ID TF3C2_HUMAN Reviewed; 911 AA. AC Q8WUA4; D6W557; Q16632; Q9BWI7; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 24-JAN-2024, entry version 195. DE RecName: Full=General transcription factor 3C polypeptide 2; DE AltName: Full=TF3C-beta; DE AltName: Full=Transcription factor IIIC 110 kDa subunit; DE Short=TFIIIC 110 kDa subunit; DE Short=TFIIIC110; DE AltName: Full=Transcription factor IIIC subunit beta; GN Name=GTF3C2; Synonyms=KIAA0011; 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 1), PROTEIN SEQUENCE OF 41-62; 338-354; RP 642-654 AND 757-774, AND IDENTIFICATION OF SUBUNITS OF TFIIIC2 COMPLEX. RX PubMed=7729686; DOI=10.1101/gad.9.6.675; RA Sinn E., Wang Z., Kovelman R., Roeder R.G.; RT "Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta) whose RT presence correlates with activation of RNA polymerase III-mediated RT transcription by adenovirus E1A expression and serum factors."; RL Genes Dev. 9:675-685(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-911. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-167, AND RP IDENTIFICATION BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND THR-895, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-167; SER-871; RP SER-892 AND SER-893, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-220 AND SER-892, AND 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-167; SER-597; RP SER-871; THR-895 AND SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-260 AND SER-901, AND 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). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Required for RNA polymerase III-mediated transcription. CC Component of TFIIIC that initiates transcription complex assembly on CC tRNA and is required for transcription of 5S rRNA and other stable CC nuclear and cytoplasmic RNAs. May play a direct role in stabilizing CC interactions of TFIIIC2 with TFIIIC1. CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. CC -!- INTERACTION: CC Q8WUA4; Q12789: GTF3C1; NbExp=2; IntAct=EBI-1237062, EBI-357956; CC Q8WUA4; P42345: MTOR; NbExp=3; IntAct=EBI-1237062, EBI-359260; CC Q8WUA4; Q8N122: RPTOR; NbExp=3; IntAct=EBI-1237062, EBI-1567928; CC Q8WUA4-2; Q08AM6: VAC14; NbExp=3; IntAct=EBI-11957962, EBI-2107455; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WUA4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WUA4-2; Sequence=VSP_010566, VSP_010567; 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; D13636; BAA02800.1; -; mRNA. DR EMBL; BT009799; AAP88801.1; -; mRNA. DR EMBL; CH471053; EAX00595.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00596.1; -; Genomic_DNA. DR EMBL; BC000212; AAH00212.1; -; mRNA. DR EMBL; BC020981; AAH20981.1; -; mRNA. DR EMBL; AF054988; AAC09349.1; -; mRNA. DR CCDS; CCDS1749.1; -. [Q8WUA4-1] DR PIR; A56465; A56465. DR RefSeq; NP_001030598.1; NM_001035521.2. [Q8WUA4-1] DR RefSeq; NP_001305838.1; NM_001318909.1. [Q8WUA4-1] DR RefSeq; NP_001512.1; NM_001521.3. [Q8WUA4-1] DR PDB; 8CLI; EM; 3.20 A; C=1-911. DR PDB; 8CLJ; EM; 3.20 A; C/H=1-911. DR PDB; 8CLL; EM; 3.40 A; C/H=1-911. DR PDBsum; 8CLI; -. DR PDBsum; 8CLJ; -. DR PDBsum; 8CLL; -. DR AlphaFoldDB; Q8WUA4; -. DR EMDB; EMD-16713; -. DR EMDB; EMD-16714; -. DR EMDB; EMD-16717; -. DR SMR; Q8WUA4; -. DR BioGRID; 109231; 187. DR ComplexPortal; CPX-2373; General transcription factor TFIIIC complex. DR CORUM; Q8WUA4; -. DR DIP; DIP-38213N; -. DR IntAct; Q8WUA4; 71. DR MINT; Q8WUA4; -. DR STRING; 9606.ENSP00000352536; -. DR GlyGen; Q8WUA4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8WUA4; -. DR MetOSite; Q8WUA4; -. DR PhosphoSitePlus; Q8WUA4; -. DR SwissPalm; Q8WUA4; -. DR BioMuta; GTF3C2; -. DR DMDM; 48428661; -. DR EPD; Q8WUA4; -. DR jPOST; Q8WUA4; -. DR MassIVE; Q8WUA4; -. DR MaxQB; Q8WUA4; -. DR PaxDb; 9606-ENSP00000352536; -. DR PeptideAtlas; Q8WUA4; -. DR ProteomicsDB; 74647; -. [Q8WUA4-1] DR ProteomicsDB; 74648; -. [Q8WUA4-2] DR Pumba; Q8WUA4; -. DR Antibodypedia; 13626; 227 antibodies from 28 providers. DR DNASU; 2976; -. DR Ensembl; ENST00000264720.8; ENSP00000264720.3; ENSG00000115207.15. [Q8WUA4-1] DR Ensembl; ENST00000359541.6; ENSP00000352536.2; ENSG00000115207.15. [Q8WUA4-1] DR GeneID; 2976; -. DR KEGG; hsa:2976; -. DR MANE-Select; ENST00000264720.8; ENSP00000264720.3; NM_001035521.3; NP_001030598.1. DR UCSC; uc002rju.3; human. [Q8WUA4-1] DR AGR; HGNC:4665; -. DR CTD; 2976; -. DR DisGeNET; 2976; -. DR GeneCards; GTF3C2; -. DR HGNC; HGNC:4665; GTF3C2. DR HPA; ENSG00000115207; Low tissue specificity. DR MIM; 604883; gene. DR neXtProt; NX_Q8WUA4; -. DR OpenTargets; ENSG00000115207; -. DR PharmGKB; PA29053; -. DR VEuPathDB; HostDB:ENSG00000115207; -. DR eggNOG; ENOG502RAA6; Eukaryota. DR GeneTree; ENSGT00390000018632; -. DR HOGENOM; CLU_014720_0_0_1; -. DR InParanoid; Q8WUA4; -. DR OMA; DKGFIWQ; -. DR OrthoDB; 2919637at2759; -. DR PhylomeDB; Q8WUA4; -. DR TreeFam; TF314779; -. DR PathwayCommons; Q8WUA4; -. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter. DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter. DR SignaLink; Q8WUA4; -. DR SIGNOR; Q8WUA4; -. DR BioGRID-ORCS; 2976; 617 hits in 1166 CRISPR screens. DR ChiTaRS; GTF3C2; human. DR GeneWiki; GTF3C2; -. DR GenomeRNAi; 2976; -. DR Pharos; Q8WUA4; Tbio. DR PRO; PR:Q8WUA4; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8WUA4; Protein. DR Bgee; ENSG00000115207; Expressed in lower esophagus mucosa and 103 other cell types or tissues. DR ExpressionAtlas; Q8WUA4; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL. DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central. DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IC:HGNC-UCL. DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:HGNC-UCL. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR15052:SF2; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 2; 1. DR PANTHER; PTHR15052; RNA POLYMERASE III TRANSCRIPTION INITIATION FACTOR COMPLEX SUBUNIT; 1. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 4. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q8WUA4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; WD repeat. FT CHAIN 1..911 FT /note="General transcription factor 3C polypeptide 2" FT /id="PRO_0000050985" FT REPEAT 366..426 FT /note="WD 1" FT REPEAT 427..483 FT /note="WD 2" FT REPEAT 484..535 FT /note="WD 3" FT REPEAT 536..603 FT /note="WD 4" FT REPEAT 604..654 FT /note="WD 5" FT REPEAT 655..690 FT /note="WD 6" FT REGION 24..187 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 205..297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 765..785 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 889..911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..50 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..110 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..183 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..265 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 266..285 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 768..785 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 167 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 597 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 871 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 892 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 895 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 901 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 579..585 FT /note="MVVFWNL -> KKNQNKT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010566" FT VAR_SEQ 586..911 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010567" FT CONFLICT 301 FT /note="N -> D (in Ref. 3; AAP88801 and 4; AAH20981)" FT /evidence="ECO:0000305" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 301..321 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 384..386 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 397..402 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 414..419 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 437..443 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 449..451 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 458..467 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 470..475 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 495..503 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 508..514 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 516..522 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 532..535 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 538..541 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 556..562 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 570..575 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 578..584 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 590..592 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 601..603 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 606..610 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 618..621 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 628..632 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 634..636 FT /evidence="ECO:0007829|PDB:8CLJ" FT STRAND 637..642 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 650..654 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 658..662 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 668..674 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 676..678 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 681..683 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 685..689 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 692..694 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 699..703 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 708..713 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 715..717 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 719..724 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 727..733 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 741..743 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 747..750 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 751..761 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 787..791 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 794..800 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 809..811 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 813..821 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 822..824 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 837..842 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 847..850 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 851..856 FT /evidence="ECO:0007829|PDB:8CLI" FT STRAND 860..865 FT /evidence="ECO:0007829|PDB:8CLI" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:8CLI" FT HELIX 872..888 FT /evidence="ECO:0007829|PDB:8CLI" SQ SEQUENCE 911 AA; 100680 MW; B59D91DE74555192 CRC64; MDTCGVGYVA LGEAGPVGNM TVVDSPGQEV LNQLDVKTSS EMTSAEASVE MSLPTPLPGF EDSPDQRRLP PEQESLSRLE QPDLSSEMSK VSKPRASKPG RKRGGRTRKG PKRPQQPNPP SAPLVPGLLD QSNPLSTPMP KKRGRKSKAE LLLLKLSKDL DRPESQSPKR PPEDFETPSG ERPRRRAAQV ALLYLQELAE ELSTALPAPV SCPEGPKVSS PTKPKKIRQP AACPGGEEVD GAPRDEDFFL QVEAEDVEES EGPSESSSEP EPVVPRSTPR GSTSGKQKPH CRGMAPNGLP NHIMAPVWKC LHLTKDFREQ KHSYWEFAEW IPLAWKWHLL SELEAAPYLP QEEKSPLFSV QREGLPEDGT LYRINRFSSI TAHPERWDVS FFTGGPLWAL DWCPVPEGAG ASQYVALFSS PDMNETHPLS QLHSGPGLLQ LWGLGTLQQE SCPGNRAHFV YGIACDNGCI WDLKFCPSGA WELPGTPRKA PLLPRLGLLA LACSDGKVLL FSLPHPEALL AQQPPDAVKP AIYKVQCVAT LQVGSMQATD PSECGQCLSL AWMPTRPHQH LAAGYYNGMV VFWNLPTNSP LQRIRLSDGS LKLYPFQCFL AHDQAVRTLQ WCKANSHFLV SAGSDRKIKF WDLRRPYEPI NSIKRFLSTE LAWLLPYNGV TVAQDNCYAS YGLCGIHYID AGYLGFKAYF TAPRKGTVWS LSGSDWLGTI AAGDISGELI AAILPDMALN PINVKRPVER RFPIYKADLI PYQDSPEGPD HSSASSGVPN PPKARTYTET VNHHYLLFQD TDLGSFHDLL RREPMLRMQE GEGHSQLCLD RLQLEAIHKV RFSPNLDSYG WLVSGGQSGL VRIHFVRGLA SPLGHRMQLE SRAHFNAMFQ PSSPTRRPGF SPTSHRLLPT P //