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P01192 (COLI_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentSecreted
   DomainSignal
   Molecular functionEndorphin
Hormone
   PTMAcetylation
Amidation
Cleavage on pair of basic residues
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processneuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 By similarity
Peptide27 – 10680NPP
PRO_0000025015
Peptide77 – 8711Melanotropin gamma
PRO_0000025016
Propeptide109 – 13325
PRO_0000025017
Peptide136 – 17439Corticotropin Ref.5 Ref.8
PRO_0000025018
Peptide136 – 14813Melanotropin alpha Ref.9
PRO_0000025019
Peptide154 – 17421Corticotropin-like intermediary peptide
PRO_0000025020
Peptide177 – 26791Lipotropin beta Ref.10
PRO_0000025021
Peptide177 – 23458Lipotropin gamma
PRO_0000025022
Peptide217 – 23418Melanotropin beta Ref.13 Ref.14
PRO_0000025023
Peptide237 – 26731Beta-endorphin Ref.16
PRO_0000025024
Peptide237 – 2415Met-enkephalin Ref.15
PRO_0000025025

Amino acid modifications

Modified residue871Phenylalanine amide
Modified residue1361N-acetylserine By similarity
Modified residue1481Valine amide
Glycosylation911N-linked (GlcNAc...) Potential

Natural variations

Natural variant1431R → T.

Experimental info

Sequence conflict61G → S Ref.3
Sequence conflict61G → S Ref.4
Sequence conflict151T → A Ref.3
Sequence conflict151T → A Ref.4
Sequence conflict231G → E Ref.3
Sequence conflict231G → E Ref.4
Sequence conflict491A → S Ref.4

Sequences

Sequence LengthMass (Da)Tools
P01192 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: A6DB487A5032B648

FASTA26728,895
        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 

« Hide

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.
PIRCTPGP. A93496.
RefSeqNP_999023.1. NM_213858.1.
UniGeneSsc.14556.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396863.
KEGGssc:396863.

Organism-specific databases

CTD5443.

Phylogenomic databases

HOVERGENHBG004341.
KOK05228.

Family and domain databases

InterProIPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view]
PfamPF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view]
PRINTSPR00383. MELANOCORTIN.
ProtoNetSearch...

Entry information

Entry nameCOLI_PIG
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families