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P01192

- COLI_PIG

UniProt

P01192 - COLI_PIG

Protein

Pro-opiomelanocortin

Gene

POMC

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (23 Oct 1986)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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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    MPRLCGSRSG ALLLTLLLQA SMGVRGWCLE SSQCQDLSTE SNLLACIRAC    50
    KPDLSAETPV FPGNGDAQPL TENPRKYVMG HFRWDRFGRR NGSSSGGGGG 100
    GGGAGQKREE EEVAAGEGPG PRGDGVAPGP RQDKRSYSME HFRWGKPVGK 150
    KRRPVKVYPN GAEDELAEAF PLEFRRELAG APPEPARDPE APAEGAAARA 200
    ELEYGLVAEA EAAEKKDEGP YKMEHFRWGS PPKDKRYGGF MTSEKSQTPL 250
    VTLFKNAIVK NAHKKGQ 267
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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 1, 2014
    This is version 82 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