ID   PEBP1_RABIT             Reviewed;         187 AA.
AC   Q8MK67;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Qian Z., Barmack N.H.;
RT   "Activity-dependent expression of phosphatidylethanolamine-binding protein
RT   (PEBP) in rabbit cerebellum by optokinetic stimulation.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY094175; AAM22502.1; -; mRNA.
DR   RefSeq; NP_001075612.1; NM_001082143.1.
DR   AlphaFoldDB; Q8MK67; -.
DR   SMR; Q8MK67; -.
DR   STRING; 9986.ENSOCUP00000007249; -.
DR   MEROPS; I51.002; -.
DR   GeneID; 100008884; -.
DR   KEGG; ocu:100008884; -.
DR   CTD; 5037; -.
DR   eggNOG; KOG3346; Eukaryota.
DR   InParanoid; Q8MK67; -.
DR   OrthoDB; 1557122at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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   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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Disulfide bond; Lipid-binding; Nucleotide-binding;
KW   Phosphoprotein; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..187
FT                   /note="Phosphatidylethanolamine-binding protein 1"
FT                   /id="PRO_0000276762"
FT   PEPTIDE         1..12
FT                   /note="Hippocampal cholinergic neurostimulating peptide"
FT                   /id="PRO_0000276763"
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"
SQ   SEQUENCE   187 AA;  20994 MW;  3109EFEEFD6FD61A CRC64;
     MPVDLSKWSG PLSLQEVEER PQHPLQVTYS GVALDELGQV LTPTQVKNRP TSIVWDGLDP
     DKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGGNISSG TVLSDYVGSG PPKGTGLHRY
     VWLVYEQDGP LKCDEPVLSN RSGDHRGKFK VANFRKKYHL GTPVAGSCYQ AEWDDYVPKL
     YELLSGK