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Protein

Phosphatidylethanolamine-binding protein 1

Gene

Pebp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity).By similarity
HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor.

Miscellaneous

Seems to be associated with memory and learning disorder.

GO - Molecular functioni

  • ATP binding Source: RGD
  • enzyme binding Source: RGD
  • kinase binding Source: RGD
  • lipid binding Source: RGD
  • mitogen-activated protein kinase binding Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • RNA binding Source: RGD
  • serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  • aging Source: RGD
  • eating behavior Source: RGD
  • hippocampus development Source: RGD
  • MAPK cascade Source: RGD
  • negative regulation of MAPK cascade Source: RGD
  • negative regulation of protein phosphorylation Source: RGD
  • positive regulation of acetylcholine metabolic process Source: RGD
  • positive regulation of cAMP-mediated signaling Source: RGD
  • positive regulation of mitotic nuclear division Source: RGD
  • regulation of neurotransmitter levels Source: RGD
  • regulation of the force of heart contraction Source: RGD
  • response to activity Source: RGD
  • response to calcium ion Source: RGD
  • response to cAMP Source: RGD
  • response to corticosterone Source: RGD
  • response to drug Source: RGD
  • response to electrical stimulus Source: RGD
  • response to ethanol Source: RGD
  • response to heat Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to oxidative stress Source: RGD
  • response to toxic substance Source: RGD
  • response to wounding Source: RGD
  • spermatid development Source: RGD
  • sperm capacitation Source: RGD

Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor
LigandATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-5674135. MAP2K and MAPK activation.
R-RNO-5675221. Negative regulation of MAPK pathway.

Protein family/group databases

MEROPSiI51.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine-binding protein 1
Short name:
PEBP-1
Alternative name(s):
23 kDa morphine-binding protein
HCNPpp
P23K
Cleaved into the following chain:
Gene namesi
Name:Pebp1
Synonyms:Pbp, Pebp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi62017. Pebp1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000232772 – 187Phosphatidylethanolamine-binding protein 1Add BLAST186
PeptideiPRO_00000232782 – 12Hippocampal cholinergic neurostimulating peptideBy similarityAdd BLAST11

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; in peptide hippocampal cholinergic neurostimulating1 Publication1
Modified residuei6PhosphoserineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei42PhosphothreonineBy similarity1
Modified residuei52PhosphoserineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei98PhosphoserineBy similarity1
Modified residuei153PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP31044.
PRIDEiP31044.

2D gel databases

World-2DPAGEi0004:P31044.

PTM databases

iPTMnetiP31044.
PhosphoSitePlusiP31044.

Expressioni

Tissue specificityi

Major component of epididymal secretions and sperm plasma membranes. It is present in cytosols from a variety of other tissues. Highly expressed in brain.

Gene expression databases

BgeeiENSRNOG00000001136.
GenevisibleiP31044. RN.

Interactioni

Subunit structurei

Has a tendency to form dimers by disulfide cross-linking. Interacts with RAF1 and this interaction is enhanced if RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: RGD
  • kinase binding Source: RGD
  • mitogen-activated protein kinase binding Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

BioGridi248176. 10 interactors.
MINTiMINT-4568954.
STRINGi10116.ENSRNOP00000001500.

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Helixi14 – 16Combined sources3
Beta strandi22 – 24Combined sources3
Beta strandi26 – 28Combined sources3
Beta strandi32 – 34Combined sources3
Helixi43 – 46Combined sources4
Beta strandi51 – 54Combined sources4
Beta strandi62 – 74Combined sources13
Beta strandi76 – 78Combined sources3
Beta strandi84 – 93Combined sources10
Helixi97 – 99Combined sources3
Beta strandi100 – 104Combined sources5
Beta strandi118 – 126Combined sources9
Helixi151 – 157Combined sources7
Beta strandi164 – 171Combined sources8
Helixi177 – 184Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IQXX-ray2.20A/B/C1-187[»]
2IQYX-ray1.40A1-187[»]
ProteinModelPortaliP31044.
SMRiP31044.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31044.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 134Interaction with RAF1By similarityAdd BLAST42

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3346. Eukaryota.
COG1881. LUCA.
GeneTreeiENSGT00900000141013.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP31044.
OMAiRPTSIEW.
OrthoDBiEOG091G0KH6.
PhylomeDBiP31044.
TreeFamiTF315074.

Family and domain databases

CDDicd00866. PEBP_euk. 1 hit.
Gene3Di3.90.280.10. 1 hit.
InterProiView protein in InterPro
IPR008914. PEBP.
IPR036610. PEBP-like_sf.
IPR035810. PEBP_euk.
IPR001858. Phosphotidylethanolamine-bd_CS.
PANTHERiPTHR11362. PTHR11362. 1 hit.
PfamiView protein in Pfam
PF01161. PBP. 1 hit.
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiView protein in PROSITE
PS01220. PBP. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P31044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAADISQWAG PLSLQEVDEP PQHALRVDYG GVTVDELGKV LTPTQVMNRP
60 70 80 90 100
SSISWDGLDP GKLYTLVLTD PDAPSRKDPK FREWHHFLVV NMKGNDISSG
110 120 130 140 150
TVLSEYVGSG PPKDTGLHRY VWLVYEQEQP LNCDEPILSN KSGDNRGKFK
160 170 180
VESFRKKYHL GAPVAGTCFQ AEWDDSVPKL HDQLAGK
Length:187
Mass (Da):20,801
Last modified:January 23, 2007 - v3
Checksum:iF2BF053FE34B8056
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49R → G AA sequence (PubMed:1932083).Curated1
Sequence conflicti54 – 55SW → TA AA sequence (PubMed:1932083).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75253 mRNA. Translation: CAA53032.1.
X75254 Genomic DNA. Translation: CAA53033.1.
X71873 mRNA. Translation: CAA50708.1.
BC063171 mRNA. Translation: AAH63171.1.
PIRiA36126.
S18358.
RefSeqiNP_058932.1. NM_017236.1.
UniGeneiRn.29745.

Genome annotation databases

EnsembliENSRNOT00000001500; ENSRNOP00000001500; ENSRNOG00000001136.
GeneIDi29542.
KEGGirno:29542.
UCSCiRGD:62017. rat.

Similar proteinsi

Entry informationi

Entry nameiPEBP1_RAT
AccessioniPrimary (citable) accession number: P31044
Secondary accession number(s): P31045
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 150 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families