P01192 (COLI_PIG) 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 106	80	NPP		PRO_0000025015
	Peptide	77 – 87	11	Melanotropin gamma		PRO_0000025016
	Propeptide	109 – 133	25			PRO_0000025017
	Peptide	136 – 174	39	Corticotropin Ref.5 Ref.8		PRO_0000025018
	Peptide	136 – 148	13	Melanotropin alpha Ref.9		PRO_0000025019
	Peptide	154 – 174	21	Corticotropin-like intermediary peptide		PRO_0000025020
	Peptide	177 – 267	91	Lipotropin beta Ref.10		PRO_0000025021
	Peptide	177 – 234	58	Lipotropin gamma		PRO_0000025022
	Peptide	217 – 234	18	Melanotropin beta Ref.13 Ref.14		PRO_0000025023
	Peptide	237 – 267	31	Beta-endorphin Ref.16		PRO_0000025024
	Peptide	237 – 241	5	Met-enkephalin Ref.15		PRO_0000025025
Amino acid modifications
	Modified residue	87	1	Phenylalanine amide
	Modified residue	136	1	N-acetylserine By similarity
	Modified residue	148	1	Valine amide
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	143	1	R → T.
Experimental info
	Sequence conflict	6	1	G → S Ref.3
	Sequence conflict	6	1	G → S Ref.4
	Sequence conflict	15	1	T → A Ref.3
	Sequence conflict	15	1	T → A Ref.4
	Sequence conflict	23	1	G → E Ref.3
	Sequence conflict	23	1	G → E Ref.4
	Sequence conflict	49	1	A → S Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P01192 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: A6DB487A5032B648	FASTA	267	28,895
	10 20 30 40 50 60 MPRLCGSRSG ALLLTLLLQA SMGVRGWCLE SSQCQDLSTE SNLLACIRAC KPDLSAETPV 70 80 90 100 110 120 FPGNGDAQPL TENPRKYVMG HFRWDRFGRR NGSSSGGGGG GGGAGQKREE EEVAAGEGPG 130 140 150 160 170 180 PRGDGVAPGP RQDKRSYSME HFRWGKPVGK KRRPVKVYPN GAEDELAEAF PLEFRRELAG 190 200 210 220 230 240 APPEPARDPE APAEGAAARA ELEYGLVAEA EAAEKKDEGP YKMEHFRWGS PPKDKRYGGF 250 260 MTSEKSQTPL VTLFKNAIVK NAHKKGQ

References

[1]	"Sequence of the cDNA encoding porcine pro-opiomelanocortin." Gossard F.J., Chang A.C.Y., Cohen S.N. Biochim. Biophys. Acta 866:68-74(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete structure of the porcine pro-opiomelanocortin mRNA derived from the nucleotide sequence of cloned cDNA." Boileau G., Barbeau C., Jeannotte L., Chretien M., Drouin J. Nucleic Acids Res. 11:8063-8071(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Presence of the same transcript of pro-opiomelanocortin (POMC) genes in the porcine anterior and intermediate pituitary lobes." Gen K., Hirai T., Kato T., Kato Y. Mol. Cell. Endocrinol. 103:101-108(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"5' sequence of porcine and rat pro-opiomelanocortin mRNA. One porcine and two rat forms." Oates E., Herbert E. J. Biol. Chem. 259:7421-7425(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Studies with corticotropin. III. Determination of the structure of beta-corticotropin and its active degradation products." Shepherd R.G., Willson S.D., Howard K.S., Bell P.H., Davies D.S., Davis S.B., Eigner E.A., Shakespeare N.E. J. Am. Chem. Soc. 78:5067-5076(1956) Cited for: PROTEIN SEQUENCE OF 136-174.
[6]	"Revised amino-acid sequences for porcine and human adrenocorticotrophic hormone." Riniker B., Sieber P., Rittel W., Zuber H. Nature New Biol. 235:114-115(1972) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 160 AND 165.
[7]	"Re-examination of the sequence of the C-terminal tryptic fragment from porcine adrenocorticotropic hormone." Graf L. Acta Biochim. Biophys. Acad. Sci. Hung. 7:293-297(1972) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION (CORTICOTROPIN).
[8]	"Isolation and full structural characterisation of six adrenocorticotropin-like peptides from porcine pituitary gland. Identification of three novel fragments of adrenocorticotropin and of two forms of a novel adrenocorticotropin-like peptide." Voigt K., Stegmaier W., McGregor G.P., Roesch H., Seliger H. Eur. J. Biochem. 194:225-236(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 136-174.
[9]	"Amino-acid sequence of the alpha-melanocyte-stimulating hormone." Harris J.I., Lerner A.B. Nature 179:1346-1347(1957) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 136-148.
[10]	"Amino acid sequence of porcine beta-lipotropic hormone." Graf L., Barat E., Cseh G., Sajgo M. Biochim. Biophys. Acta 229:276-278(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 177-267.
[11]	"Complete amino acid sequence of porcine beta-lipotropic hormone (beta-LPH)." Gilardeau C., Chretien M. (In) Meienhofer J. (eds.); Chemistry and biology of peptides, pp.609-611, Ann Arbor Sci. Pub., Ann Arbor (1972) Cited for: SEQUENCE REVISION (LIPOTROPIN).
[12]	"Complete amino acid sequence in the molecule of porcine beta-lipotropin." Pankov Y.A., Yudaev N.A. Biokhimiia 37:991-1004(1972) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 211.
[13]	"Amino-acid sequence of a melanophore-stimulating peptide." Harris J.I., Roos P. Nature 178:90-90(1956) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 217-234.
[14]	"The structure of the beta-melanocyte-stimulating hormone." Geschwind I.I., Li C.H., Barnafi L. J. Am. Chem. Soc. 79:620-625(1957) Cited for: PROTEIN SEQUENCE OF 217-234.
[15]	"Identification of two related pentapeptides from the brain with potent opiate agonist activity." Hughes J., Smith T.W., Kosterlitz H.W., Fothergill L.A., Morgan B.A., Morris H.R. Nature 258:577-579(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 237-241.
[16]	"Isolation of a COOH-terminal beta-lipotropin fragment (residues 61-91) with morphine-like analgesic activity from porcine pituitary glands." Graf L., Barat E., Patthy A. Acta Biochim. Biophys. Acad. Sci. Hung. 11:121-122(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 237-267.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X03561 mRNA. Translation: CAA27248.1. X00135 mRNA. Translation: CAA24968.1. S73519 mRNA. Translation: AAB32312.1.
PIR	CTPGP. A93496.
RefSeq	NP_999023.1. NM_213858.1.
UniGene	Ssc.14556.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396863.
KEGG	ssc:396863.
Organism-specific databases
CTD	5443.
Phylogenomic databases
HOVERGEN	HBG004341.
KO	K05228.
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...

Entry information

Entry name

COLI_PIG

Accession

Primary (citable) accession number: P01192
Secondary accession number(s): Q95246

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 23, 1986
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program