ID   TF3C4_HUMAN             Reviewed;         822 AA.
AC   Q9UKN8; Q5VZJ7;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=General transcription factor 3C polypeptide 4;
DE            EC=2.3.1.48;
DE   AltName: Full=TF3C-delta;
DE   AltName: Full=Transcription factor IIIC 90 kDa subunit;
DE            Short=TFIIIC 90 kDa subunit;
DE            Short=TFIIIC90;
DE   AltName: Full=Transcription factor IIIC subunit delta;
GN   Name=GTF3C4;
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], PROTEIN SEQUENCE OF 139-156; 170-179; 614-626
RP   AND 643-659, AND INTERACTION WITH GTF3C1; GTF3C2; GTF3C5; BRF1; POLR3C AND
RP   POLR3F.
RX   PubMed=10523658; DOI=10.1128/mcb.19.11.7697;
RA   Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.;
RT   "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the
RT   RNA polymerase III machinery and contains a histone-specific
RT   acetyltransferase activity.";
RL   Mol. Cell. Biol. 19:7697-7704(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Placenta, 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   [5]
RP   IDENTIFICATION IN TFIIIC COMPLEX, AND INTERACTION WITH GTF3C6.
RX   PubMed=17409385; DOI=10.1074/jbc.m611542200;
RA   Dumay-Odelot H., Marck C., Durrieu-Gaillard S., Lefebvre O., Jourdain S.,
RA   Prochazkova M., Pflieger A., Teichmann M.;
RT   "Identification, molecular cloning, and characterization of the sixth
RT   subunit of human transcription factor TFIIIC.";
RL   J. Biol. Chem. 282:17179-17189(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-604; SER-611 AND
RP   SER-652, AND IDENTIFICATION BY 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   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-629, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Essential for RNA polymerase III to make a number of small
CC       nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-
CC       associated (VA) RNA of both cellular and viral origin. Has histone
CC       acetyltransferase activity (HAT) with unique specificity for free and
CC       nucleosomal H3. May cooperate with GTF3C5 in facilitating the
CC       recruitment of TFIIIB and RNA polymerase through direct interactions
CC       with BRF1, POLR3C and POLR3F. May be localized close to the A box.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC       with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and POLR3F.
CC       {ECO:0000269|PubMed:10523658, ECO:0000269|PubMed:17409385}.
CC   -!- INTERACTION:
CC       Q9UKN8; Q969F1: GTF3C6; NbExp=2; IntAct=EBI-1237240, EBI-6268616;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the TFIIIC subunit 4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11619.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF142328; AAF05087.1; -; mRNA.
DR   EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW88011.1; -; Genomic_DNA.
DR   EMBL; BC011619; AAH11619.1; ALT_SEQ; mRNA.
DR   EMBL; BC094774; AAH94774.1; -; mRNA.
DR   EMBL; BC104755; AAI04756.1; -; mRNA.
DR   EMBL; BC112245; AAI12246.1; -; mRNA.
DR   CCDS; CCDS6953.1; -.
DR   RefSeq; NP_036336.2; NM_012204.3.
DR   PDB; 8CLI; EM; 3.20 A; B=1-822.
DR   PDB; 8CLJ; EM; 3.20 A; B/G=1-822.
DR   PDB; 8CLL; EM; 3.40 A; B/G=1-822.
DR   PDBsum; 8CLI; -.
DR   PDBsum; 8CLJ; -.
DR   PDBsum; 8CLL; -.
DR   AlphaFoldDB; Q9UKN8; -.
DR   EMDB; EMD-16713; -.
DR   EMDB; EMD-16714; -.
DR   EMDB; EMD-16717; -.
DR   SMR; Q9UKN8; -.
DR   BioGRID; 114738; 188.
DR   ComplexPortal; CPX-2373; General transcription factor TFIIIC complex.
DR   CORUM; Q9UKN8; -.
DR   IntAct; Q9UKN8; 51.
DR   MINT; Q9UKN8; -.
DR   STRING; 9606.ENSP00000361219; -.
DR   GlyGen; Q9UKN8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UKN8; -.
DR   MetOSite; Q9UKN8; -.
DR   PhosphoSitePlus; Q9UKN8; -.
DR   SwissPalm; Q9UKN8; -.
DR   BioMuta; GTF3C4; -.
DR   DMDM; 212276467; -.
DR   EPD; Q9UKN8; -.
DR   jPOST; Q9UKN8; -.
DR   MassIVE; Q9UKN8; -.
DR   MaxQB; Q9UKN8; -.
DR   PaxDb; 9606-ENSP00000361219; -.
DR   PeptideAtlas; Q9UKN8; -.
DR   ProteomicsDB; 84826; -.
DR   Pumba; Q9UKN8; -.
DR   Antibodypedia; 31705; 263 antibodies from 27 providers.
DR   DNASU; 9329; -.
DR   Ensembl; ENST00000372146.5; ENSP00000361219.4; ENSG00000125484.12.
DR   GeneID; 9329; -.
DR   KEGG; hsa:9329; -.
DR   MANE-Select; ENST00000372146.5; ENSP00000361219.4; NM_012204.4; NP_036336.2.
DR   UCSC; uc010mzv.4; human.
DR   AGR; HGNC:4667; -.
DR   CTD; 9329; -.
DR   GeneCards; GTF3C4; -.
DR   HGNC; HGNC:4667; GTF3C4.
DR   HPA; ENSG00000125484; Low tissue specificity.
DR   MIM; 604892; gene.
DR   neXtProt; NX_Q9UKN8; -.
DR   OpenTargets; ENSG00000125484; -.
DR   PharmGKB; PA29055; -.
DR   VEuPathDB; HostDB:ENSG00000125484; -.
DR   eggNOG; ENOG502QTDJ; Eukaryota.
DR   GeneTree; ENSGT00390000011873; -.
DR   HOGENOM; CLU_018536_0_0_1; -.
DR   InParanoid; Q9UKN8; -.
DR   OMA; WKPSHED; -.
DR   OrthoDB; 5395638at2759; -.
DR   PhylomeDB; Q9UKN8; -.
DR   TreeFam; TF328412; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   PathwayCommons; Q9UKN8; -.
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; Q9UKN8; -.
DR   SIGNOR; Q9UKN8; -.
DR   BioGRID-ORCS; 9329; 550 hits in 1193 CRISPR screens.
DR   ChiTaRS; GTF3C4; human.
DR   GeneWiki; GTF3C4; -.
DR   GenomeRNAi; 9329; -.
DR   Pharos; Q9UKN8; Tdark.
DR   PRO; PR:Q9UKN8; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9UKN8; Protein.
DR   Bgee; ENSG00000125484; Expressed in primordial germ cell in gonad and 179 other cell types or tissues.
DR   ExpressionAtlas; Q9UKN8; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR   GO; GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
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; IC:HGNC-UCL.
DR   GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; TAS:ProtInc.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR   InterPro; IPR045803; DUF5921.
DR   InterPro; IPR044230; GTF3C4.
DR   InterPro; IPR024761; TFIIIC_delta_N.
DR   InterPro; IPR024764; TFIIIC_Znf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR15496:SF2; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 4; 1.
DR   PANTHER; PTHR15496; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 4 FAMILY; 1.
DR   Pfam; PF19336; DUF5921; 1.
DR   Pfam; PF12657; TFIIIC_delta; 1.
DR   Pfam; PF12660; zf-TFIIIC; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   Genevisible; Q9UKN8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transferase; Ubl conjugation.
FT   CHAIN           1..822
FT                   /note="General transcription factor 3C polypeptide 4"
FT                   /id="PRO_0000209713"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         604
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        225
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        629
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CONFLICT        268
FT                   /note="C -> S (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="C -> R (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="V -> L (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="L -> V (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="S -> K (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        690
FT                   /note="R -> P (in Ref. 1; AAF05087)"
FT                   /evidence="ECO:0000305"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          103..110
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           123..134
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           139..147
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          175..179
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           208..218
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            225..227
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           236..244
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          248..257
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          273..280
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          283..293
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           297..299
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          300..307
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          311..323
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          326..335
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          340..343
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          360..363
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          371..381
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            382..385
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          386..395
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          398..407
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          410..418
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          428..431
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            433..435
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          438..441
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          447..454
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          456..466
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           468..472
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          474..482
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          488..495
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          509..514
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           518..526
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           533..536
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           537..550
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           555..567
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           571..587
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           664..695
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           709..715
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          720..722
FT                   /evidence="ECO:0007829|PDB:8CLJ"
FT   HELIX           725..737
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            748..750
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          758..763
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          769..772
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            774..776
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          782..784
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           804..809
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            815..817
FT                   /evidence="ECO:0007829|PDB:8CLI"
SQ   SEQUENCE   822 AA;  91982 MW;  2546A1E7D87F563C CRC64;
     MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM VTRREPAVKL
     QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ DLVIHRTSVP APLNSCLLKV
     GSKTEVAECK EKFAASKDPT VSQTFMLDRV FNPEGKALPP MRGFKYTSWS PMGCDANGRC
     LLAALTMDNR LTIQANLNRL QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ
     RRHSMQTPVR MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI
     SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV KGYFTLRQPV
     ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF WCLLLISKAG LNVHNSHVTG
     LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL IPIFTDVALK FEHQLIKLSD VFGSVRTHGI
     AVSPCGAYLA IITTEGMING LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI
     DLVRWKILKD KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT
     HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD DSLPTTGDAG
     GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW ITENTSIPTR GLCNFLMSDE
     EYDDRTARVL IGHISKKMNK QTFPEHCSLC KEILPFTDRK QAVCSNGHIW LRCFLTYQSC
     QSLIYRRCLL HDSIARHPAP EDPDWIKRLL QSPCPFCDSP VF
//