PLEK_MOUSE
ID PLEK_MOUSE Reviewed; 350 AA.
AC Q9JHK5; Q9ERI9;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pleckstrin;
GN Name=Plek;
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].
RC STRAIN=BALB/cJ;
RX PubMed=10860665; DOI=10.1006/geno.2000.6210;
RA Cmarik J.L., Hegamyer G., Gerrard B., Dean M., Colburn N.H.;
RT "cDNA cloning and mapping of mouse pleckstrin (Plek), a gene upregulated in
RT transformation-resistant cells.";
RL Genomics 66:204-212(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang Y., Wu G., Paige C.J.;
RT "Involvement of pleckstrin in B cell differentiation and activation.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ahn H.-J., Cho J.-J.;
RT "Mouse pleckstrin 1 is induced in mast cells after IgE cross-linking.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, 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).
RN [6]
RP STRUCTURE BY NMR OF 126-223.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the DEP domain of mouse pleckstrin.";
RL Submitted (JAN-2004) to the PDB data bank.
CC -!- FUNCTION: Major protein kinase C substrate of platelets.
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DR EMBL; AF181829; AAF75830.1; -; mRNA.
DR EMBL; AF073294; AAF72039.1; -; mRNA.
DR EMBL; AF303745; AAG29513.1; -; mRNA.
DR EMBL; BC066185; AAH66185.1; -; mRNA.
DR CCDS; CCDS24446.1; -.
DR RefSeq; NP_062422.1; NM_019549.2.
DR PDB; 1UHW; NMR; -; A=126-221.
DR PDBsum; 1UHW; -.
DR AlphaFoldDB; Q9JHK5; -.
DR SMR; Q9JHK5; -.
DR BioGRID; 207832; 7.
DR STRING; 10090.ENSMUSP00000099945; -.
DR iPTMnet; Q9JHK5; -.
DR PhosphoSitePlus; Q9JHK5; -.
DR SwissPalm; Q9JHK5; -.
DR EPD; Q9JHK5; -.
DR MaxQB; Q9JHK5; -.
DR PaxDb; Q9JHK5; -.
DR PRIDE; Q9JHK5; -.
DR ProteomicsDB; 288251; -.
DR Antibodypedia; 30933; 476 antibodies from 37 providers.
DR DNASU; 56193; -.
DR Ensembl; ENSMUST00000102881; ENSMUSP00000099945; ENSMUSG00000020120.
DR GeneID; 56193; -.
DR KEGG; mmu:56193; -.
DR UCSC; uc007ibv.2; mouse.
DR CTD; 5341; -.
DR MGI; MGI:1860485; Plek.
DR VEuPathDB; HostDB:ENSMUSG00000020120; -.
DR eggNOG; ENOG502QQIA; Eukaryota.
DR GeneTree; ENSGT00940000157885; -.
DR HOGENOM; CLU_067828_0_0_1; -.
DR InParanoid; Q9JHK5; -.
DR OMA; MEPKQIR; -.
DR OrthoDB; 717547at2759; -.
DR PhylomeDB; Q9JHK5; -.
DR TreeFam; TF332246; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 56193; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Plek; mouse.
DR EvolutionaryTrace; Q9JHK5; -.
DR PRO; PR:Q9JHK5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JHK5; protein.
DR Bgee; ENSMUSG00000020120; Expressed in blood and 226 other tissues.
DR ExpressionAtlas; Q9JHK5; baseline and differential.
DR Genevisible; Q9JHK5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; ISO:MGI.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0010920; P:negative regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
DR GO; GO:0030845; P:phospholipase C-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:BHF-UCL.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:BHF-UCL.
DR GO; GO:0010925; P:positive regulation of inositol-polyphosphate 5-phosphatase activity; ISO:MGI.
DR GO; GO:0033625; P:positive regulation of integrin activation; IMP:BHF-UCL.
DR GO; GO:0010572; P:positive regulation of platelet activation; IMP:BHF-UCL.
DR GO; GO:0070528; P:protein kinase C signaling; IMP:BHF-UCL.
DR GO; GO:0070560; P:protein secretion by platelet; IMP:BHF-UCL.
DR GO; GO:0060305; P:regulation of cell diameter; ISO:MGI.
DR GO; GO:0031529; P:ruffle organization; ISO:MGI.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:BHF-UCL.
DR CDD; cd04445; DEP_PLEK1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037371; PLEK_DEP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..350
FT /note="Pleckstrin"
FT /id="PRO_0000053860"
FT DOMAIN 4..101
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 136..221
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 244..347
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08567"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08567"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 120
FT /note="L -> Q (in Ref. 3; AAG29513)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> L (in Ref. 3; AAG29513)"
FT /evidence="ECO:0000305"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1UHW"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1UHW"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1UHW"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1UHW"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:1UHW"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1UHW"
SQ SEQUENCE 350 AA; 39901 MW; 348F3CB469B7CC53 CRC64;
MEPKRIREGY LVKKGSVFNT WKPMWVVLLE DGIEFYKKKS DNSPKGMIPL KGSTLTSPCQ
DFGKRMFVLK ITTTKQQDHF FQAAFLEERD AWVRDIKKAI KCIEGGQKFA RKSTRRSIRL
PETIDLGALY LSMKDPEKGI KELNLEKDKK VFNHCLTGSG VIDWLVSNKL VRNRQEGLMI
SASLLSEGYL QPAGDLSKNA ADGIAENPFL DSPDAFYYFP DSGFFCEENS SDDDVILREE
FRGVIIKQGC LLKQGHRRKN WKVRKFILRE DPAYLHYYDP AGGEDPLGAV HLRGCVVTSV
ESSHDVKKSD EENLFEIITA DEVHYYLQAA TSKERTEWIK AIQVASRTGK
