PEBP1_BOVIN
ID PEBP1_BOVIN Reviewed; 187 AA.
AC P13696; Q3T0H9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phosphatidylethanolamine-binding protein 1;
DE Short=PEBP-1;
DE AltName: Full=Basic cytosolic 21 kDa protein;
DE AltName: Full=HCNPpp;
DE Contains:
DE RecName: Full=Hippocampal cholinergic neurostimulating peptide;
DE Short=HCNP;
GN Name=PEBP1; Synonyms=PBP, PEBP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-187.
RC TISSUE=Brain;
RX PubMed=3609012; DOI=10.1111/j.1432-1033.1987.tb13519.x;
RA Schoentgen F., Saccoccio F., Jolles J., Bernier I., Jolles P.;
RT "Complete amino acid sequence of a basic 21-kDa protein from bovine brain
RT cytosol.";
RL Eur. J. Biochem. 166:333-338(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).
RX PubMed=9782057; DOI=10.1016/s0969-2126(98)00126-9;
RA Serre L., Vallee B., Bureaud N., Schoentgen F., Zelwer C.;
RT "Crystal structure of the phosphatidylethanolamine-binding protein from
RT bovine brain: a novel structural class of phospholipid-binding proteins.";
RL Structure 6:1255-1265(1998).
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 (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 -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102389; AAI02390.1; -; mRNA.
DR PIR; S00056; S00056.
DR RefSeq; NP_001028795.1; NM_001033623.2.
DR PDB; 1A44; X-ray; 1.84 A; A=2-186.
DR PDB; 1B7A; X-ray; 2.25 A; A/B=2-187.
DR PDBsum; 1A44; -.
DR PDBsum; 1B7A; -.
DR AlphaFoldDB; P13696; -.
DR SMR; P13696; -.
DR BioGRID; 160663; 1.
DR IntAct; P13696; 1.
DR STRING; 9913.ENSBTAP00000024107; -.
DR MEROPS; I51.002; -.
DR PaxDb; P13696; -.
DR PeptideAtlas; P13696; -.
DR PRIDE; P13696; -.
DR Ensembl; ENSBTAT00000024107; ENSBTAP00000024107; ENSBTAG00000018115.
DR GeneID; 431786; -.
DR KEGG; bta:431786; -.
DR CTD; 5037; -.
DR VEuPathDB; HostDB:ENSBTAG00000018115; -.
DR VGNC; VGNC:32735; PEBP1.
DR eggNOG; KOG3346; Eukaryota.
DR GeneTree; ENSGT00940000157251; -.
DR HOGENOM; CLU_043994_5_0_1; -.
DR InParanoid; P13696; -.
DR OMA; TGCVMSD; -.
DR OrthoDB; 1557122at2759; -.
DR TreeFam; TF315074; -.
DR Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR EvolutionaryTrace; P13696; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000018115; Expressed in retina and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
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; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Lipid-binding; Nucleotide-binding; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Serine protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3609012"
FT CHAIN 2..187
FT /note="Phosphatidylethanolamine-binding protein 1"
FT /id="PRO_0000023269"
FT PEPTIDE 2..12
FT /note="Hippocampal cholinergic neurostimulating peptide"
FT /id="PRO_0000023270"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..134
FT /note="Interaction with RAF1"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31044"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT MOD_RES 52
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 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30086"
FT CONFLICT 118
FT /note="H -> R (in Ref. 1; AAI02390)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1A44"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1A44"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1A44"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1A44"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1A44"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1A44"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1A44"
SQ SEQUENCE 187 AA; 20986 MW; 1997AB34F966B649 CRC64;
MPVDLSKWSG PLSLQEVDER PQHPLQVKYG GAEVDELGKV LTPTQVKNRP TSITWDGLDP
GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNNISSG TVLSDYVGSG PPKGTGLHRY
VWLVYEQEGP LKCDEPILSN RSGDHRGKFK VASFRKKYEL GAPVAGTCYQ AEWDDYVPKL
YEQLSGK
