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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.

GO - Molecular functioni

  • ATP 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
  • 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: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

ATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi62017. Pebp1.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: RGD
  • axon terminus Source: RGD
  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • extracellular space Source: RGD
  • Golgi apparatus Source: RGD
  • mitochondrial outer membrane Source: RGD
  • mitochondrion Source: RGD
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • rough endoplasmic reticulum Source: RGD
  • synaptic vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 187186Phosphatidylethanolamine-binding protein 1PRO_0000023277Add
BLAST
Peptidei2 – 1211Hippocampal cholinergic neurostimulating peptideBy similarityPRO_0000023278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine; in peptide hippocampal cholinergic neurostimulating1 Publication
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei42 – 421PhosphothreonineBy similarity
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP31044.
PRIDEiP31044.

2D gel databases

World-2DPAGE0004:P31044.

PTM databases

iPTMnetiP31044.
PhosphoSiteiP31044.

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

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

  • 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 interactions.
MINTiMINT-4568954.
STRINGi10116.ENSRNOP00000001500.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi14 – 163Combined sources
Beta strandi22 – 243Combined sources
Beta strandi26 – 283Combined sources
Beta strandi32 – 343Combined sources
Helixi43 – 464Combined sources
Beta strandi51 – 544Combined sources
Beta strandi62 – 7413Combined sources
Beta strandi76 – 783Combined sources
Beta strandi84 – 9310Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi118 – 1269Combined sources
Helixi151 – 1577Combined sources
Beta strandi164 – 1718Combined sources
Helixi177 – 1848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQXX-ray2.20A/B/C1-187[»]
2IQYX-ray1.40A1-187[»]
ProteinModelPortaliP31044.
SMRiP31044. Positions 1-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31044.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 13442Interaction with RAF1By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3346. Eukaryota.
COG1881. LUCA.
GeneTreeiENSGT00840000129869.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP31044.
OMAiSIEWEGC.
OrthoDBiEOG7P02K3.
PhylomeDBiP31044.
TreeFamiTF315074.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491R → G AA sequence (PubMed:1932083).Curated
Sequence conflicti54 – 552SW → TA AA sequence (PubMed:1932083).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQXX-ray2.20A/B/C1-187[»]
2IQYX-ray1.40A1-187[»]
ProteinModelPortaliP31044.
SMRiP31044. Positions 1-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiI51.002.

PTM databases

iPTMnetiP31044.
PhosphoSiteiP31044.

2D gel databases

World-2DPAGE0004:P31044.

Proteomic databases

PaxDbiP31044.
PRIDEiP31044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5037.
RGDi62017. Pebp1.

Phylogenomic databases

eggNOGiKOG3346. Eukaryota.
COG1881. LUCA.
GeneTreeiENSGT00840000129869.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP31044.
OMAiSIEWEGC.
OrthoDBiEOG7P02K3.
PhylomeDBiP31044.
TreeFamiTF315074.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP31044.
NextBioi609545.
PROiP31044.

Gene expression databases

GenevisibleiP31044. RN.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, cloning, and tissue distribution of a 23-kDa rat protein isolated by morphine affinity chromatography."
    Grandy D.K., Hanneman E., Bunzow J., Shih M., Machida C.A., Bidlack J.M., Civelli O.
    Mol. Endocrinol. 4:1370-1376(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein."
    Tohdoh N., Tojo S., Agui H., Ojika K.
    Brain Res. Mol. Brain Res. 30:381-384(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Wistar.
    Tissue: Hippocampus.
  3. "Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions."
    Perry A.C.F., Hall L., Bell A.E., Jones R.
    Biochem. J. 301:235-242(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Epididymis and Liver.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  5. "Purification and structural analysis of hippocampal cholinergic neurostimulating peptide."
    Ojika K., Kojima S., Ueki Y., Fukushima N., Hayashi K., Yamamoto M.
    Brain Res. 572:164-171(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2.
  6. Lubec G., Diao W., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 27-62; 63-76; 81-113 AND 158-179, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  7. "A 23 kDa protein from rat sperm plasma membranes shows sequence similarity and phospholipid binding properties to a bovine brain cytosolic protein."
    Jones R., Hall L.
    Biochim. Biophys. Acta 1080:78-82(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-56 AND 93-112.
    Tissue: Sperm.
  8. Cited for: CHARACTERIZATION.
  9. "Specific binding of 125I-hippocampal cholinergic neurostimulating peptide (HCNP) to rat brain membranes: characterization and regional distribution."
    Morishita M., Otsuka Y., Matsukawa N., Suzuki H., Nakazawa H., Maki M., Katou H., Ueda R., Ojika K.
    Brain Res. 965:194-202(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-52 AND SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPEBP1_RAT
AccessioniPrimary (citable) accession number: P31044
Secondary accession number(s): P31045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Seems to be associated with memory and learning disorder.

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

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 one 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.