PEBP1_CANLF
ID PEBP1_CANLF Reviewed; 187 AA.
AC Q3YIX4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Phosphatidylethanolamine-binding protein 1;
DE Short=PEBP-1;
DE AltName: Full=HCNPpp;
DE AltName: Full=Raf kinase inhibitor protein;
DE Short=RKIP;
DE Contains:
DE RecName: Full=Hippocampal cholinergic neurostimulating peptide;
DE Short=HCNP;
GN Name=PEBP1; Synonyms=PBP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAF1, AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=16183022; DOI=10.1016/j.chembiol.2005.07.007;
RA Zhu S., Mc Henry K.T., Lane W.S., Fenteany G.;
RT "A chemical inhibitor reveals the role of Raf kinase inhibitor protein in
RT cell migration.";
RL Chem. Biol. 12:981-991(2005).
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). Involved in the positive regulation of epithelial cell
CC migration. 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; DQ130016; AAZ79335.1; -; mRNA.
DR RefSeq; NP_001041557.1; NM_001048092.1.
DR AlphaFoldDB; Q3YIX4; -.
DR SMR; Q3YIX4; -.
DR STRING; 9615.ENSCAFP00000059981; -.
DR MEROPS; I51.002; -.
DR PaxDb; Q3YIX4; -.
DR PRIDE; Q3YIX4; -.
DR Ensembl; ENSCAFT00000015761; ENSCAFP00000014590; ENSCAFG00000009910.
DR Ensembl; ENSCAFT00030046545; ENSCAFP00030040682; ENSCAFG00030025209.
DR GeneID; 477501; -.
DR KEGG; cfa:477501; -.
DR CTD; 5037; -.
DR eggNOG; KOG3346; Eukaryota.
DR InParanoid; Q3YIX4; -.
DR OrthoDB; 1557122at2759; -.
DR Reactome; R-CFA-5674135; MAP2K and MAPK activation.
DR Reactome; R-CFA-5675221; Negative regulation of MAPK pathway.
DR Proteomes; UP000002254; 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 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 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_0000276760"
FT PEPTIDE 1..12
FT /note="Hippocampal cholinergic neurostimulating peptide"
FT /id="PRO_0000276761"
FT REGION 93..134
FT /note="Interaction with RAF1"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 187 AA; 20922 MW; 242C36492684548B CRC64;
MPVDLGKWSG PLSLQEVEER PQHALHVKYT GTEVDELGKV LTPTQVKNRP TSIAWDGLDP
GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG TVLSDYVGSG PPKGTGLHRY
VWLVYEQSGP LKCDEPILSN RSGDHRGKFK VASFRKKYEL GPPVAGTCYQ AEWDDYVPKL
CEQLSGK
