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PLEK2_MOUSE
ID   PLEK2_MOUSE             Reviewed;         353 AA.
AC   Q9WV52;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Pleckstrin-2;
GN   Name=Plek2;
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].
RX   PubMed=10419454; DOI=10.1074/jbc.274.31.21515;
RA   Hu M., Bauman E.M., Roll R.L., Yeilding N., Abrams C.S.;
RT   "Pleckstrin 2, a widely expressed paralog of pleckstrin involved in actin
RT   rearrangement.";
RL   J. Biol. Chem. 274:21515-21518(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10548495; DOI=10.1006/bbrc.1999.1461;
RA   Inazu T., Yamada K., Miyamoto K.;
RT   "Cloning and expression of pleckstrin 2, a novel member of the pleckstrin
RT   family.";
RL   Biochem. Biophys. Res. Commun. 265:87-93(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   STRUCTURE BY NMR OF 129-235.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the DEP domain of mouse pleckstrin2.";
RL   Submitted (APR-2004) to the PDB data bank.
CC   -!- FUNCTION: May help orchestrate cytoskeletal arrangement. Contribute to
CC       lamellipodia formation. Overexpression of pleckstrin 2 causes large
CC       lamellipodia and peripheral ruffle formation.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium membrane;
CC       Peripheral membrane protein. Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in the thymus, large
CC       bowel, small bowel, stomach, and prostate.
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DR   EMBL; AF157600; AAD42973.1; -; mRNA.
DR   EMBL; AF170564; AAD46924.1; -; mRNA.
DR   EMBL; BC028902; AAH28902.1; -; mRNA.
DR   CCDS; CCDS26004.1; -.
DR   PIR; JC7128; JC7128.
DR   RefSeq; NP_038766.1; NM_013738.3.
DR   PDB; 1V3F; NMR; -; A=129-235.
DR   PDBsum; 1V3F; -.
DR   AlphaFoldDB; Q9WV52; -.
DR   SMR; Q9WV52; -.
DR   STRING; 10090.ENSMUSP00000021544; -.
DR   iPTMnet; Q9WV52; -.
DR   PhosphoSitePlus; Q9WV52; -.
DR   MaxQB; Q9WV52; -.
DR   PaxDb; Q9WV52; -.
DR   PeptideAtlas; Q9WV52; -.
DR   PRIDE; Q9WV52; -.
DR   ProteomicsDB; 288250; -.
DR   Antibodypedia; 96; 86 antibodies from 19 providers.
DR   DNASU; 27260; -.
DR   Ensembl; ENSMUST00000021544; ENSMUSP00000021544; ENSMUSG00000021118.
DR   GeneID; 27260; -.
DR   KEGG; mmu:27260; -.
DR   UCSC; uc007nzl.2; mouse.
DR   CTD; 26499; -.
DR   MGI; MGI:1351466; Plek2.
DR   VEuPathDB; HostDB:ENSMUSG00000021118; -.
DR   eggNOG; ENOG502QYJ8; Eukaryota.
DR   GeneTree; ENSGT00940000157229; -.
DR   HOGENOM; CLU_067828_0_0_1; -.
DR   InParanoid; Q9WV52; -.
DR   OMA; ITKNDIH; -.
DR   OrthoDB; 717547at2759; -.
DR   PhylomeDB; Q9WV52; -.
DR   TreeFam; TF332246; -.
DR   BioGRID-ORCS; 27260; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Plek2; mouse.
DR   EvolutionaryTrace; Q9WV52; -.
DR   PRO; PR:Q9WV52; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9WV52; protein.
DR   Bgee; ENSMUSG00000021118; Expressed in dorsal pancreas and 121 other tissues.
DR   Genevisible; Q9WV52; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:MGI.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:MGI.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0031346; P:positive regulation of cell projection organization; IMP:MGI.
DR   GO; GO:0120034; P:positive regulation of plasma membrane bounded cell projection assembly; IDA:MGI.
DR   CDD; cd04444; DEP_PLEK2; 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; IPR037369; PLEK2_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; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..353
FT                   /note="Pleckstrin-2"
FT                   /id="PRO_0000053863"
FT   DOMAIN          4..104
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          139..225
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   DOMAIN          247..353
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYT0"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYT0"
FT   HELIX           129..136
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   HELIX           177..190
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:1V3F"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:1V3F"
SQ   SEQUENCE   353 AA;  40018 MW;  4593DC41B62E9A5A CRC64;
     MEDGVLKEGF LVKRGHIVHN WKARWFILRQ NTLLYYKLEG GRRVTPPKGR IVLDGCTITC
     PCLEYENRPL LIKLKTRTST EYFLEACSRE ERDSWAFEIT GAIHAGQPGK IQQLHILKNS
     FKLPPHISLH RIVDKMHDTS TGIRPSPNME QGSTYKKTFL GSSLVDWLIS SNFAASRLEA
     VTLASMLMEE NFLRPVGVRS MGAIRSGDLA EQFLDDSTAL YTFAESYKKK VSSKEEISLS
     TMELSGTVVK QGYLSKQGHK RKNWKVRRFV LRKDPAFLHY YDPSKEENRP VGGFSLRGSL
     VSALEDNGVP TGVKGNVQGN LFKVITKDDT HYYIQASSKA ERAEWIEAIK KLT
 
 
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