PLCB2_HUMAN
ID PLCB2_HUMAN Reviewed; 1185 AA.
AC Q00722; A8K6J2; B9EGH5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:9188725};
DE AltName: Full=Phosphoinositide phospholipase C-beta-2;
DE AltName: Full=Phospholipase C-beta-2;
DE Short=PLC-beta-2;
GN Name=PLCB2 {ECO:0000312|HGNC:HGNC:9055};
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] (ISOFORM 2), INTERACTION WITH RAC1, AND
RP CATALYTIC ACTIVITY.
RX PubMed=1644792; DOI=10.1016/s0021-9258(18)41963-1;
RA Park D., Jhon D.-Y., Kriz R., Knopf J., Rhee S.G.;
RT "Cloning, sequencing, expression, and Gq-independent activation of
RT phospholipase C-beta 2.";
RL J. Biol. Chem. 267:16048-16055(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-1095.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9188725; DOI=10.1021/bi9702288;
RA Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A.,
RA Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.;
RT "Phosphoinositide binding specificity among phospholipase C isozymes as
RT determined by photo-cross-linking to novel substrate and product analogs.";
RL Biochemistry 36:7239-7248(1997).
RN [6]
RP INTERACTION WITH WDR26 AND A G-BETA:GAMMA UNIT.
RX PubMed=23625927; DOI=10.1074/jbc.m113.462564;
RA Sun Z., Smrcka A.V., Chen S.;
RT "WDR26 functions as a scaffolding protein to promote Gbetagamma-mediated
RT phospholipase C beta2 (PLCbeta2) activation in leukocytes.";
RL J. Biol. Chem. 288:16715-16725(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-803 (ISOFORM 2) IN COMPLEX WITH
RP RAC1, AND MUTAGENESIS OF GLN-52.
RX PubMed=17115053; DOI=10.1038/nsmb1175;
RA Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K.,
RA Sondek J.;
RT "Crystal structure of Rac1 bound to its effector phospholipase C-beta2.";
RL Nat. Struct. Mol. Biol. 13:1135-1140(2006).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000269|PubMed:1644792, ECO:0000269|PubMed:9188725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000269|PubMed:9188725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:9188725};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000269|PubMed:1644792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000305|PubMed:1644792};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts with RAC1 (PubMed:1644792). Forms a complex composed
CC of at least WDR26, a G-beta:gamma unit, and PLCB2 (PubMed:23625927).
CC {ECO:0000269|PubMed:1644792, ECO:0000269|PubMed:23625927}.
CC -!- INTERACTION:
CC Q00722; Q9UBT7: CTNNAL1; NbExp=3; IntAct=EBI-968381, EBI-514206;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00722-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00722-2; Sequence=VSP_035770;
CC Name=3;
CC IsoId=Q00722-3; Sequence=VSP_054490;
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-2 is most
CC effectively mediated by one G-protein alpha subunit, alpha-16.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLCB2ID41743ch15q15.html";
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DR EMBL; M95678; AAA36453.1; -; mRNA.
DR EMBL; AK291657; BAF84346.1; -; mRNA.
DR EMBL; AC020658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136467; AAI36468.1; -; mRNA.
DR CCDS; CCDS42020.1; -. [Q00722-1]
DR CCDS; CCDS61591.1; -. [Q00722-3]
DR CCDS; CCDS61592.1; -. [Q00722-2]
DR PIR; A43346; A43346.
DR RefSeq; NP_001271226.1; NM_001284297.1. [Q00722-2]
DR RefSeq; NP_001271227.1; NM_001284298.1. [Q00722-3]
DR RefSeq; NP_004564.2; NM_004573.2. [Q00722-1]
DR PDB; 2FJU; X-ray; 2.20 A; B=1-803.
DR PDB; 2ZKM; X-ray; 1.62 A; X=1-803.
DR PDBsum; 2FJU; -.
DR PDBsum; 2ZKM; -.
DR AlphaFoldDB; Q00722; -.
DR SMR; Q00722; -.
DR BioGRID; 111346; 16.
DR DIP; DIP-29259N; -.
DR IntAct; Q00722; 4.
DR STRING; 9606.ENSP00000260402; -.
DR SwissLipids; SLP:000000948; -.
DR iPTMnet; Q00722; -.
DR MetOSite; Q00722; -.
DR PhosphoSitePlus; Q00722; -.
DR BioMuta; PLCB2; -.
DR DMDM; 215273902; -.
DR EPD; Q00722; -.
DR jPOST; Q00722; -.
DR MassIVE; Q00722; -.
DR MaxQB; Q00722; -.
DR PaxDb; Q00722; -.
DR PeptideAtlas; Q00722; -.
DR PRIDE; Q00722; -.
DR ProteomicsDB; 57870; -. [Q00722-1]
DR ProteomicsDB; 57871; -. [Q00722-2]
DR ProteomicsDB; 7525; -.
DR Antibodypedia; 4002; 183 antibodies from 28 providers.
DR DNASU; 5330; -.
DR Ensembl; ENST00000260402.8; ENSP00000260402.3; ENSG00000137841.12. [Q00722-1]
DR Ensembl; ENST00000456256.6; ENSP00000411991.2; ENSG00000137841.12. [Q00722-3]
DR Ensembl; ENST00000557821.5; ENSP00000453975.1; ENSG00000137841.12. [Q00722-2]
DR GeneID; 5330; -.
DR KEGG; hsa:5330; -.
DR MANE-Select; ENST00000260402.8; ENSP00000260402.3; NM_004573.3; NP_004564.2.
DR UCSC; uc001zld.4; human. [Q00722-1]
DR CTD; 5330; -.
DR DisGeNET; 5330; -.
DR GeneCards; PLCB2; -.
DR HGNC; HGNC:9055; PLCB2.
DR HPA; ENSG00000137841; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 604114; gene.
DR neXtProt; NX_Q00722; -.
DR OpenTargets; ENSG00000137841; -.
DR PharmGKB; PA33385; -.
DR VEuPathDB; HostDB:ENSG00000137841; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000159326; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR InParanoid; Q00722; -.
DR OMA; NMALFEY; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q00722; -.
DR TreeFam; TF313216; -.
DR BioCyc; MetaCyc:HS06408-MON; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; Q00722; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SABIO-RK; Q00722; -.
DR SignaLink; Q00722; -.
DR SIGNOR; Q00722; -.
DR BioGRID-ORCS; 5330; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; PLCB2; human.
DR EvolutionaryTrace; Q00722; -.
DR GeneWiki; PLCB2; -.
DR GenomeRNAi; 5330; -.
DR Pharos; Q00722; Tbio.
DR PRO; PR:Q00722; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q00722; protein.
DR Bgee; ENSG00000137841; Expressed in granulocyte and 114 other tissues.
DR ExpressionAtlas; Q00722; baseline and differential.
DR Genevisible; Q00722; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; TAS:Reactome.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:ProtInc.
DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR028403; PLC-beta2.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF10; PTHR10336:SF10; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein;
KW Reference proteome; Transducer.
FT CHAIN 1..1185
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-2"
FT /id="PRO_0000088489"
FT DOMAIN 312..463
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 546..662
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 662..790
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 460..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 988..1147
FT /evidence="ECO:0000255"
FT COMPBIAS 464..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 492..495
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1644792"
FT /id="VSP_035770"
FT VAR_SEQ 868..882
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054490"
FT VARIANT 324
FT /note="N -> I (in dbSNP:rs45628633)"
FT /id="VAR_047509"
FT VARIANT 598
FT /note="R -> H (in dbSNP:rs8025153)"
FT /id="VAR_047510"
FT VARIANT 664
FT /note="P -> L (in dbSNP:rs9972332)"
FT /id="VAR_047511"
FT VARIANT 712
FT /note="G -> R (in dbSNP:rs28395835)"
FT /id="VAR_047512"
FT VARIANT 1095
FT /note="E -> G (in dbSNP:rs936212)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_047513"
FT MUTAGEN 52
FT /note="Q->A: Strongly reduces interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:17115053"
FT CONFLICT 119
FT /note="K -> R (in Ref. 2; BAF84346)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="K -> R (in Ref. 2; BAF84346)"
FT /evidence="ECO:0000305"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:2FJU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2FJU"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:2FJU"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:2FJU"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 414..428
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 451..456
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 561..567
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 572..577
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 618..622
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 637..645
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 675..680
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 682..693
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 701..708
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 738..745
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 750..757
FT /evidence="ECO:0007829|PDB:2ZKM"
FT TURN 758..760
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 761..769
FT /evidence="ECO:0007829|PDB:2ZKM"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 776..783
FT /evidence="ECO:0007829|PDB:2ZKM"
FT STRAND 789..802
FT /evidence="ECO:0007829|PDB:2ZKM"
SQ SEQUENCE 1185 AA; 134024 MW; A0397309D943672A CRC64;
MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT YQSKEMEFLD
ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE
NVGKAWAEDV LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR
VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH
LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN
SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC
WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM
AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSGP TSSSKDTGGE
AEGSSPPSAP AGEGTVWAGE EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV
TAYEEMSSLV NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM
SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG QSGYLLKHEF
MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR TYVEVELFGL PGDPKRRYRT
KLSPSTNSIN PVWKEEPFVF EKILMPELAS LRVAVMEEGN KFLGHRIIPI NALNSGYHHL
CLHSESNMPL TMPALFIFLE MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL
PEKPFPLASP VASQVNGALA PTSNGSPAAR AGAREEAMKE AAEPRTASLE ELRELKGVVK
LQRRHEKELR ELERRGARRW EELLQRGAAQ LAELGPPGVG GVGACKLGPG KGSRKKRSLP
REESAGAAPG EGPEGVDGRV RELKDRLELE LLRQGEEQYE CVLKRKEQHV AEQISKMMEL
AREKQAAELK ALKETSENDT KEMKKKLETK RLERIQGMTK VTTDKMAQER LKREINNSHI
QEVVQVIKQM TENLERHQEK LEEKQAACLE QIREMEKQFQ KEALAEYEAR MKGLEAEVKE
SVRACLRTCF PSEAKDKPER ACECPPELCE QDPLIAKADA QESRL
