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Protein

Pro-opiomelanocortin

Gene

Pomc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

ACTH stimulates the adrenal glands to release cortisol.
MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes.
Beta-endorphin and Met-enkephalin are endogenous opiates.

GO - Molecular functioni

GO - Biological processi

  • cell-cell signaling Source: UniProtKB
  • cellular pigmentation Source: UniProtKB
  • generation of precursor metabolites and energy Source: UniProtKB
  • glucose homeostasis Source: MGI
  • negative regulation of tumor necrosis factor production Source: UniProtKB
  • neuropeptide signaling pathway Source: UniProtKB-KW
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of appetite Source: UniProtKB
  • regulation of blood pressure Source: MGI
  • regulation of corticosterone secretion Source: MGI
  • regulation of glycogen metabolic process Source: MGI
  • signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endorphin, Hormone

Enzyme and pathway databases

ReactomeiREACT_281686. Endogenous sterols.
REACT_297155. Opioid Signalling.
REACT_297756. Glucocorticoid biosynthesis.
REACT_303206. G-protein activation.
REACT_305222. Androgen biosynthesis.
REACT_313192. G alpha (s) signalling events.
REACT_319210. Peptide ligand-binding receptors.
REACT_331048. G alpha (i) signalling events.
REACT_350396. Peptide hormone biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-opiomelanocortin
Short name:
POMC
Alternative name(s):
Corticotropin-lipotropin
Cleaved into the following 10 chains:
Alternative name(s):
Gamma-MSH
Alternative name(s):
Adrenocorticotropic hormone
Short name:
ACTH
Alternative name(s):
Alpha-MSH
Alternative name(s):
Beta-LPH
Alternative name(s):
Gamma-LPH
Alternative name(s):
Beta-MSH
Gene namesi
Name:Pomc
Synonyms:Pomc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:97742. Pomc.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular space Source: UniProtKB
  • peroxisomal matrix Source: MGI
  • secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626By similarityAdd
BLAST
Peptidei27 – 10074NPPPRO_0000024996Add
BLAST
Peptidei77 – 8711Melanotropin gammaPRO_0000024997Add
BLAST
Propeptidei103 – 12119PRO_0000024998Add
BLAST
Peptidei124 – 16239CorticotropinPRO_0000024999Add
BLAST
Peptidei124 – 13613Melanotropin alphaPRO_0000025000Add
BLAST
Peptidei142 – 16221Corticotropin-like intermediary peptidePRO_0000025001Add
BLAST
Peptidei165 – 23571Lipotropin betaPRO_0000025002Add
BLAST
Peptidei165 – 20238Lipotropin gammaPRO_0000025003Add
BLAST
Peptidei185 – 20218Melanotropin betaPRO_0000025004Add
BLAST
Peptidei205 – 23531Beta-endorphinPRO_0000025005Add
BLAST
Peptidei205 – 2095Met-enkephalinPRO_0000025006

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phenylalanine amideBy similarity
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Modified residuei124 – 1241N-acetylserineBy similarity
Modified residuei136 – 1361Valine amideBy similarity
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Modified residuei154 – 1541PhosphoserineBy similarity

Post-translational modificationi

Specific enzymatic cleavages at paired basic residues yield the different active peptides.

Keywords - PTMi

Acetylation, Amidation, Cleavage on pair of basic residues, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01193.
PRIDEiP01193.

PTM databases

PhosphoSiteiP01193.
UniCarbKBiP01193.

Miscellaneous databases

PMAP-CutDBP01193.

Expressioni

Tissue specificityi

ACTH and MSH are produced by the pituitary gland.

Gene expression databases

BgeeiP01193.
CleanExiMM_POMC.
GenevisibleiP01193. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020990.

Structurei

3D structure databases

ProteinModelPortaliP01193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the POMC family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45039.
GeneTreeiENSGT00390000016811.
HOGENOMiHOG000111887.
HOVERGENiHBG004341.
InParanoidiP01193.
KOiK05228.
OMAiRACKPDL.
OrthoDBiEOG74TX0W.
PhylomeDBiP01193.
TreeFamiTF333215.

Family and domain databases

InterProiIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamiPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSiPR00383. MELANOCORTIN.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRFCYSRSG ALLLALLLQT SIDVWSWCLE SSQCQDLTTE SNLLACIRAC
60 70 80 90 100
KLDLSLETPV FPGNGDEQPL TENPRKYVMG HFRWDRFGPR NSSSAGSAAQ
110 120 130 140 150
RRAEEEAVWG DGSPEPSPRE GKRSYSMEHF RWGKPVGKKR RPVKVYPNVA
160 170 180 190 200
ENESAEAFPL EFKRELEGER PLGLEQVLES DAEKDDGPYR VEHFRWSNPP
210 220 230
KDKRYGGFMT SEKSQTPLVT LFKNAIIKNA HKKGQ
Length:235
Mass (Da):26,707
Last modified:July 21, 1986 - v1
Checksum:iEF98C0A95D6B4991
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761Q → H in CAA24770 (PubMed:6308009).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00612, J00611 Genomic DNA. Translation: AAB59729.1.
V01528 Genomic DNA. Translation: CAA24769.1.
V01529 Genomic DNA. Translation: CAA24770.1.
AK017492 mRNA. Translation: BAB30771.1.
AK017581 mRNA. Translation: BAB30818.1.
AK030714 mRNA. Translation: BAC27095.1.
AK077426 mRNA. Translation: BAC36795.1.
AK133592 mRNA. Translation: BAE21739.1.
AK133646 mRNA. Translation: BAE21764.1.
AK133740 mRNA. Translation: BAE21815.1.
AK133776 mRNA. Translation: BAE21833.1.
AK133800 mRNA. Translation: BAE21850.1.
BC061215 mRNA. Translation: AAH61215.1.
M30489 mRNA. Translation: AAA37169.1.
V00831 mRNA. No translation available.
CCDSiCCDS25785.1.
PIRiA91312. CTMSP.
RefSeqiNP_001265510.1. NM_001278581.1.
NP_001265511.1. NM_001278582.1.
NP_001265512.1. NM_001278583.1.
NP_001265513.1. NM_001278584.1.
NP_032921.1. NM_008895.4.
UniGeneiMm.277996.

Genome annotation databases

EnsembliENSMUST00000020990; ENSMUSP00000020990; ENSMUSG00000020660.
GeneIDi18976.
KEGGimmu:18976.
UCSCiuc007mxe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00612, J00611 Genomic DNA. Translation: AAB59729.1.
V01528 Genomic DNA. Translation: CAA24769.1.
V01529 Genomic DNA. Translation: CAA24770.1.
AK017492 mRNA. Translation: BAB30771.1.
AK017581 mRNA. Translation: BAB30818.1.
AK030714 mRNA. Translation: BAC27095.1.
AK077426 mRNA. Translation: BAC36795.1.
AK133592 mRNA. Translation: BAE21739.1.
AK133646 mRNA. Translation: BAE21764.1.
AK133740 mRNA. Translation: BAE21815.1.
AK133776 mRNA. Translation: BAE21833.1.
AK133800 mRNA. Translation: BAE21850.1.
BC061215 mRNA. Translation: AAH61215.1.
M30489 mRNA. Translation: AAA37169.1.
V00831 mRNA. No translation available.
CCDSiCCDS25785.1.
PIRiA91312. CTMSP.
RefSeqiNP_001265510.1. NM_001278581.1.
NP_001265511.1. NM_001278582.1.
NP_001265512.1. NM_001278583.1.
NP_001265513.1. NM_001278584.1.
NP_032921.1. NM_008895.4.
UniGeneiMm.277996.

3D structure databases

ProteinModelPortaliP01193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020990.

PTM databases

PhosphoSiteiP01193.
UniCarbKBiP01193.

Proteomic databases

PaxDbiP01193.
PRIDEiP01193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020990; ENSMUSP00000020990; ENSMUSG00000020660.
GeneIDi18976.
KEGGimmu:18976.
UCSCiuc007mxe.1. mouse.

Organism-specific databases

CTDi5443.
MGIiMGI:97742. Pomc.

Phylogenomic databases

eggNOGiNOG45039.
GeneTreeiENSGT00390000016811.
HOGENOMiHOG000111887.
HOVERGENiHBG004341.
InParanoidiP01193.
KOiK05228.
OMAiRACKPDL.
OrthoDBiEOG74TX0W.
PhylomeDBiP01193.
TreeFamiTF333215.

Enzyme and pathway databases

ReactomeiREACT_281686. Endogenous sterols.
REACT_297155. Opioid Signalling.
REACT_297756. Glucocorticoid biosynthesis.
REACT_303206. G-protein activation.
REACT_305222. Androgen biosynthesis.
REACT_313192. G alpha (s) signalling events.
REACT_319210. Peptide ligand-binding receptors.
REACT_331048. G alpha (i) signalling events.
REACT_350396. Peptide hormone biosynthesis.

Miscellaneous databases

ChiTaRSiPomc. mouse.
NextBioi295340.
PMAP-CutDBP01193.
PROiP01193.
SOURCEiSearch...

Gene expression databases

BgeeiP01193.
CleanExiMM_POMC.
GenevisibleiP01193. MM.

Family and domain databases

InterProiIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamiPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSiPR00383. MELANOCORTIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the mouse corticotropin-beta-lipotropin precursor gene and a related pseudogene."
    Notake M., Tobimatsu T., Watanabe Y., Takahashi H., Mishina M., Numa S.
    FEBS Lett. 156:67-71(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The mouse genome contains two nonallelic pro-opiomelanocortin genes."
    Uhler M., Herbert E., D'Eustachio P., Ruddle F.D.
    J. Biol. Chem. 258:9444-9453(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pituitary.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  5. "Expression of mouse proopiomelanocortin in an insulinoma cell line. Requirements for beta-endorphin processing."
    Thorne B.A., Caton L.W., Thomas G.
    J. Biol. Chem. 264:3545-3552(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-36.
  6. "Nucleotide and amino acid sequence of lymphocyte-derived corticotropin: endotoxin induction of a truncated peptide."
    Smith E.M., Galin F.S., Leboeuf R.D., Coppenhaver D.H., Harbour D.V., Blalock E.J.
    Proc. Natl. Acad. Sci. U.S.A. 87:1057-1060(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-162.
    Strain: C3H.
    Tissue: Lymphocyte.
  7. "Corticotropin and beta-endorphin: construction and analysis of recombinant DNA complementary to mRNA for the common precursor."
    Roberts J.L., Seeburg P.H., Shine J., Herbert E., Baxter J.D., Goodman H.M.
    Proc. Natl. Acad. Sci. U.S.A. 76:2153-2157(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 187-234.

Entry informationi

Entry nameiCOLI_MOUSE
AccessioniPrimary (citable) accession number: P01193
Secondary accession number(s): P01200, Q544U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.