PEBP1_MOUSE
ID PEBP1_MOUSE Reviewed; 187 AA.
AC P70296; Q9D8G9; Q9JJ58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Phosphatidylethanolamine-binding protein 1;
DE Short=PEBP-1;
DE AltName: Full=HCNPpp;
DE Contains:
DE RecName: Full=Hippocampal cholinergic neurostimulating peptide;
DE Short=HCNP;
GN Name=Pebp1; Synonyms=Pbp, Pebp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lin B., Frischauf A.-M.;
RT "Cloning of mouse phosphatidylethanolamine binding protein gene.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10051191; DOI=10.1016/s0306-4522(98)00215-2;
RA Matsukawa N., Tooyama I., Kimura H., Yamamoto T., Tsugu Y., Oomura Y.,
RA Ojika K.;
RT "Increased expression of hippocampal cholinergic neurostimulating peptide-
RT related components and their messenger RNAs in the hippocampus of aged
RT senescence-accelerated mice.";
RL Neuroscience 88:79-92(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Matsukawa N.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-39; 63-76; 94-141
RP AND 158-180.
RC STRAIN=C57BL/6J;
RX PubMed=11034991; DOI=10.1074/jbc.m002524200;
RA Hengst U., Albrecht H., Hess D., Monard D.;
RT "The phosphatidylethanolamine-binding protein is the prototype of a novel
RT family of serine protease inhibitors.";
RL J. Biol. Chem. 276:535-540(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Mammary gland, and Retina;
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 [7]
RP PROTEIN SEQUENCE OF 63-76 AND 94-119, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC Inhibits the kinase activity of RAF1 by inhibiting its activation and
CC by dissociating the RAF1/MEK complex and acting as a competitive
CC inhibitor of MEK phosphorylation (By similarity). {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 (By similarity).
CC {ECO:0000250}.
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.
CC -!- TISSUE SPECIFICITY: HCNP is expressed in brain. Increased expression in
CC aged senescence-accelerated mice.
CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. {ECO:0000305}.
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DR EMBL; U43206; AAB06983.1; -; mRNA.
DR EMBL; AF300422; AAG25635.1; -; mRNA.
DR EMBL; AB046417; BAB03276.1; -; mRNA.
DR EMBL; AK088212; BAC40214.1; -; mRNA.
DR EMBL; BC008169; AAH08169.1; -; mRNA.
DR EMBL; BC083063; AAH83063.1; -; mRNA.
DR CCDS; CCDS39234.1; -.
DR PIR; PN0043; PN0043.
DR RefSeq; NP_061346.2; NM_018858.2.
DR PDB; 6ENS; X-ray; 1.30 A; A=2-187.
DR PDBsum; 6ENS; -.
DR AlphaFoldDB; P70296; -.
DR SMR; P70296; -.
DR BioGRID; 204834; 11.
DR IntAct; P70296; 3.
DR STRING; 10090.ENSMUSP00000048425; -.
DR MEROPS; I51.002; -.
DR iPTMnet; P70296; -.
DR PhosphoSitePlus; P70296; -.
DR SwissPalm; P70296; -.
DR REPRODUCTION-2DPAGE; P70296; -.
DR UCD-2DPAGE; P70296; -.
DR CPTAC; non-CPTAC-3731; -.
DR CPTAC; non-CPTAC-3995; -.
DR EPD; P70296; -.
DR jPOST; P70296; -.
DR PaxDb; P70296; -.
DR PeptideAtlas; P70296; -.
DR PRIDE; P70296; -.
DR ProteomicsDB; 287670; -.
DR TopDownProteomics; P70296; -.
DR DNASU; 23980; -.
DR Ensembl; ENSMUST00000036951; ENSMUSP00000048425; ENSMUSG00000032959.
DR GeneID; 23980; -.
DR KEGG; mmu:23980; -.
DR UCSC; uc008zfl.1; mouse.
DR CTD; 5037; -.
DR MGI; MGI:1344408; Pebp1.
DR VEuPathDB; HostDB:ENSMUSG00000032959; -.
DR eggNOG; KOG3346; Eukaryota.
DR GeneTree; ENSGT00940000157251; -.
DR InParanoid; P70296; -.
DR OMA; TGCVMSD; -.
DR OrthoDB; 1557122at2759; -.
DR PhylomeDB; P70296; -.
DR TreeFam; TF315074; -.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 23980; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Pebp1; mouse.
DR PRO; PR:P70296; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P70296; protein.
DR Bgee; ENSMUSG00000032959; Expressed in testis and 64 other tissues.
DR ExpressionAtlas; P70296; baseline and differential.
DR Genevisible; P70296; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0060409; P:positive regulation of acetylcholine metabolic process; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; ISO:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:MGI.
DR GO; GO:0048240; P:sperm capacitation; IDA:MGI.
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;
KW Nucleotide-binding; Phosphoprotein; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10051191"
FT CHAIN 2..187
FT /note="Phosphatidylethanolamine-binding protein 1"
FT /id="PRO_0000023275"
FT PEPTIDE 2..12
FT /note="Hippocampal cholinergic neurostimulating peptide"
FT /id="PRO_0000023276"
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:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 116
FT /note="G -> S (in Ref. 1; AAB06983)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:6ENS"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6ENS"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:6ENS"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6ENS"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:6ENS"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6ENS"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6ENS"
SQ SEQUENCE 187 AA; 20830 MW; 4059C7C6E4A8BAA0 CRC64;
MAADISQWAG PLCLQEVDEP PQHALRVDYA GVTVDELGKV LTPTQVMNRP SSISWDGLDP
GKLYTLVLTD PDAPSRKDPK FREWHHFLVV NMKGNDISSG TVLSDYVGSG PPSGTGLHRY
VWLVYEQEQP LSCDEPILSN KSGDNRGKFK VETFRKKYNL GAPVAGTCYQ AEWDDYVPKL
YEQLSGK
