P01193 (COLI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pro-opiomelanocortin
Short name=POMC

Alternative name(s):
Corticotropin-lipotropin

Cleaved into the following 10 chains:

1. NPP
2. Melanotropin gamma
   Alternative name(s):
   Gamma-MSH
3. Corticotropin
   Alternative name(s):
   Adrenocorticotropic hormone
   Short name=ACTH
4. Melanotropin alpha
   Alternative name(s):
   Alpha-MSH
5. Corticotropin-like intermediary peptide
   Short name=CLIP
6. Lipotropin beta
   Alternative name(s):
   Beta-LPH
7. Lipotropin gamma
   Alternative name(s):
   Gamma-LPH
8. Melanotropin beta
   Alternative name(s):
   Beta-MSH
9. Beta-endorphin
10. Met-enkephalin

Gene names

Name:	Pomc
Synonyms:	Pomc1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subcellular location	Secreted By similarity.
Tissue specificity	ACTH and MSH are produced by the pituitary gland.
Post-translational modification	Specific enzymatic cleavages at paired basic residues yield the different active peptides.
Sequence similarities	Belongs to the POMC family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Endorphin Hormone
PTM	Acetylation Amidation Cleavage on pair of basic residues Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell signaling Inferred from sequence or structural similarity. Source: UniProtKB cellular pigmentation Inferred from sequence or structural similarity. Source: UniProtKB generation of precursor metabolites and energy Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of tumor necrosis factor production Inferred from sequence or structural similarity. Source: UniProtKB neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB regulation of appetite Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from genetic interaction PubMed 16243970. Source: MGI signal transduction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB peroxisomal matrix Inferred from electronic annotation. Source: Compara secretory granule Inferred from direct assay PubMed 1329576. Source: MGI
Molecular_function	hormone activity Inferred from direct assay PubMed 15467755. Source: MGI type 1 melanocortin receptor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	By similarity
	Peptide	27 – 100	74	NPP		PRO_0000024996
	Peptide	77 – 87	11	Melanotropin gamma		PRO_0000024997
	Propeptide	103 – 121	19			PRO_0000024998
	Peptide	124 – 162	39	Corticotropin		PRO_0000024999
	Peptide	124 – 136	13	Melanotropin alpha		PRO_0000025000
	Peptide	142 – 162	21	Corticotropin-like intermediary peptide		PRO_0000025001
	Peptide	165 – 235	71	Lipotropin beta		PRO_0000025002
	Peptide	165 – 202	38	Lipotropin gamma		PRO_0000025003
	Peptide	185 – 202	18	Melanotropin beta		PRO_0000025004
	Peptide	205 – 235	31	Beta-endorphin		PRO_0000025005
	Peptide	205 – 209	5	Met-enkephalin		PRO_0000025006
Amino acid modifications
	Modified residue	87	1	Phenylalanine amide By similarity
	Modified residue	124	1	N-acetylserine By similarity
	Modified residue	136	1	Valine amide By similarity
	Modified residue	154	1	Phosphoserine By similarity
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	152	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	176	1	Q → H in CAA24770. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P01193 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: EF98C0A95D6B4991	FASTA	235	26,707
	10 20 30 40 50 60 MPRFCYSRSG ALLLALLLQT SIDVWSWCLE SSQCQDLTTE SNLLACIRAC KLDLSLETPV 70 80 90 100 110 120 FPGNGDEQPL TENPRKYVMG HFRWDRFGPR NSSSAGSAAQ RRAEEEAVWG DGSPEPSPRE 130 140 150 160 170 180 GKRSYSMEHF RWGKPVGKKR RPVKVYPNVA ENESAEAFPL EFKRELEGER PLGLEQVLES 190 200 210 220 230 DAEKDDGPYR VEHFRWSNPP KDKRYGGFMT SEKSQTPLVT LFKNAIIKNA HKKGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00132282.
PIR	CTMSP. A91312.
RefSeq	NP_032921.1. NM_008895.3.
UniGene	Mm.277996.
3D structure databases
ProteinModelPortal	P01193.
ModBase	Search...
PTM databases
GlycoSuiteDB	P01193.
PhosphoSite	P01193.
Proteomic databases
PaxDb	P01193.
PRIDE	P01193.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020990; ENSMUSP00000020990; ENSMUSG00000020660.
GeneID	18976.
KEGG	mmu:18976.
UCSC	uc007mxe.1. mouse.
Organism-specific databases
CTD	5443.
MGI	MGI:97742. Pomc.
Phylogenomic databases
eggNOG	NOG45039.
GeneTree	ENSGT00390000016811.
HOGENOM	HOG000111887.
HOVERGEN	HBG004341.
InParanoid	P01193.
KO	K05228.
OMA	CKPDLSA.
OrthoDB	EOG466VN8.
Gene expression databases
Bgee	P01193.
CleanEx	MM_POMC.
Genevestigator	P01193.
GermOnline	ENSMUSG00000020660. Mus musculus.
Family and domain databases
InterPro	IPR001941. Mcortin_ACTH. IPR013531. Mcrtin_ACTH_cent. IPR013593. Melanocortin_N. IPR013532. Opioid_neuropept. [Graphical view]
Pfam	PF00976. ACTH_domain. 1 hit. PF08384. NPP. 1 hit. PF08035. Op_neuropeptide. 1 hit. [Graphical view]
PRINTS	PR00383. MELANOCORTIN.
ProtoNet	Search...
Other
ChiTaRS	POMC. mouse.
NextBio	295340.
PMAP-CutDB	P01193.
SOURCE	Search...

Entry information

Entry name

COLI_MOUSE

Accession

Primary (citable) accession number: P01193
Secondary accession number(s): P01200, Q544U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program