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Protein

Proenkephalin-A

Gene

PENK

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
OMAiFMKKMDE.
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

        10         20         30         40         50
MARFLGLCTW LLALGPGLLA TVRAECSQDC ATCSYRLARP TDLNPLACTL
60 70 80 90 100
ECEGKLPSLK TWETCKELLQ LTKLELPPDA TSALSKQEES HLLAKKYGGF
110 120 130 140 150
MKRYGGFMKK MDELYPLEVE EEANGGEVLG KRYGGFMKKD AEEDDGLGNS
160 170 180 190 200
SNLLKELLGA GDQREGSLHQ EGSDAEDVSK RYGGFMRGLK RSPHLEDETK
210 220 230 240 250
ELQKRYGGFM RRVGRPEWWM DYQKRYGGFL KRFAEPLPSE EEGESYSKEV
260
PEMEKRYGGF MRF
Length:263
Mass (Da):29,788
Last modified:July 21, 1986 - v1
Checksum:i0E400338A228B0D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006478.

Proteomic databases

PRIDEiP01211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5179.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20805387.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 101 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.