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Protein

Phosphatidylethanolamine-binding protein 1

Gene

PEBP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-5674135. MAP2K and MAPK activation.
R-BTA-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):
Basic cytosolic 21 kDa protein
HCNPpp
Cleaved into the following chain:
Gene namesi
Name:PEBP1
Synonyms:PBP, PEBP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 187186Phosphatidylethanolamine-binding protein 1PRO_0000023269Add
BLAST
Peptidei2 – 1211Hippocampal cholinergic neurostimulating peptidePRO_0000023270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei42 – 421PhosphothreonineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei153 – 1531PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP13696.
PRIDEiP13696.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024107.

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 – 294Combined sources
Beta strandi32 – 343Combined sources
Turni43 – 464Combined sources
Beta strandi51 – 544Combined sources
Beta strandi62 – 709Combined 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
1A44X-ray1.84A2-186[»]
1B7AX-ray2.25A/B2-187[»]
ProteinModelPortaliP13696.
SMRiP13696. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13696.

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.
InParanoidiP13696.
OMAiGKFKVAN.
OrthoDBiEOG7P02K3.
TreeFamiTF315074.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR008914. PEBP.
IPR001858. Phosphotidylethanolamine-bd_CS.
[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.

P13696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVDLSKWSG PLSLQEVDER PQHPLQVKYG GAEVDELGKV LTPTQVKNRP
60 70 80 90 100
TSITWDGLDP GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNNISSG
110 120 130 140 150
TVLSDYVGSG PPKGTGLHRY VWLVYEQEGP LKCDEPILSN RSGDHRGKFK
160 170 180
VASFRKKYEL GAPVAGTCYQ AEWDDYVPKL YEQLSGK
Length:187
Mass (Da):20,986
Last modified:January 23, 2007 - v2
Checksum:i1997AB34F966B649
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181H → R in AAI02390 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102389 mRNA. Translation: AAI02390.1.
PIRiS00056.
RefSeqiNP_001028795.1. NM_001033623.2.
UniGeneiBt.59089.

Genome annotation databases

EnsembliENSBTAT00000024107; ENSBTAP00000024107; ENSBTAG00000018115.
GeneIDi431786.
KEGGibta:431786.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102389 mRNA. Translation: AAI02390.1.
PIRiS00056.
RefSeqiNP_001028795.1. NM_001033623.2.
UniGeneiBt.59089.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A44X-ray1.84A2-186[»]
1B7AX-ray2.25A/B2-187[»]
ProteinModelPortaliP13696.
SMRiP13696. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024107.

Protein family/group databases

MEROPSiI51.002.

Proteomic databases

PaxDbiP13696.
PRIDEiP13696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024107; ENSBTAP00000024107; ENSBTAG00000018115.
GeneIDi431786.
KEGGibta:431786.

Organism-specific databases

CTDi5037.

Phylogenomic databases

eggNOGiKOG3346. Eukaryota.
COG1881. LUCA.
GeneTreeiENSGT00840000129869.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP13696.
OMAiGKFKVAN.
OrthoDBiEOG7P02K3.
TreeFamiTF315074.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP13696.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR008914. PEBP.
IPR001858. Phosphotidylethanolamine-bd_CS.
[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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  2. "Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol."
    Schoentgen F., Saccoccio F., Jolles J., Bernier I., Jolles P.
    Eur. J. Biochem. 166:333-338(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-187.
    Tissue: Brain.
  3. "Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins."
    Serre L., Vallee B., Bureaud N., Schoentgen F., Zelwer C.
    Structure 6:1255-1265(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).

Entry informationi

Entry nameiPEBP1_BOVIN
AccessioniPrimary (citable) accession number: P13696
Secondary accession number(s): Q3T0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 123 of the entry and version 2 of the sequence. [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

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.