PEBP1_RAT
ID PEBP1_RAT Reviewed; 187 AA.
AC P31044; P31045;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphatidylethanolamine-binding protein 1;
DE Short=PEBP-1;
DE AltName: Full=23 kDa morphine-binding protein;
DE AltName: Full=HCNPpp;
DE AltName: Full=P23K;
DE Contains:
DE RecName: Full=Hippocampal cholinergic neurostimulating peptide;
DE Short=HCNP;
GN Name=Pebp1; Synonyms=Pbp, Pebp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1978248; DOI=10.1210/mend-4-9-1370;
RA Grandy D.K., Hanneman E., Bunzow J., Shih M., Machida C.A., Bidlack J.M.,
RA Civelli O.;
RT "Purification, cloning, and tissue distribution of a 23-kDa rat protein
RT isolated by morphine affinity chromatography.";
RL Mol. Endocrinol. 4:1370-1376(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=7637590; DOI=10.1016/0169-328x(95)00029-r;
RA Tohdoh N., Tojo S., Agui H., Ojika K.;
RT "Sequence homology of rat and human HCNP precursor proteins, bovine
RT phosphatidylethanolamine-binding protein and rat 23-kDa protein associated
RT with the opioid-binding protein.";
RL Brain Res. Mol. Brain Res. 30:381-384(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Epididymis, and Liver;
RX PubMed=8037677; DOI=10.1042/bj3010235;
RA Perry A.C.F., Hall L., Bell A.E., Jones R.;
RT "Sequence analysis of a mammalian phospholipid-binding protein from testis
RT and epididymis and its distribution between spermatozoa and extracellular
RT secretions.";
RL Biochem. J. 301:235-242(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
RX PubMed=1611510; DOI=10.1016/0006-8993(92)90465-l;
RA Ojika K., Kojima S., Ueki Y., Fukushima N., Hayashi K., Yamamoto M.;
RT "Purification and structural analysis of hippocampal cholinergic
RT neurostimulating peptide.";
RL Brain Res. 572:164-171(1992).
RN [6]
RP PROTEIN SEQUENCE OF 27-62; 63-76; 81-113 AND 158-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Diao W., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 40-56 AND 93-112.
RC TISSUE=Sperm;
RX PubMed=1932083; DOI=10.1016/0167-4838(91)90114-f;
RA Jones R., Hall L.;
RT "A 23 kDa protein from rat sperm plasma membranes shows sequence similarity
RT and phospholipid binding properties to a bovine brain cytosolic protein.";
RL Biochim. Biophys. Acta 1080:78-82(1991).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10622376; DOI=10.1016/s0301-0082(99)00021-0;
RA Ojika K., Mitake S., Tohdoh N., Appel S.H., Otsuka Y., Katada E.,
RA Matsukawa N.;
RT "Hippocampal cholinergic neurostimulating peptides (HCNP).";
RL Prog. Neurobiol. 60:37-83(2000).
RN [9]
RP CHARACTERIZATION.
RX PubMed=12591138; DOI=10.1016/s0006-8993(02)04194-x;
RA Morishita M., Otsuka Y., Matsukawa N., Suzuki H., Nakazawa H., Maki M.,
RA Katou H., Ueda R., Ojika K.;
RT "Specific binding of 125I-hippocampal cholinergic neurostimulating peptide
RT (HCNP) to rat brain membranes: characterization and regional
RT distribution.";
RL Brain Res. 965:194-202(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-52 AND SER-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower
CC affinity for phosphatidylinositol and phosphatidylcholine. Serine
CC protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin
CC but not trypsin, tissue type plasminogen activator and elastase (By
CC similarity). Inhibits the kinase activity of RAF1 by inhibiting its
CC activation and by dissociating the RAF1/MEK complex and acting as a
CC competitive inhibitor of MEK phosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: HCNP may be involved in the function of the presynaptic
CC cholinergic neurons of the central nervous system. HCNP increases the
CC production of choline acetyltransferase but not acetylcholinesterase.
CC Seems to be mediated by a specific receptor.
CC -!- SUBUNIT: Has a tendency to form dimers by disulfide cross-linking.
CC Interacts with RAF1 and this interaction is enhanced if RAF1 is
CC phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-
CC 341'. Interacts with ALOX15; in response to IL13/interleukin-13,
CC prevents the interaction of PEBP1 with RAF1 to activate the ERK
CC signaling cascade (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Major component of epididymal secretions and sperm
CC plasma membranes. It is present in cytosols from a variety of other
CC tissues. Highly expressed in brain.
CC -!- MISCELLANEOUS: Seems to be associated with memory and learning
CC disorder.
CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. {ECO:0000305}.
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DR EMBL; X75253; CAA53032.1; -; mRNA.
DR EMBL; X75254; CAA53033.1; -; Genomic_DNA.
DR EMBL; X71873; CAA50708.1; -; mRNA.
DR EMBL; BC063171; AAH63171.1; -; mRNA.
DR PIR; A36126; A36126.
DR PIR; S18358; S18358.
DR RefSeq; NP_058932.1; NM_017236.1.
DR PDB; 2IQX; X-ray; 2.20 A; A/B/C=1-187.
DR PDB; 2IQY; X-ray; 1.40 A; A=1-187.
DR PDB; 6ENT; X-ray; 2.66 A; A=2-187.
DR PDBsum; 2IQX; -.
DR PDBsum; 2IQY; -.
DR PDBsum; 6ENT; -.
DR AlphaFoldDB; P31044; -.
DR BMRB; P31044; -.
DR SMR; P31044; -.
DR BioGRID; 248176; 11.
DR STRING; 10116.ENSRNOP00000001500; -.
DR MEROPS; I51.002; -.
DR iPTMnet; P31044; -.
DR PhosphoSitePlus; P31044; -.
DR World-2DPAGE; 0004:P31044; -.
DR jPOST; P31044; -.
DR PaxDb; P31044; -.
DR PRIDE; P31044; -.
DR GeneID; 29542; -.
DR KEGG; rno:29542; -.
DR UCSC; RGD:62017; rat.
DR CTD; 5037; -.
DR RGD; 62017; Pebp1.
DR VEuPathDB; HostDB:ENSRNOG00000001136; -.
DR eggNOG; KOG3346; Eukaryota.
DR HOGENOM; CLU_043994_5_0_1; -.
DR InParanoid; P31044; -.
DR OMA; TGCVMSD; -.
DR OrthoDB; 1557122at2759; -.
DR PhylomeDB; P31044; -.
DR TreeFam; TF315074; -.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR EvolutionaryTrace; P31044; -.
DR PRO; PR:P31044; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001136; Expressed in testis and 20 other tissues.
DR Genevisible; P31044; RN.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0008289; F:lipid binding; TAS:RGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0042755; P:eating behavior; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0000165; P:MAPK cascade; IDA:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0060409; P:positive regulation of acetylcholine metabolic process; IDA:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:RGD.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; IDA:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IDA:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR CDD; cd00866; PEBP_euk; 1.
DR Gene3D; 3.90.280.10; -; 1.
DR InterPro; IPR008914; PEBP.
DR InterPro; IPR036610; PEBP-like_sf.
DR InterPro; IPR035810; PEBP_euk.
DR InterPro; IPR001858; Phosphatidylethanolamine-bd_CS.
DR PANTHER; PTHR11362; PTHR11362; 1.
DR Pfam; PF01161; PBP; 1.
DR SUPFAM; SSF49777; SSF49777; 1.
DR PROSITE; PS01220; PBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipid-binding; Membrane;
KW Nucleotide-binding; Phosphoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1611510"
FT CHAIN 2..187
FT /note="Phosphatidylethanolamine-binding protein 1"
FT /id="PRO_0000023277"
FT PEPTIDE 2..12
FT /note="Hippocampal cholinergic neurostimulating peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023278"
FT REGION 93..134
FT /note="Interaction with RAF1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine; in peptide hippocampal cholinergic
FT neurostimulating"
FT /evidence="ECO:0000269|PubMed:1611510"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT CONFLICT 49
FT /note="R -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..55
FT /note="SW -> TA (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:2IQY"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2IQX"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2IQY"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2IQY"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2IQY"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2IQY"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:2IQY"
SQ SEQUENCE 187 AA; 20801 MW; F2BF053FE34B8056 CRC64;
MAADISQWAG PLSLQEVDEP PQHALRVDYG GVTVDELGKV LTPTQVMNRP SSISWDGLDP
GKLYTLVLTD PDAPSRKDPK FREWHHFLVV NMKGNDISSG TVLSEYVGSG PPKDTGLHRY
VWLVYEQEQP LNCDEPILSN KSGDNRGKFK VESFRKKYHL GAPVAGTCFQ AEWDDSVPKL
HDQLAGK
