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 27-MAR-2024, entry version 210. 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="https://atlasgeneticsoncology.org/gene/41743/PLCB2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 19. 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; 9606-ENSP00000260402; -. DR PeptideAtlas; Q00722; -. DR ProteomicsDB; 57870; -. [Q00722-1] DR ProteomicsDB; 57871; -. [Q00722-2] DR ProteomicsDB; 7525; -. DR Pumba; Q00722; -. DR Antibodypedia; 4002; 230 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 AGR; HGNC:9055; -. 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; RLAKCQD; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q00722; -. DR TreeFam; TF313216; -. DR BioCyc; MetaCyc:HS06408-MONOMER; -. 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 1160 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 116 other cell types or tissues. DR ExpressionAtlas; Q00722; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IEA:Ensembl. DR GO; GO:0098992; C:neuronal dense core vesicle; 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 GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd16209; EFh_PI-PLCbeta2; 1. DR CDD; cd13361; PH_PLC_beta; 1. DR CDD; cd08624; PI-PLCc_beta2; 1. DR Gene3D; 2.30.29.240; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1. DR Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 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_cat. 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; IPR046969; PLCbeta2_EF. DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom. DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y. DR PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-2; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; SSF69989; C-terminal domain of PLC-beta; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. DR Genevisible; Q00722; HS. 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 //