.
PubMed=11244459; DOI=10.1038/sj.ijo.0801485;
del Giudice E.M., Cirillo G., Santoro N., D'Urso L., Carbone M.T.,
Toro R.D., Perrone L.;
"Molecular screening of the proopiomelanocortin (POMC) gene in Italian
obese children: report of three new mutations.";
Int. J. Obes. Relat. Metab. Disord. 25:61-67(2001).
[30]
VARIANT GLY-236, CHARACTERIZATION OF VARIANT GLY-236, AND POSSIBLE
INVOLVEMENT IN OBESITY.
PubMed=12165561; DOI=10.1093/hmg/11.17.1997;
Challis B.G., Pritchard L.E., Creemers J.W.M., Delplanque J.,
Keogh J.M., Luan J., Wareham N.J., Yeo G.S.H., Bhattacharyya S.,
Froguel P., White A., Farooqi I.S., O'Rahilly S.;
"A missense mutation disrupting a dibasic prohormone processing site
in pro-opiomelanocortin (POMC) increases susceptibility to early-onset
obesity through a novel molecular mechanism.";
Hum. Mol. Genet. 11:1997-2004(2002).
-!- FUNCTION: Corticotropin: Stimulates the adrenal glands to release
cortisol.
-!- FUNCTION: Melanocyte-stimulating hormone alpha: Anorexigenic
peptide. Increases the pigmentation of skin by increasing melanin
production in melanocytes.
-!- FUNCTION: Melanocyte-stimulating hormone beta: Increases the
pigmentation of skin by increasing melanin production in
melanocytes.
-!- FUNCTION: Beta-endorphin: Endogenous orexigenic opiate.
-!- FUNCTION: Met-enkephalin: Endogenous opiate.
-!- INTERACTION:
Q68D86:CCDC102B; NbExp=4; IntAct=EBI-12219503, EBI-10171570;
O75031:HSF2BP; NbExp=4; IntAct=EBI-12219503, EBI-7116203;
Q8NI38:NFKBID; NbExp=4; IntAct=EBI-12219503, EBI-10271199;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01193}.
Note=Melanocyte-stimulating hormone alpha and beta-endorphin are
stored in separate granules in hypothalamic POMC neurons,
suggesting that secretion may be under the control of different
regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
-!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary
gland.
-!- PTM: Specific enzymatic cleavages at paired basic residues yield
the different active peptides. {ECO:0000269|PubMed:2839146}.
-!- PTM: O-glycosylated; reducing sugar is probably N-
acetylgalactosamine.
-!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized
by an increase of body weight beyond the limitation of skeletal
and physical requirements, as the result of excessive accumulation
of body fat. {ECO:0000269|PubMed:12165561}. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- DISEASE: Pro-opiomelanocortinin deficiency (POMCD) [MIM:609734]:
Affected individuals present early-onset obesity, adrenal
insufficiency and red hair. {ECO:0000269|PubMed:9620771}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the POMC family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Melanocyte-stimulating hormone
entry;
URL="https://en.wikipedia.org/wiki/Melanocyte-stimulating_hormone";
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EMBL; M38297; AAA60140.1; -; mRNA.
EMBL; J00292; AAB59621.1; -; Genomic_DNA.
EMBL; J00291; AAB59621.1; JOINED; Genomic_DNA.
EMBL; V01510; CAA24754.1; -; Genomic_DNA.
EMBL; AC012457; AAY24354.1; -; Genomic_DNA.
EMBL; CH471053; EAX00729.1; -; Genomic_DNA.
EMBL; CH471053; EAX00730.1; -; Genomic_DNA.
EMBL; BC065832; AAH65832.1; -; mRNA.
EMBL; M25896; AAA35799.1; -; mRNA.
CCDS; CCDS1717.1; -.
PIR; A17229; CTHUP.
RefSeq; NP_000930.1; NM_000939.3.
RefSeq; NP_001030333.1; NM_001035256.2.
RefSeq; NP_001306133.1; NM_001319204.1.
RefSeq; NP_001306134.1; NM_001319205.1.
UniGene; Hs.1897; -.
PDB; 4XNH; X-ray; 2.10 A; F=138-145.
PDB; 4XPD; X-ray; 2.81 A; F=138-145.
PDB; 4Y49; X-ray; 3.95 A; E/K/Q=138-145.
PDBsum; 4XNH; -.
PDBsum; 4XPD; -.
PDBsum; 4Y49; -.
ProteinModelPortal; P01189; -.
SMR; P01189; -.
BioGrid; 111439; 14.
IntAct; P01189; 15.
STRING; 9606.ENSP00000264708; -.
DrugBank; DB01565; Dihydromorphine.
DrugBank; DB01497; Etorphine.
DrugBank; DB00836; Loperamide.
iPTMnet; P01189; -.
PhosphoSitePlus; P01189; -.
BioMuta; POMC; -.
DMDM; 116880; -.
EPD; P01189; -.
PaxDb; P01189; -.
PeptideAtlas; P01189; -.
PRIDE; P01189; -.
DNASU; 5443; -.
Ensembl; ENST00000264708; ENSP00000264708; ENSG00000115138.
Ensembl; ENST00000380794; ENSP00000370171; ENSG00000115138.
Ensembl; ENST00000395826; ENSP00000379170; ENSG00000115138.
Ensembl; ENST00000405623; ENSP00000384092; ENSG00000115138.
GeneID; 5443; -.
KEGG; hsa:5443; -.
UCSC; uc002rfy.1; human.
CTD; 5443; -.
DisGeNET; 5443; -.
EuPathDB; HostDB:ENSG00000115138.10; -.
GeneCards; POMC; -.
GeneReviews; POMC; -.
HGNC; HGNC:9201; POMC.
HPA; CAB002762; -.
HPA; HPA046135; -.
HPA; HPA063644; -.
MalaCards; POMC; -.
MIM; 176830; gene.
MIM; 601665; phenotype.
MIM; 609734; phenotype.
neXtProt; NX_P01189; -.
OpenTargets; ENSG00000115138; -.
Orphanet; 71526; Obesity due to pro-opiomelanocortin deficiency.
PharmGKB; PA33526; -.
eggNOG; ENOG410IKR5; Eukaryota.
eggNOG; ENOG410Z5R4; LUCA.
GeneTree; ENSGT00390000016811; -.
HOVERGEN; HBG004341; -.
InParanoid; P01189; -.
KO; K05228; -.
OMA; RACKPDL; -.
OrthoDB; EOG091G0V3J; -.
PhylomeDB; P01189; -.
TreeFam; TF333215; -.
Reactome; R-HSA-111885; Opioid Signalling.
Reactome; R-HSA-193048; Androgen biosynthesis.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
Reactome; R-HSA-202040; G-protein activation.
Reactome; R-HSA-209952; Peptide hormone biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-5579031; Defective ACTH causes Obesity and Pro-opiomelanocortinin deficiency (POMCD).
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P01189; -.
ChiTaRS; POMC; human.
GeneWiki; Proopiomelanocortin; -.
GenomeRNAi; 5443; -.
PMAP-CutDB; P01189; -.
PRO; PR:P01189; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115138; -.
CleanEx; HS_POMC; -.
ExpressionAtlas; P01189; baseline and differential.
Genevisible; P01189; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0001664; F:G-protein coupled receptor binding; IDA:BHF-UCL.
GO; GO:0005179; F:hormone activity; IMP:UniProtKB.
GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IMP:UniProtKB.
GO; GO:0070996; F:type 1 melanocortin receptor binding; IDA:BHF-UCL.
GO; GO:0031781; F:type 3 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0031782; F:type 4 melanocortin receptor binding; IPI:BHF-UCL.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IMP:UniProtKB.
GO; GO:0033059; P:cellular pigmentation; IMP:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0035821; P:modification of morphology or physiology of other organism; IMP:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
GO; GO:0016486; P:peptide hormone processing; TAS:Reactome.
GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032098; P:regulation of appetite; IMP:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:2000852; P:regulation of corticosterone secretion; IBA:GO_Central.
GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
InterPro; IPR013531; Mcrtin_ACTH_cent.
InterPro; IPR013593; Melanocortin_N.
InterPro; IPR013532; Opioid_neuropept.
InterPro; IPR001941; PMOC.
Pfam; PF00976; ACTH_domain; 3.
Pfam; PF08384; NPP; 1.
Pfam; PF08035; Op_neuropeptide; 1.
PRINTS; PR00383; MELANOCORTIN.
SMART; SM01363; ACTH_domain; 2.
SMART; SM01364; NPP; 1.
SMART; SM01365; Op_neuropeptide; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Amidation;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Endorphin; Glycoprotein;
Hormone; Obesity; Phosphoprotein; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:6267033,
ECO:0000269|PubMed:6945581}.
PEPTIDE 27 102 NPP.
/FTId=PRO_0000024966.
PEPTIDE 77 87 Melanotropin gamma.
{ECO:0000269|PubMed:2839146}.
/FTId=PRO_0000024967.
PEPTIDE 105 134 Potential peptide.
/FTId=PRO_0000024968.
PEPTIDE 138 176 Corticotropin.
/FTId=PRO_0000024969.
PEPTIDE 138 150 Melanocyte-stimulating hormone alpha.
/FTId=PRO_0000024970.
PEPTIDE 156 176 Corticotropin-like intermediary peptide.
/FTId=PRO_0000024971.
PEPTIDE 179 267 Lipotropin beta.
/FTId=PRO_0000024972.
PEPTIDE 179 234 Lipotropin gamma.
/FTId=PRO_0000024973.
PEPTIDE 217 234 Melanocyte-stimulating hormone beta.
/FTId=PRO_0000024974.
PEPTIDE 237 267 Beta-endorphin.
/FTId=PRO_0000024975.
PEPTIDE 237 241 Met-enkephalin.
/FTId=PRO_0000024976.
MOD_RES 87 87 Phenylalanine amide. {ECO:0000250}.
MOD_RES 134 134 Glutamic acid 1-amide.
{ECO:0000269|PubMed:6272808}.
MOD_RES 138 138 N-acetylserine; in Corticotropin.
{ECO:0000250|UniProtKB:P01191}.
MOD_RES 150 150 Valine amide. {ECO:0000250}.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:16807684}.
CARBOHYD 71 71 O-linked (HexNAc...) threonine.
{ECO:0000269|PubMed:6267033}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
DISULFID 28 50 {ECO:0000250}.
VARIANT 7 7 S -> T. {ECO:0000269|PubMed:11244459}.
/FTId=VAR_010699.
VARIANT 9 9 S -> L (in dbSNP:rs139750421).
{ECO:0000269|PubMed:11244459}.
/FTId=VAR_010700.
VARIANT 62 62 P -> L (in dbSNP:rs28932471).
/FTId=VAR_029762.
VARIANT 97 99 Missing. {ECO:0000269|PubMed:11244459,
ECO:0000269|PubMed:7828531,
ECO:0000269|PubMed:9768693}.
/FTId=VAR_010714.
VARIANT 106 106 D -> N (in dbSNP:rs750136455).
{ECO:0000269|PubMed:9768693}.
/FTId=VAR_010715.
VARIANT 132 132 P -> A (in dbSNP:rs8192606).
/FTId=VAR_029314.
VARIANT 214 214 E -> G (in dbSNP:rs80326661).
{ECO:0000269|PubMed:9768693}.
/FTId=VAR_010716.
VARIANT 236 236 R -> G (may confer susceptibility to
obesity; reduces the ability to activate
melanocortin receptor 4;
dbSNP:rs28932472).
{ECO:0000269|PubMed:11244459,
ECO:0000269|PubMed:12165561}.
/FTId=VAR_010701.
VARIANT 236 236 R -> Q. {ECO:0000269|PubMed:10193875}.
/FTId=VAR_012201.
CONFLICT 48 48 R -> G (in Ref. 8). {ECO:0000305}.
CONFLICT 115 115 P -> T (in Ref. 2). {ECO:0000305}.
SEQUENCE 267 AA; 29424 MW; B927323474A67536 CRC64;
MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC KPDLSAETPM
FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSSGSSGA GQKREDVSAG EDCGPLPEGG
PEPRSDGAKP GPREGKRSYS MEHFRWGKPV GKKRRPVKVY PNGAEDESAE AFPLEFKREL
TGQRLREGDG PDGPADDGAG AQADLEHSLL VAAEKKDEGP YRMEHFRWGS PPKDKRYGGF
MTSEKSQTPL VTLFKNAIIK NAYKKGE


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