ID L2GL2_HUMAN Reviewed; 1020 AA. AC Q6P1M3; Q14521; Q9BR62; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 171. DE RecName: Full=LLGL scribble cell polarity complex component 2; DE AltName: Full=HGL; DE AltName: Full=Lethal(2) giant larvae protein homolog 2; GN Name=LLGL2; 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 C), AND VARIANT HIS-45. RA Wiemann S., Tommerup N., Celis J.E., Ansorge W., Leffers H.; RT "A human homolog of the Drosophila 1(2) giant larvae tumor suppressor maps RT to 17q24-25."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B), AND VARIANTS RP LEU-479 AND SER-759. RC TISSUE=Lung, and 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 [4] RP INTERACTION WITH GPSM2/LGN, SUBCELLULAR LOCATION, AND FUNCTION. RC TISSUE=Brain; RX PubMed=15632202; DOI=10.1074/jbc.c400440200; RA Yasumi M., Sakisaka T., Hoshino T., Kimura T., Sakamoto Y., Yamanaka T., RA Ohno S., Takai Y.; RT "Direct binding of Lgl2 to LGN during mitosis and its requirement for RT normal cell division."; RL J. Biol. Chem. 280:6761-6765(2005). RN [5] RP INTERACTION WITH PARD6B/PAR-6 AND PRKCI/APKC, PHOSPHORYLATION AT SER-653, RP AND MUTAGENESIS OF SER-641; SER-645; SER-649; SER-653; SER-660 AND SER-663. RX PubMed=12725730; DOI=10.1016/s0960-9822(03)00244-6; RA Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A., Hirose T., RA Iwamatsu A., Shinohara A., Ohno S.; RT "Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of RT PAR-3 to regulate epithelial cell polarity."; RL Curr. Biol. 13:734-743(2003). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP INTERACTION WITH DCAF1. RX PubMed=20644714; DOI=10.1371/journal.pbio.1000422; RA Tamori Y., Bialucha C.U., Tian A.G., Kajita M., Huang Y.C., Norman M., RA Harrison N., Poulton J., Ivanovitch K., Disch L., Liu T., Deng W.M., RA Fujita Y.; RT "Involvement of Lgl and Mahjong/VprBP in cell competition."; RL PLoS Biol. 8:E1000422-E1000422(2010). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP IDENTIFICATION BY 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). CC -!- FUNCTION: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par- CC 6, which may ensure the correct organization and orientation of bipolar CC spindles for normal cell division. This complex plays roles in the CC initial phase of the establishment of epithelial cell polarity. CC {ECO:0000269|PubMed:15632202}. CC -!- SUBUNIT: Interacts with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6. The CC complex is enhanced during mitosis. Interacts with DCAF1. CC {ECO:0000269|PubMed:12725730, ECO:0000269|PubMed:15632202, CC ECO:0000269|PubMed:20644714}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15632202}. CC Note=Localized in the perinuclear structure and faintly at the cell- CC cell contacts sites in the interphase. Localized at the cell periphery CC during metaphase. Cortical localization in mitotic cells. Found in the CC lateral region of polarized epithelial cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=C; CC IsoId=Q6P1M3-1; Sequence=Displayed; CC Name=A; CC IsoId=Q6P1M3-2; Sequence=VSP_017946; CC Name=B; CC IsoId=Q6P1M3-3; Sequence=VSP_047387, VSP_047388; CC -!- PTM: Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced CC during cell polarization induced by calcium. Phosphorylation may occur CC during the cell-cell contact-induced cell polarization and may CC contribute to the segregation of LLGL2 from the PRKCI/aPKC and CC PARD6B/Par-6 complex. {ECO:0000269|PubMed:12725730}. CC -!- MISCELLANEOUS: Overexpression of LLGL2 inhibits the tight junction CC formation. CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}. 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; X87342; CAA60780.1; -; mRNA. DR EMBL; AC100787; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006503; AAH06503.1; -; mRNA. DR EMBL; BC010879; AAH10879.1; -; mRNA. DR EMBL; BC064994; AAH64994.1; -; mRNA. DR CCDS; CCDS11725.1; -. [Q6P1M3-2] DR CCDS; CCDS32733.1; -. [Q6P1M3-1] DR CCDS; CCDS45776.1; -. [Q6P1M3-3] DR PIR; S55474; S55474. DR RefSeq; NP_001015002.1; NM_001015002.1. [Q6P1M3-3] DR RefSeq; NP_001026973.1; NM_001031803.1. [Q6P1M3-1] DR RefSeq; NP_004515.2; NM_004524.2. [Q6P1M3-2] DR RefSeq; XP_016880115.1; XM_017024626.1. [Q6P1M3-1] DR RefSeq; XP_016880119.1; XM_017024630.1. DR PDB; 3WP0; X-ray; 2.04 A; B=640-654. DR PDB; 3WP1; X-ray; 2.80 A; A=646-657. DR PDB; 6N8P; X-ray; 3.19 A; A=12-978. DR PDB; 6N8Q; X-ray; 2.20 A; A=12-978. DR PDB; 6N8R; X-ray; 1.91 A; A=12-978. DR PDB; 6N8S; X-ray; 3.90 A; A/D=12-978. DR PDBsum; 3WP0; -. DR PDBsum; 3WP1; -. DR PDBsum; 6N8P; -. DR PDBsum; 6N8Q; -. DR PDBsum; 6N8R; -. DR PDBsum; 6N8S; -. DR AlphaFoldDB; Q6P1M3; -. DR SMR; Q6P1M3; -. DR BioGRID; 110181; 137. DR ComplexPortal; CPX-6168; Scribble cell polarity complex, DLG1-LLGL2-SCRIB variant. DR ComplexPortal; CPX-6184; Scribble cell polarity complex, DLG2-LLGL2-SCRIB variant. DR ComplexPortal; CPX-6185; Scribble cell polarity complex, DLG3-LLGL2-SCRIB variant. DR ComplexPortal; CPX-6186; Scribble cell polarity complex, DLG4-LLGL2-SCRIB variant. DR ComplexPortal; CPX-6187; Scribble cell polarity complex, DLG5-LLGL2-SCRIB variant. DR CORUM; Q6P1M3; -. DR IntAct; Q6P1M3; 93. DR STRING; 9606.ENSP00000376333; -. DR GlyGen; Q6P1M3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6P1M3; -. DR PhosphoSitePlus; Q6P1M3; -. DR BioMuta; LLGL2; -. DR DMDM; 93204600; -. DR EPD; Q6P1M3; -. DR jPOST; Q6P1M3; -. DR MassIVE; Q6P1M3; -. DR MaxQB; Q6P1M3; -. DR PaxDb; 9606-ENSP00000376333; -. DR PeptideAtlas; Q6P1M3; -. DR ProteomicsDB; 66850; -. [Q6P1M3-1] DR ProteomicsDB; 66851; -. [Q6P1M3-2] DR ProteomicsDB; 66852; -. [Q6P1M3-3] DR Pumba; Q6P1M3; -. DR Antibodypedia; 19581; 231 antibodies from 27 providers. DR DNASU; 3993; -. DR Ensembl; ENST00000167462.9; ENSP00000167462.5; ENSG00000073350.14. [Q6P1M3-2] DR Ensembl; ENST00000375227.8; ENSP00000364375.4; ENSG00000073350.14. [Q6P1M3-3] DR Ensembl; ENST00000392550.8; ENSP00000376333.4; ENSG00000073350.14. [Q6P1M3-1] DR Ensembl; ENST00000578363.5; ENSP00000464603.1; ENSG00000073350.14. [Q6P1M3-3] DR GeneID; 3993; -. DR KEGG; hsa:3993; -. DR MANE-Select; ENST00000392550.8; ENSP00000376333.4; NM_001031803.2; NP_001026973.1. DR UCSC; uc002jog.2; human. [Q6P1M3-1] DR AGR; HGNC:6629; -. DR CTD; 3993; -. DR DisGeNET; 3993; -. DR GeneCards; LLGL2; -. DR HGNC; HGNC:6629; LLGL2. DR HPA; ENSG00000073350; Low tissue specificity. DR MIM; 618483; gene. DR neXtProt; NX_Q6P1M3; -. DR OpenTargets; ENSG00000073350; -. DR PharmGKB; PA30397; -. DR VEuPathDB; HostDB:ENSG00000073350; -. DR eggNOG; KOG1983; Eukaryota. DR GeneTree; ENSGT00950000182906; -. DR HOGENOM; CLU_046862_0_0_1; -. DR InParanoid; Q6P1M3; -. DR OMA; TKNHSRP; -. DR OrthoDB; 415950at2759; -. DR PhylomeDB; Q6P1M3; -. DR TreeFam; TF314585; -. DR PathwayCommons; Q6P1M3; -. DR SignaLink; Q6P1M3; -. DR SIGNOR; Q6P1M3; -. DR BioGRID-ORCS; 3993; 14 hits in 1155 CRISPR screens. DR ChiTaRS; LLGL2; human. DR GenomeRNAi; 3993; -. DR Pharos; Q6P1M3; Tbio. DR PRO; PR:Q6P1M3; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6P1M3; Protein. DR Bgee; ENSG00000073350; Expressed in mucosa of transverse colon and 157 other cell types or tissues. DR ExpressionAtlas; Q6P1M3; baseline and differential. DR GO; GO:0005912; C:adherens junction; NAS:ComplexPortal. DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central. DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0051294; P:establishment of spindle orientation; IBA:GO_Central. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:ComplexPortal. DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW. DR GO; GO:0015820; P:leucine transport; IMP:UniProtKB. DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IDA:UniProtKB. DR GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central. DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central. DR DisProt; DP02730; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR000664; Lethal2_giant. DR InterPro; IPR013577; LLGL2. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR10241; LETHAL 2 GIANT LARVAE PROTEIN; 1. DR PANTHER; PTHR10241:SF20; LLGL SCRIBBLE CELL POLARITY COMPLEX COMPONENT 2; 1. DR Pfam; PF08366; LLGL; 1. DR Pfam; PF00400; WD40; 1. DR PRINTS; PR00962; LETHAL2GIANT. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR Genevisible; Q6P1M3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm; KW Exocytosis; Phosphoprotein; Reference proteome; Repeat; WD repeat. FT CHAIN 1..1020 FT /note="LLGL scribble cell polarity complex component 2" FT /id="PRO_0000232728" FT REPEAT 36..69 FT /note="WD 1" FT REPEAT 76..117 FT /note="WD 2" FT REPEAT 132..169 FT /note="WD 3" FT REPEAT 193..227 FT /note="WD 4" FT REPEAT 233..268 FT /note="WD 5" FT REPEAT 282..324 FT /note="WD 6" FT REPEAT 332..366 FT /note="WD 7" FT REPEAT 388..464 FT /note="WD 8" FT REPEAT 508..583 FT /note="WD 9" FT REPEAT 592..653 FT /note="WD 10" FT REPEAT 713..769 FT /note="WD 11" FT REPEAT 778..830 FT /note="WD 12" FT REPEAT 835..888 FT /note="WD 13" FT REPEAT 902..925 FT /note="WD 14" FT REGION 653..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 938..975 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 992..1020 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 653 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12725730" FT MOD_RES 965 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1015 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 346..356 FT /note="TFDDPYALVVL -> SRRASGVGAQG (in isoform B)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047387" FT VAR_SEQ 357..1020 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047388" FT VAR_SEQ 986..1020 FT /note="VLKEIQSTLEGDRGSGNWRSHRAAVGCSLSNGGAE -> AATGVHIEPPWGA FT ASAMAEQSEWLSVQAAR (in isoform A)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017946" FT VARIANT 45 FT /note="R -> H (in dbSNP:rs1671036)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_050069" FT VARIANT 479 FT /note="F -> L (in dbSNP:rs1671021)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_050070" FT VARIANT 488 FT /note="P -> L (in dbSNP:rs35991442)" FT /id="VAR_050071" FT VARIANT 490 FT /note="L -> P (in dbSNP:rs1671021)" FT /id="VAR_050072" FT VARIANT 748 FT /note="R -> H (in dbSNP:rs35474687)" FT /id="VAR_034058" FT VARIANT 759 FT /note="P -> S (in dbSNP:rs1661715)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_050073" FT VARIANT 790 FT /note="P -> L (in dbSNP:rs1661714)" FT /id="VAR_050075" FT VARIANT 1001 FT /note="G -> S (in dbSNP:rs35886912)" FT /id="VAR_034059" FT MUTAGEN 641 FT /note="S->A: No effect on phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT MUTAGEN 645 FT /note="S->A: Decrease of phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT MUTAGEN 649 FT /note="S->A: Decrease of phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT MUTAGEN 653 FT /note="S->A: Loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT MUTAGEN 660 FT /note="S->A: Decrease of phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT MUTAGEN 663 FT /note="S->A: No effect on phosphorylation." FT /evidence="ECO:0000269|PubMed:12725730" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 21..30 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 33..41 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 83..92 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 95..105 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 108..118 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 158..161 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 171..176 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 200..208 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 222..228 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 233..238 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 242..249 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:6N8P" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 297..302 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 306..309 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 313..319 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 322..330 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 332..340 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 350..359 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 361..368 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 387..393 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 398..411 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 437..442 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 445..451 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 453..456 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 458..464 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 503..505 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 507..512 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 514..516 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 518..523 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 526..536 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 538..541 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 543..548 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 549..552 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 569..573 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 575..587 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 598..601 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 608..615 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 616..619 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 620..626 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 645..649 FT /evidence="ECO:0007829|PDB:3WP0" FT HELIX 652..656 FT /evidence="ECO:0007829|PDB:3WP1" FT STRAND 713..721 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 723..727 FT /evidence="ECO:0007829|PDB:6N8P" FT STRAND 730..737 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 740..748 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 753..755 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 761..769 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 776..782 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 794..797 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 799..801 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 810..823 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 824..827 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 828..834 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 835..839 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 843..852 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 854..856 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 860..868 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 873..877 FT /evidence="ECO:0007829|PDB:6N8R" FT TURN 878..880 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 883..887 FT /evidence="ECO:0007829|PDB:6N8R" FT HELIX 895..900 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 907..914 FT /evidence="ECO:0007829|PDB:6N8R" FT STRAND 917..924 FT /evidence="ECO:0007829|PDB:6N8R" SQ SEQUENCE 1020 AA; 113448 MW; 9C36BFF9F94314B5 CRC64; MRRFLRPGHD PVRERLKRDL FQFNKTVEHG FPHQPSALGY SPSLRILAIG TRSGAIKLYG APGVEFMGLH QENNAVTQIH LLPGQCQLVT LLDDNSLHLW SLKVKGGASE LQEDESFTLR GPPGAAPSAT QITVVLPHSS CELLYLGTES GNVFVVQLPA FRALEDRTIS SDAVLQRLPE EARHRRVFEM VEALQEHPRD PNQILIGYSR GLVVIWDLQG SRVLYHFLSS QQLENIWWQR DGRLLVSCHS DGSYCQWPVS SEAQQPEPLR SLVPYGPFPC KAITRILWLT TRQGLPFTIF QGGMPRASYG DRHCISVIHD GQQTAFDFTS RVIGFTVLTE ADPAATFDDP YALVVLAEEE LVVIDLQTAG WPPVQLPYLA SLHCSAITCS HHVSNIPLKL WERIIAAGSR QNAHFSTMEW PIDGGTSLTP APPQRDLLLT GHEDGTVRFW DASGVCLRLL YKLSTVRVFL TDTDPNENFS AQGEDEWPPL RKVGSFDPYS DDPRLGIQKI FLCKYSGYLA VAGTAGQVLV LELNDEAAEQ AVEQVEADLL QDQEGYRWKG HERLAARSGP VRFEPGFQPF VLVQCQPPAV VTSLALHSEW RLVAFGTSHG FGLFDHQQRR QVFVKCTLHP SDQLALEGPL SRVKSLKKSL RQSFRRMRRS RVSSRKRHPA GPPGEAQEGS AKAERPGLQN MELAPVQRKI EARSAEDSFT GFVRTLYFAD TYLKDSSRHC PSLWAGTNGG TIYAFSLRVP PAERRMDEPV RAEQAKEIQL MHRAPVVGIL VLDGHSVPLP EPLEVAHDLS KSPDMQGSHQ LLVVSEEQFK VFTLPKVSAK LKLKLTALEG SRVRRVSVAH FGSRRAEDYG EHHLAVLTNL GDIQVVSLPL LKPQVRYSCI RREDVSGIAS CVFTKYGQGF YLISPSEFER FSLSTKWLVE PRCLVDSAET KNHRPGNGAG PKKAPSRARN SGTQSDGEEK QPGLVMERAL LSDERVLKEI QSTLEGDRGS GNWRSHRAAV GCSLSNGGAE //