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P01211

- PENK_BOVIN

UniProt

P01211 - PENK_BOVIN

Protein

Proenkephalin-A

Gene

PENK

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Met- and Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. PENK(111-130) and PENK(233-254) increase glutamate release in the striatum. PENK(111-130) decreases GABA concentration in the striatum.
    Enkelytin possesses antibacterial activity against Gram-positive bacteria such as Micrococcus luteus and Bacillus megaterium.

    GO - Biological processi

    1. aggressive behavior Source: Ensembl
    2. behavioral fear response Source: Ensembl
    3. defense response to bacterium Source: UniProtKB-KW
    4. locomotory behavior Source: Ensembl
    5. neuropeptide signaling pathway Source: UniProtKB-KW
    6. sensory perception of pain Source: Ensembl
    7. startle response Source: Ensembl

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Endorphin, Neuropeptide, Opioid peptide

    Enzyme and pathway databases

    ReactomeiREACT_210568. G alpha (i) signalling events.
    REACT_219025. Peptide ligand-binding receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proenkephalin-A
    Cleaved into the following 9 chains:
    Gene namesi
    Name:PENK
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 14

    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 – 2424Sequence AnalysisAdd
    BLAST
    Peptidei25 – 9470SynenkephalinPRO_0000008206Add
    BLAST
    Peptidei97 – 1015Met-enkephalinPRO_0000008207
    Peptidei104 – 1085Met-enkephalinPRO_0000008208
    Peptidei111 – 13020PENK(111-130)By similarityPRO_0000377682Add
    BLAST
    Peptidei133 – 1375Met-enkephalinPRO_0000008210
    Peptidei140 – 17940PENK(140-179)By similarityPRO_0000377683Add
    BLAST
    Peptidei182 – 1898Met-enkephalin-Arg-Gly-LeuPRO_0000008212
    Propeptidei192 – 20312PRO_0000008213Add
    BLAST
    Peptidei206 – 2105Met-enkephalinPRO_0000008214
    Propeptidei213 – 22311PRO_0000008215Add
    BLAST
    Peptidei226 – 2305Leu-enkephalinPRO_0000008216
    Peptidei233 – 26129EnkelytinPRO_0000008217Add
    BLAST
    Peptidei233 – 25422PENK(233-254)By similarityPRO_0000377684Add
    BLAST
    Peptidei257 – 2637Met-enkephalin-Arg-PhePRO_0000008218

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 48By similarity
    Disulfide bondi30 ↔ 52By similarity
    Disulfide bondi33 ↔ 65By similarity

    Post-translational modificationi

    The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PRIDEiP01211.

    Interactioni

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000006478.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40630.
    GeneTreeiENSGT00530000063761.
    HOGENOMiHOG000013003.
    HOVERGENiHBG000063.
    InParanoidiP01211.
    OMAiGGFMKKD.
    OrthoDBiEOG75TMCR.
    TreeFamiTF332620.

    Family and domain databases

    InterProiIPR006024. Opioid_neupept.
    IPR000703. Proenkphlin_A.
    [Graphical view]
    PANTHERiPTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF3. PTHR11438:SF3. 1 hit.
    PfamiPF01160. Opiods_neuropep. 1 hit.
    [Graphical view]
    PRINTSiPR01028. OPIOIDPRCRSR.
    PR01029. PENKAPRCRSR.
    PROSITEiPS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01211-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARFLGLCTW LLALGPGLLA TVRAECSQDC ATCSYRLARP TDLNPLACTL    50
    ECEGKLPSLK TWETCKELLQ LTKLELPPDA TSALSKQEES HLLAKKYGGF 100
    MKRYGGFMKK MDELYPLEVE EEANGGEVLG KRYGGFMKKD AEEDDGLGNS 150
    SNLLKELLGA GDQREGSLHQ EGSDAEDVSK RYGGFMRGLK RSPHLEDETK 200
    ELQKRYGGFM RRVGRPEWWM DYQKRYGGFL KRFAEPLPSE EEGESYSKEV 250
    PEMEKRYGGF MRF 263
    Length:263
    Mass (Da):29,788
    Last modified:July 21, 1986 - v1
    Checksum:i0E400338A228B0D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00109 mRNA. Translation: CAA23443.1.
    BC111279 mRNA. Translation: AAI11280.1.
    V00108 mRNA. Translation: CAA23442.1.
    J00012 mRNA. Translation: AAA30673.1.
    PIRiA93272. EQBOA.
    RefSeqiNP_776566.1. NM_174141.2.
    UniGeneiBt.166.

    Genome annotation databases

    EnsembliENSBTAT00000006478; ENSBTAP00000006478; ENSBTAG00000004924.
    GeneIDi281387.
    KEGGibta:281387.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00109 mRNA. Translation: CAA23443.1 .
    BC111279 mRNA. Translation: AAI11280.1 .
    V00108 mRNA. Translation: CAA23442.1 .
    J00012 mRNA. Translation: AAA30673.1 .
    PIRi A93272. EQBOA.
    RefSeqi NP_776566.1. NM_174141.2.
    UniGenei Bt.166.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000006478.

    Proteomic databases

    PRIDEi P01211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000006478 ; ENSBTAP00000006478 ; ENSBTAG00000004924 .
    GeneIDi 281387.
    KEGGi bta:281387.

    Organism-specific databases

    CTDi 5179.

    Phylogenomic databases

    eggNOGi NOG40630.
    GeneTreei ENSGT00530000063761.
    HOGENOMi HOG000013003.
    HOVERGENi HBG000063.
    InParanoidi P01211.
    OMAi GGFMKKD.
    OrthoDBi EOG75TMCR.
    TreeFami TF332620.

    Enzyme and pathway databases

    Reactomei REACT_210568. G alpha (i) signalling events.
    REACT_219025. Peptide ligand-binding receptors.

    Miscellaneous databases

    NextBioi 20805387.

    Family and domain databases

    InterProi IPR006024. Opioid_neupept.
    IPR000703. Proenkphlin_A.
    [Graphical view ]
    PANTHERi PTHR11438. PTHR11438. 1 hit.
    PTHR11438:SF3. PTHR11438:SF3. 1 hit.
    Pfami PF01160. Opiods_neuropep. 1 hit.
    [Graphical view ]
    PRINTSi PR01028. OPIOIDPRCRSR.
    PR01029. PENKAPRCRSR.
    PROSITEi PS01252. OPIOIDS_PRECURSOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin."
      Noda M., Furutani Y., Takahashi H., Toyosato M., Hirose T., Inayama S., Nakanishi S., Numa S.
      Nature 295:202-206(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    3. "Molecular cloning establishes proenkephalin as precursor of enkephalin-containing peptides."
      Gubler U., Seeburg P., Hoffman B.J., Gage L.P., Udenfriend S.
      Nature 295:206-208(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-263.
    4. "Partial characterization of the mRNA that codes for enkephalins in bovine adrenal medulla and human pheochromocytoma."
      Comb M., Herbert E., Crea R.
      Proc. Natl. Acad. Sci. U.S.A. 79:360-364(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-229.
    5. "The C-terminal bisphosphorylated proenkephalin-A-(209-237)-peptide from adrenal medullary chromaffin granules possesses antibacterial activity."
      Goumon Y., Strub J.-M., Moniatte M., Nulans G., Poteur L., Hubert P., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.
      Eur. J. Biochem. 235:516-525(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 233-261.
      Tissue: Chromaffin cell.

    Entry informationi

    Entry nameiPENK_BOVIN
    AccessioniPrimary (citable) accession number: P01211
    Secondary accession number(s): Q2T9T4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 99 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