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P70296 (PEBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylethanolamine-binding protein 1

Short name=PEBP-1
Alternative name(s):
HCNPpp

Cleaved into the following chain:

  1. Hippocampal cholinergic neurostimulating peptide
    Short name=HCNP
Gene names
Name:Pebp1
Synonyms:Pbp, Pebp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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.

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.

Subunit structure

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.

Subcellular location

Cytoplasm.

Tissue specificity

HCNP is expressed in brain. Increased expression in aged senescence-accelerated mice.

Sequence similarities

Belongs to the phosphatidylethanolamine-binding protein family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

eating behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of acetylcholine metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

regulation of neurotransmitter levels

Inferred from electronic annotation. Source: Ensembl

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from electronic annotation. Source: Ensembl

sperm capacitation

Inferred from direct assay PubMed 16183867. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from electronic annotation. Source: Ensembl

axon terminus

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 16183867. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 187186Phosphatidylethanolamine-binding protein 1
PRO_0000023275
Peptide2 – 1211Hippocampal cholinergic neurostimulating peptide Ref.2
PRO_0000023276

Regions

Region93 – 13442Interaction with RAF1 By similarity

Amino acid modifications

Modified residue21N-acetylalanine; in peptide hippocampal cholinergic neurostimulating By similarity
Modified residue421Phosphothreonine By similarity
Modified residue521Phosphoserine By similarity

Experimental info

Sequence conflict1161G → S in AAB06983. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70296 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4059C7C6E4A8BAA0

FASTA18720,830
        10         20         30         40         50         60 
MAADISQWAG PLCLQEVDEP PQHALRVDYA GVTVDELGKV LTPTQVMNRP SSISWDGLDP 

        70         80         90        100        110        120 
GKLYTLVLTD PDAPSRKDPK FREWHHFLVV NMKGNDISSG TVLSDYVGSG PPSGTGLHRY 

       130        140        150        160        170        180 
VWLVYEQEQP LSCDEPILSN KSGDNRGKFK VETFRKKYNL GAPVAGTCYQ AEWDDYVPKL 


YEQLSGK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of mouse phosphatidylethanolamine binding protein gene."
Lin B., Frischauf A.-M.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Increased expression of hippocampal cholinergic neurostimulating peptide-related components and their messenger RNAs in the hippocampus of aged senescence-accelerated mice."
Matsukawa N., Tooyama I., Kimura H., Yamamoto T., Tsugu Y., Oomura Y., Ojika K.
Neuroscience 88:79-92(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12.
Strain: BALB/c.
Tissue: Brain.
[3]Matsukawa N.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors."
Hengst U., Albrecht H., Hess D., Monard D.
J. Biol. Chem. 276:535-540(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-39; 63-76; 94-141 AND 158-180.
Strain: C57BL/6.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[6]"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].
Strain: C57BL/6 and NMRI.
Tissue: Mammary gland and Retina.
[7]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 63-76 AND 94-119, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43206 mRNA. Translation: AAB06983.1.
AF300422 mRNA. Translation: AAG25635.1.
AB046417 mRNA. Translation: BAB03276.1.
AK088212 mRNA. Translation: BAC40214.1.
BC008169 mRNA. Translation: AAH08169.1.
BC083063 mRNA. Translation: AAH83063.1.
CCDSCCDS39234.1.
PIRPN0043.
RefSeqNP_061346.2. NM_018858.2.
UniGeneMm.195898.
Mm.338476.
Mm.371595.

3D structure databases

ProteinModelPortalP70296.
SMRP70296. Positions 1-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204834. 1 interaction.
IntActP70296. 5 interactions.
MINTMINT-1869573.
STRING10090.ENSMUSP00000107604.

Protein family/group databases

MEROPSI51.002.

PTM databases

PhosphoSiteP70296.

2D gel databases

REPRODUCTION-2DPAGEP70296.
UCD-2DPAGEP70296.

Proteomic databases

MaxQBP70296.
PaxDbP70296.
PRIDEP70296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036951; ENSMUSP00000048425; ENSMUSG00000032959.
GeneID23980.
KEGGmmu:23980.
UCSCuc008zfl.1. mouse.

Organism-specific databases

CTD5037.
MGIMGI:1344408. Pebp1.

Phylogenomic databases

eggNOGNOG146517.
HOGENOMHOG000237655.
HOVERGENHBG008165.
OrthoDBEOG7P02K3.
PhylomeDBP70296.
TreeFamTF315074.

Gene expression databases

ArrayExpressP70296.
BgeeP70296.
CleanExMM_PEBP1.
GenevestigatorP70296.

Family and domain databases

Gene3D3.90.280.10. 1 hit.
InterProIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMSSF49777. SSF49777. 1 hit.
PROSITEPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303865.
PROP70296.
SOURCESearch...

Entry information

Entry namePEBP1_MOUSE
AccessionPrimary (citable) accession number: P70296
Secondary accession number(s): Q9D8G9, Q9JJ58
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot