L2GL2_HUMAN
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 03-AUG-2022, entry version 162.
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}.
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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. [Q6P1M3-2]
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; 124.
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; Q6P1M3; -.
DR PeptideAtlas; Q6P1M3; -.
DR PRIDE; Q6P1M3; -.
DR ProteomicsDB; 66850; -. [Q6P1M3-1]
DR ProteomicsDB; 66851; -. [Q6P1M3-2]
DR ProteomicsDB; 66852; -. [Q6P1M3-3]
DR Antibodypedia; 19581; 211 antibodies from 26 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 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; QWPVSGD; -.
DR OrthoDB; 122541at2759; -.
DR PhylomeDB; Q6P1M3; -.
DR TreeFam; TF314585; -.
DR PathwayCommons; Q6P1M3; -.
DR SignaLink; Q6P1M3; -.
DR SIGNOR; Q6P1M3; -.
DR BioGRID-ORCS; 3993; 13 hits in 1072 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 155 other tissues.
DR ExpressionAtlas; Q6P1M3; baseline and differential.
DR Genevisible; Q6P1M3; HS.
DR GO; GO:0005912; C:adherens junction; IC: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; IC: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; -; 2.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08366; LLGL; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
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
