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P01192

- COLI_PIG

UniProt

P01192 - COLI_PIG

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Protein

Pro-opiomelanocortin

Gene

POMC

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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 - Biological processi

  1. neuropeptide signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endorphin, Hormone

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626By similarityAdd
BLAST
Peptidei27 – 10680NPPPRO_0000025015Add
BLAST
Peptidei77 – 8711Melanotropin gammaPRO_0000025016Add
BLAST
Propeptidei109 – 13325PRO_0000025017Add
BLAST
Peptidei136 – 17439CorticotropinPRO_0000025018Add
BLAST
Peptidei136 – 14813Melanotropin alphaPRO_0000025019Add
BLAST
Peptidei154 – 17421Corticotropin-like intermediary peptidePRO_0000025020Add
BLAST
Peptidei177 – 26791Lipotropin betaPRO_0000025021Add
BLAST
Peptidei177 – 23458Lipotropin gammaPRO_0000025022Add
BLAST
Peptidei217 – 23418Melanotropin betaPRO_0000025023Add
BLAST
Peptidei237 – 26731Beta-endorphinPRO_0000025024Add
BLAST
Peptidei237 – 2415Met-enkephalinPRO_0000025025

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phenylalanine amide
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Modified residuei136 – 1361N-acetylserineBy similarity
Modified residuei148 – 1481Valine amide

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

Expressioni

Tissue specificityi

ACTH and MSH are produced by the pituitary gland.

Family & Domainsi

Sequence similaritiesi

Belongs to the POMC family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004341.
InParanoidiP01192.
KOiK05228.

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.

P01192-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MPRLCGSRSG ALLLTLLLQA SMGVRGWCLE SSQCQDLSTE SNLLACIRAC
60 70 80 90 100
KPDLSAETPV FPGNGDAQPL TENPRKYVMG HFRWDRFGRR NGSSSGGGGG
110 120 130 140 150
GGGAGQKREE EEVAAGEGPG PRGDGVAPGP RQDKRSYSME HFRWGKPVGK
160 170 180 190 200
KRRPVKVYPN GAEDELAEAF PLEFRRELAG APPEPARDPE APAEGAAARA
210 220 230 240 250
ELEYGLVAEA EAAEKKDEGP YKMEHFRWGS PPKDKRYGGF MTSEKSQTPL
260
VTLFKNAIVK NAHKKGQ
Length:267
Mass (Da):28,895
Last modified:October 23, 1986 - v1
Checksum:iA6DB487A5032B648
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61G → S(PubMed:7958386)Curated
Sequence conflicti6 – 61G → S(PubMed:6547437)Curated
Sequence conflicti15 – 151T → A(PubMed:7958386)Curated
Sequence conflicti15 – 151T → A(PubMed:6547437)Curated
Sequence conflicti23 – 231G → E(PubMed:7958386)Curated
Sequence conflicti23 – 231G → E(PubMed:6547437)Curated
Sequence conflicti49 – 491A → S(PubMed:6547437)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431R → T.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03561 mRNA. Translation: CAA27248.1.
X00135 mRNA. Translation: CAA24968.1.
S73519 mRNA. Translation: AAB32312.1.
PIRiA93496. CTPGP.
RefSeqiNP_999023.1. NM_213858.1.
UniGeneiSsc.14556.

Genome annotation databases

GeneIDi396863.
KEGGissc:396863.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03561 mRNA. Translation: CAA27248.1 .
X00135 mRNA. Translation: CAA24968.1 .
S73519 mRNA. Translation: AAB32312.1 .
PIRi A93496. CTPGP.
RefSeqi NP_999023.1. NM_213858.1.
UniGenei Ssc.14556.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396863.
KEGGi ssc:396863.

Organism-specific databases

CTDi 5443.

Phylogenomic databases

HOVERGENi HBG004341.
InParanoidi P01192.
KOi K05228.

Family and domain databases

InterProi IPR001941. Mcortin_ACTH.
IPR013531. Mcrtin_ACTH_cent.
IPR013593. Melanocortin_N.
IPR013532. Opioid_neuropept.
[Graphical view ]
Pfami PF00976. ACTH_domain. 1 hit.
PF08384. NPP. 1 hit.
PF08035. Op_neuropeptide. 1 hit.
[Graphical view ]
PRINTSi PR00383. MELANOCORTIN.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCOLI_PIG
AccessioniPrimary (citable) accession number: P01192
Secondary accession number(s): Q95246
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: October 29, 2014
This is version 83 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3