ID BRF2_HUMAN Reviewed; 419 AA. AC Q9HAW0; B2RD62; B4DFZ6; D3DSW6; Q9H2Y3; Q9H3B3; Q9NUY6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 14-DEC-2022, entry version 177. DE RecName: Full=Transcription factor IIIB 50 kDa subunit; DE Short=TFIIIB50 {ECO:0000303|PubMed:11121026}; DE Short=hTFIIIB50 {ECO:0000303|PubMed:11121026}; DE AltName: Full=B-related factor 2; DE Short=BRF-2; DE AltName: Full=hBRFU; GN Name=BRF2; Synonyms=BRFU {ECO:0000303|PubMed:11040218}; ORFNames=PRO1470; 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), AND FUNCTION. RX PubMed=11040218; DOI=10.1101/gad.836400; RA Schramm L., Pendergrast P.S., Sun Y., Hernandez N.; RT "Different human TFIIIB activities direct RNA polymerase III transcription RT from TATA-containing and TATA-less promoters."; RL Genes Dev. 14:2650-2663(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=11121026; DOI=10.1073/pnas.97.26.14200; RA Teichmann M., Wang Z., Roeder R.G.; RT "A stable complex of a novel transcription factor IIB- related factor, RT human TFIIIB50, and associated proteins mediate selective transcription by RT RNA polymerase III of genes with upstream promoter elements."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14200-14205(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, Placenta, and Umbilical cord blood; 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 [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] (ISOFORM 1). RC TISSUE=Eye; 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 264-419 (ISOFORM 1). RC TISSUE=Fetal liver; RX PubMed=11483580; DOI=10.1101/gr.175501; RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.; RT "Gene expression profiling in human fetal liver and identification of RT tissue- and developmental-stage-specific genes through compiled expression RT profiles and efficient cloning of full-length cDNAs."; RL Genome Res. 11:1392-1403(2001). RN [7] RP FUNCTION, AND INTERACTION WITH TBP. RX PubMed=11564744; DOI=10.1074/jbc.m108515200; RA Cabart P., Murphy S.; RT "BRFU, a TFIIB-like factor, is directly recruited to the TATA-box of RT polymerase III small nuclear RNA gene promoters through its interaction RT with TATA-binding protein."; RL J. Biol. Chem. 276:43056-43064(2001). RN [8] RP IDENTIFICATION IN THE TFIIIB-ALPHA COMPLEX. RX PubMed=12016223; DOI=10.1074/jbc.m203119200; RA Cabart P., Murphy S.; RT "Assembly of human small nuclear RNA gene-specific transcription factor RT IIIB complex de novo on and off promoter."; RL J. Biol. Chem. 277:26831-26838(2002). RN [9] RP SUBUNIT. RX PubMed=12391172; DOI=10.1128/mcb.22.22.8067-8078.2002; RA Ma B., Hernandez N.; RT "Redundant cooperative interactions for assembly of a human U6 RT transcription initiation complex."; RL Mol. Cell. Biol. 22:8067-8078(2002). RN [10] RP INTERACTION WITH SNAPC4, AND SUBUNIT. RX PubMed=12621023; DOI=10.1074/jbc.m204247200; RA Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.; RT "The small nuclear RNA-activating protein 190 Myb DNA binding domain RT stimulates TATA box-binding protein-TATA box recognition."; RL J. Biol. Chem. 278:18649-18657(2003). RN [11] RP SUBUNIT. RX PubMed=14527415; DOI=10.1016/j.molcel.2003.08.011; RA Hu P., Wu S., Hernandez N.; RT "A minimal RNA polymerase III transcription system from human cells reveals RT positive and negative regulatory roles for CK2."; RL Mol. Cell 12:699-709(2003). RN [12] RP SUBUNIT. RX PubMed=16227591; DOI=10.1128/mcb.25.21.9406-9418.2005; RA Saxena A., Ma B., Schramm L., Hernandez N.; RT "Structure-function analysis of the human TFIIB-related factor II protein RT reveals an essential role for the C-terminal domain in RNA polymerase III RT transcription."; RL Mol. Cell. Biol. 25:9406-9418(2005). RN [13] RP SUBUNIT. RX PubMed=16769183; DOI=10.1016/j.gene.2006.03.012; RA Emran F., Florens L., Ma B., Swanson S.K., Washburn M.P., Hernandez N.; RT "A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription RT complexes."; RL Gene 377:96-108(2006). RN [14] RP INTERACTION WITH MAF1, AND SUBCELLULAR LOCATION. RX PubMed=17505538; DOI=10.7150/ijbs.3.292; RA Rollins J., Veras I., Cabarcas S., Willis I., Schramm L.; RT "Human Maf1 negatively regulates RNA polymerase III transcription via the RT TFIIB family members Brf1 and Brf2."; RL Int. J. Biol. Sci. 3:292-302(2007). RN [15] RP INDUCTION. RX PubMed=17624304; DOI=10.1016/j.bbrc.2007.06.114; RA Jacob J., Cabarcas S., Veras I., Zaveri N., Schramm L.; RT "The green tea component EGCG inhibits RNA polymerase III transcription."; RL Biochem. Biophys. Res. Commun. 360:778-783(2007). RN [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [18] {ECO:0007744|PDB:4ROC, ECO:0007744|PDB:4ROD, ECO:0007744|PDB:4ROE} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 62-419 IN COMPLEX WITH TBP AND RP DNA, FUNCTION, INTERACTION WITH TBP, SUBUNIT, DNA-BINDING, MUTAGENESIS OF RP ARG-110 AND CYS-361, OXIDATION AT CYS-361, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=26638071; DOI=10.1016/j.cell.2015.11.005; RA Gouge J., Satia K., Guthertz N., Widya M., Thompson A.J., Cousin P., RA Dergai O., Hernandez N., Vannini A.; RT "Redox signaling by the RNA polymerase III TFIIB-related factor Brf2."; RL Cell 163:1375-1387(2015). CC -!- FUNCTION: General activator of RNA polymerase III transcription. Factor CC exclusively required for RNA polymerase III transcription of genes with CC promoter elements upstream of the initiation sites (PubMed:11040218, CC PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the CC regulation of gene expression; functions as activator in the absence of CC oxidative stress (PubMed:26638071). Down-regulates expression of target CC genes in response to oxidative stress (PubMed:26638071). Overexpression CC protects cells against apoptosis in response to oxidative stress CC (PubMed:26638071). {ECO:0000269|PubMed:11040218, CC ECO:0000269|PubMed:11121026, ECO:0000269|PubMed:11564744, CC ECO:0000269|PubMed:26638071}. CC -!- SUBUNIT: Component of TFIIIB complexes. The TFIIIB complex has two CC activities, alpha and beta. The TFIIIB-alpha activity complex is CC composed of TBP, BDP1, and a complex containing both BRF2 and at least CC four stably associated proteins; this complex inhibits the CC transcription by pol III via its phosphorylation by CK2; YY1 CC facilitates the TFIIIB-alpha complex formation. Interacts with TBP; CC this interaction promotes recruitment of BRF2 to TATA box-containing CC promoters (PubMed:26638071). Interacts with TBP and the BURE sequence CC (GC-rich sequence downstream from the TATA box) to form a strong CC ternary complex which is joined by BDP1; this ternary complex CC stimulates pol III transcription. Forms a trimeric complex composed of CC TBP, BRF2 and mini-SNAPc complex (SNAP43, SNAP50, and the N-terminal CC third of SNAP190) on the promoter. Assembly of the TBP-BRF2 complex is CC stimulated by SNAP190. Interacts with MAF1 and SNAPC4. CC {ECO:0000269|PubMed:11564744, ECO:0000269|PubMed:12016223, CC ECO:0000269|PubMed:12391172, ECO:0000269|PubMed:12621023, CC ECO:0000269|PubMed:14527415, ECO:0000269|PubMed:16227591, CC ECO:0000269|PubMed:16769183, ECO:0000269|PubMed:17505538, CC ECO:0000269|PubMed:26638071}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17505538}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9HAW0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9HAW0-2; Sequence=VSP_056834; CC -!- INDUCTION: Down-regulated by epigallocatechin gallate (EGCG) treatment. CC {ECO:0000269|PubMed:17624304}. CC -!- PTM: In response to oxidative stress, Cys-361 is reversibly oxidized to CC cysteine sulfenic acid. Oxidation of Cys-361 impairs formation of a CC ternary complex with TBP and DNA and down-regulates expression of CC target genes in response to oxidative stress. CC {ECO:0000269|PubMed:26638071}. CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG35486.1; Type=Erroneous initiation; Evidence={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; AF298153; AAG30222.1; -; mRNA. DR EMBL; AF206673; AAG35669.2; -; mRNA. DR EMBL; AK001914; BAA91975.1; -; mRNA. DR EMBL; AK294337; BAG57607.1; -; mRNA. DR EMBL; AK315420; BAG37809.1; -; mRNA. DR EMBL; CH471080; EAW63351.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63352.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63353.1; -; Genomic_DNA. DR EMBL; BC010648; AAH10648.1; -; mRNA. DR EMBL; AF130058; AAG35486.1; ALT_INIT; mRNA. DR CCDS; CCDS6098.1; -. [Q9HAW0-1] DR RefSeq; NP_060780.2; NM_018310.3. [Q9HAW0-1] DR PDB; 4ROC; X-ray; 1.90 A; A=62-419. DR PDB; 4ROD; X-ray; 2.70 A; A=62-419. DR PDB; 4ROE; X-ray; 2.20 A; A=62-419. DR PDB; 5N9G; X-ray; 2.70 A; A/F=62-419. DR PDBsum; 4ROC; -. DR PDBsum; 4ROD; -. DR PDBsum; 4ROE; -. DR PDBsum; 5N9G; -. DR AlphaFoldDB; Q9HAW0; -. DR SMR; Q9HAW0; -. DR BioGRID; 120578; 38. DR IntAct; Q9HAW0; 3. DR STRING; 9606.ENSP00000220659; -. DR iPTMnet; Q9HAW0; -. DR PhosphoSitePlus; Q9HAW0; -. DR BioMuta; BRF2; -. DR DMDM; 74734246; -. DR EPD; Q9HAW0; -. DR jPOST; Q9HAW0; -. DR MassIVE; Q9HAW0; -. DR MaxQB; Q9HAW0; -. DR PaxDb; Q9HAW0; -. DR PeptideAtlas; Q9HAW0; -. DR ProteomicsDB; 81450; -. [Q9HAW0-1] DR Antibodypedia; 10831; 130 antibodies from 26 providers. DR DNASU; 55290; -. DR Ensembl; ENST00000220659.11; ENSP00000220659.6; ENSG00000104221.13. [Q9HAW0-1] DR GeneID; 55290; -. DR KEGG; hsa:55290; -. DR MANE-Select; ENST00000220659.11; ENSP00000220659.6; NM_018310.4; NP_060780.2. DR UCSC; uc003xkk.4; human. [Q9HAW0-1] DR AGR; HGNC:17298; -. DR CTD; 55290; -. DR DisGeNET; 55290; -. DR GeneCards; BRF2; -. DR HGNC; HGNC:17298; BRF2. DR HPA; ENSG00000104221; Low tissue specificity. DR MIM; 607013; gene. DR neXtProt; NX_Q9HAW0; -. DR OpenTargets; ENSG00000104221; -. DR PharmGKB; PA164741329; -. DR VEuPathDB; HostDB:ENSG00000104221; -. DR eggNOG; KOG1598; Eukaryota. DR GeneTree; ENSGT00390000002288; -. DR HOGENOM; CLU_039947_0_0_1; -. DR InParanoid; Q9HAW0; -. DR OMA; LARFCKM; -. DR OrthoDB; 1518547at2759; -. DR PhylomeDB; Q9HAW0; -. DR TreeFam; TF331596; -. DR PathwayCommons; Q9HAW0; -. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR SignaLink; Q9HAW0; -. DR SIGNOR; Q9HAW0; -. DR BioGRID-ORCS; 55290; 788 hits in 1085 CRISPR screens. DR ChiTaRS; BRF2; human. DR GeneWiki; BRF2_(gene); -. DR GenomeRNAi; 55290; -. DR Pharos; Q9HAW0; Tbio. DR PRO; PR:Q9HAW0; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9HAW0; protein. DR Bgee; ENSG00000104221; Expressed in skeletal muscle tissue of rectus abdominis and 204 other tissues. DR ExpressionAtlas; Q9HAW0; baseline and differential. DR Genevisible; Q9HAW0; HS. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000126; C:transcription factor TFIIIB complex; IMP:UniProtKB. DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB. DR GO; GO:0006352; P:DNA-templated transcription initiation; IBA:GO_Central. DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IMP:UniProtKB. DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR SUPFAM; SSF47954; Cyclin-like; 1. DR PROSITE; PS51134; ZF_TFIIB; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Metal-binding; Nucleus; KW Oxidation; Phosphoprotein; Reference proteome; Repeat; Stress response; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..419 FT /note="Transcription factor IIIB 50 kDa subunit" FT /id="PRO_0000337187" FT REPEAT 72..157 FT /note="1" FT REPEAT 173..249 FT /note="2" FT ZN_FING 2..36 FT /note="TFIIB-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT REGION 108..114 FT /note="Interaction with target DNA" FT /evidence="ECO:0000269|PubMed:26638071, FT ECO:0007744|PDB:4ROC, ECO:0007744|PDB:4ROD, FT ECO:0007744|PDB:4ROE" FT REGION 314..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..363 FT /note="Required for the formation of a ternary complex with FT DNA and TBP; not required for interaction with TBP in the FT absence of DNA" FT /evidence="ECO:0000269|PubMed:26638071" FT REGION 365..419 FT /note="Required for interaction with TBP and formation of a FT ternary complex with DNA and TBP" FT /evidence="ECO:0000269|PubMed:26638071" FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 361 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000269|PubMed:26638071" FT VAR_SEQ 10..32 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056834" FT MUTAGEN 110 FT /note="R->A: Decreases affinity for DNA." FT /evidence="ECO:0000269|PubMed:26638071" FT MUTAGEN 361 FT /note="C->A: Abolishes response to oxidative stress. FT Abolishes the decrease in the formation of a ternary FT complex with DNA and TBP in response to oxidative stress." FT /evidence="ECO:0000269|PubMed:26638071" FT MUTAGEN 361 FT /note="C->D: Impairs formation of a ternary complex with FT DNA and TBP." FT /evidence="ECO:0000269|PubMed:26638071" FT CONFLICT 153 FT /note="Y -> C (in Ref. 3; BAA91975)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="S -> F (in Ref. 2; AAG35669)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="T -> I (in Ref. 3; BAG57607)" FT /evidence="ECO:0000305" FT HELIX 67..82 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 87..101 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 111..128 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 135..142 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 146..159 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 197..213 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 223..237 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 262..277 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:4ROC" FT TURN 285..287 FT /evidence="ECO:0007829|PDB:4ROE" FT TURN 290..293 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 297..302 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 304..313 FT /evidence="ECO:0007829|PDB:4ROC" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 386..390 FT /evidence="ECO:0007829|PDB:4ROC" FT HELIX 396..406 FT /evidence="ECO:0007829|PDB:4ROC" SQ SEQUENCE 419 AA; 46533 MW; 90A39F72DBA14888 CRC64; MPGRGRCPDC GSTELVEDSH YSQSQLVCSD CGCVVTEGVL TTTFSDEGNL REVTYSRSTG ENEQVSRSQQ RGLRRVRDLC RVLQLPPTFE DTAVAYYQQA YRHSGIRAAR LQKKEVLVGC CVLITCRQHN WPLTMGAICT LLYADLDVFS STYMQIVKLL GLDVPSLCLA ELVKTYCSSF KLFQASPSVP AKYVEDKEKM LSRTMQLVEL ANETWLVTGR HPLPVITAAT FLAWQSLQPA DRLSCSLARF CKLANVDLPY PASSRLQELL AVLLRMAEQL AWLRVLRLDK RSVVKHIGDL LQHRQSLVRS AFRDGTAEVE TREKEPPGWG QGQGEGEVGN NSLGLPQGKR PASPALLLPP CMLKSPKRIC PVPPVSTVTG DENISDSEIE QYLRTPQEVR DFQRAQAARQ AATSVPNPP //