PEBP4_HUMAN
ID PEBP4_HUMAN Reviewed; 227 AA.
AC Q96S96; Q5EVA1; Q8WW74;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phosphatidylethanolamine-binding protein 4;
DE Short=PEBP-4;
DE Short=hPEBP4;
DE AltName: Full=Protein cousin-of-RKIP 1;
DE Flags: Precursor;
GN Name=PEBP4; Synonyms=CORK1; ORFNames=UNQ1933/PRO4408;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-125.
RA Garcia R.L., Fee F., Kolch W.;
RT "Cousin-of-RKIP 1 promotes myoblast differentiation.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-211.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-125 AND GLY-211.
RC TISSUE=Lung;
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 [4]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [5]
RP RETRACTED PAPER.
RX PubMed=15302887; DOI=10.1074/jbc.m405147200;
RA Wang X., Li N., Liu B., Sun H., Chen T., Li H., Qiu J., Zhang L., Wan T.,
RA Cao X.;
RT "A novel human phosphatidylethanolamine-binding protein resists tumor
RT necrosis factor alpha-induced apoptosis by inhibiting mitogen-activated
RT protein kinase pathway activation and phosphatidylethanolamine
RT externalization.";
RL J. Biol. Chem. 279:45855-45864(2004).
RN [6]
RP RETRACTION NOTICE OF PUBMED:15302887.
RX PubMed=32978330; DOI=10.1074/jbc.w120.015697;
RA Wang X., Li N., Liu B., Sun H., Chen T., Li H., Qiu J., Zhang L., Wan T.,
RA Cao X.;
RL J. Biol. Chem. 295:13692-13692(2020).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-169.
RX PubMed=27033522; DOI=10.1016/j.bbamcr.2016.03.022;
RA He H., Liu D., Lin H., Jiang S., Ying Y., Chun S., Deng H., Zaia J.,
RA Wen R., Luo Z.;
RT "Phosphatidylethanolamine binding protein 4 (PEBP4) is a secreted protein
RT and has multiple functions.";
RL Biochim. Biophys. Acta 1863:1682-1689(2016).
CC -!- FUNCTION: Promotes AKT phosphorylation, suggesting a possible role in
CC the PI3K-AKT signaling pathway. {ECO:0000269|PubMed:27033522}.
CC -!- INTERACTION:
CC Q96S96; P31749: AKT1; NbExp=2; IntAct=EBI-8563667, EBI-296087;
CC Q96S96; P04049: RAF1; NbExp=4; IntAct=EBI-8563667, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27033522}.
CC -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC family. {ECO:0000305}.
CC -!- CAUTION: It was previously reported that PEBP4 is a lysosomal protein
CC which is highly expressed in tumor cells, and may promote cellular
CC resistance to TNF-induced apoptosis. However the paper has since been
CC retracted by the journal due to concerns of image manipulation.
CC {ECO:0000305|PubMed:15302887, ECO:0000305|PubMed:32978330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20779.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ89467.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY037148; AAK67629.1; -; mRNA.
DR EMBL; AY730275; AAW56965.1; -; mRNA.
DR EMBL; AY359109; AAQ89467.1; ALT_FRAME; mRNA.
DR EMBL; BC020779; AAH20779.1; ALT_FRAME; mRNA.
DR CCDS; CCDS43724.1; -.
DR RefSeq; NP_659399.2; NM_144962.2.
DR RefSeq; XP_011542716.1; XM_011544414.2.
DR AlphaFoldDB; Q96S96; -.
DR SMR; Q96S96; -.
DR BioGRID; 127592; 4.
DR IntAct; Q96S96; 4.
DR MINT; Q96S96; -.
DR STRING; 9606.ENSP00000256404; -.
DR GlyGen; Q96S96; 1 site.
DR BioMuta; PEBP4; -.
DR DMDM; 143811436; -.
DR jPOST; Q96S96; -.
DR MassIVE; Q96S96; -.
DR PaxDb; Q96S96; -.
DR PeptideAtlas; Q96S96; -.
DR PRIDE; Q96S96; -.
DR ProteomicsDB; 78091; -.
DR Antibodypedia; 5316; 132 antibodies from 24 providers.
DR DNASU; 157310; -.
DR Ensembl; ENST00000256404.8; ENSP00000256404.6; ENSG00000134020.8.
DR GeneID; 157310; -.
DR KEGG; hsa:157310; -.
DR MANE-Select; ENST00000256404.8; ENSP00000256404.6; NM_144962.3; NP_659399.2.
DR UCSC; uc003xcn.2; human.
DR CTD; 157310; -.
DR DisGeNET; 157310; -.
DR GeneCards; PEBP4; -.
DR HGNC; HGNC:28319; PEBP4.
DR HPA; ENSG00000134020; Tissue enhanced (epididymis, skeletal muscle, tongue).
DR MIM; 612473; gene.
DR neXtProt; NX_Q96S96; -.
DR OpenTargets; ENSG00000134020; -.
DR PharmGKB; PA165585814; -.
DR VEuPathDB; HostDB:ENSG00000134020; -.
DR eggNOG; KOG3346; Eukaryota.
DR GeneTree; ENSGT00940000162387; -.
DR HOGENOM; CLU_089676_0_0_1; -.
DR InParanoid; Q96S96; -.
DR OMA; QKITSWM; -.
DR OrthoDB; 1557122at2759; -.
DR PhylomeDB; Q96S96; -.
DR TreeFam; TF315074; -.
DR PathwayCommons; Q96S96; -.
DR SignaLink; Q96S96; -.
DR BioGRID-ORCS; 157310; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; PEBP4; human.
DR GenomeRNAi; 157310; -.
DR Pharos; Q96S96; Tbio.
DR PRO; PR:Q96S96; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96S96; protein.
DR Bgee; ENSG00000134020; Expressed in vastus lateralis and 137 other tissues.
DR ExpressionAtlas; Q96S96; baseline and differential.
DR Genevisible; Q96S96; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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 Direct protein sequencing; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..227
FT /note="Phosphatidylethanolamine-binding protein 4"
FT /id="PRO_0000023279"
FT REGION 188..227
FT /note="Important for secretion"
FT /evidence="ECO:0000269|PubMed:27033522"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:27033522"
FT VARIANT 125
FT /note="K -> E (in dbSNP:rs1129474)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_050467"
FT VARIANT 211
FT /note="E -> G (in dbSNP:rs1047406)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050468"
SQ SEQUENCE 227 AA; 25733 MW; 0F6BD35F5EE63EC4 CRC64;
MGWTMRLVTA ALLLGLMMVV TGDEDENSPC AHEALLDEDT LFCQGLEVFY PELGNIGCKV
VPDCNNYRQK ITSWMEPIVK FPGAVDGATY ILVMVDPDAP SRAEPRQRFW RHWLVTDIKG
ADLKKGKIQG QELSAYQAPS PPAHSGFHRY QFFVYLQEGK VISLLPKENK TRGSWKMDRF
LNRFHLGEPE ASTQFMTQNY QDSPTLQAPR ERASEPKHKN QAEIAAC
