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 03-JUL-2019, entry version 158. 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}; GN ORFNames=PRO1470; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT transcription 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 RT transcription by RNA polymerase III of genes with upstream promoter RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., RA He F.; RT "Gene expression profiling in human fetal liver and identification of RT tissue- and developmental-stage-specific genes through compiled RT expression 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 RT interaction 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 RT factor 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 RT reveals 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 RT protein reveals an essential role for the C-terminal domain in RNA RT polymerase III 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., RA 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 RT the 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 RT 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 RP BY 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:0000244|PDB:4ROC, ECO:0000244|PDB:4ROD, ECO:0000244|PDB:4ROE} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 62-419 IN COMPLEX WITH TBP RP AND DNA, FUNCTION, INTERACTION WITH TBP, SUBUNIT, DNA-BINDING, RP MUTAGENESIS OF ARG-110 AND CYS-361, OXIDATION AT CYS-361, AND RP IDENTIFICATION BY MASS 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 RT Brf2."; RL Cell 163:1375-1387(2015). CC -!- FUNCTION: General activator of RNA polymerase III transcription. CC Factor exclusively required for RNA polymerase III transcription CC of genes with promoter elements upstream of the initiation sites CC (PubMed:11040218, PubMed:11121026, PubMed:11564744, CC PubMed:26638071). Contributes to the regulation of gene CC expression; functions as activator in the absence of oxidative CC stress (PubMed:26638071). Down-regulates expression of target CC genes in response to oxidative stress (PubMed:26638071). CC Overexpression protects cells against apoptosis in response to CC oxidative stress (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 CC least 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 CC TBP; this interaction promotes recruitment of BRF2 to TATA box- CC containing promoters (PubMed:26638071). Interacts with TBP and the CC BURE sequence (GC-rich sequence downstream from the TATA box) to CC form a strong ternary complex which is joined by BDP1; this CC ternary complex stimulates pol III transcription. Forms a trimeric CC complex composed of TBP, BRF2 and mini-SNAPc complex (SNAP43, CC SNAP50, and the N-terminal third of SNAP190) on the promoter. CC Assembly of the TBP-BRF2 complex is stimulated by SNAP190. CC Interacts with MAF1 and SNAPC4. {ECO:0000269|PubMed:11564744, CC ECO:0000269|PubMed:12016223, ECO:0000269|PubMed:12391172, CC ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:14527415, CC ECO:0000269|PubMed:16227591, ECO:0000269|PubMed:16769183, CC ECO:0000269|PubMed:17505538, 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 Note=No experimental confirmation available.; CC -!- INDUCTION: Down-regulated by epigallocatechin gallate (EGCG) CC treatment. {ECO:0000269|PubMed:17624304}. CC -!- PTM: In response to oxidative stress, Cys-361 is reversibly CC oxidized to cysteine sulfenic acid. Oxidation of Cys-361 impairs CC formation of a ternary complex with TBP and DNA and down-regulates CC expression of 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 SMR; Q9HAW0; -. DR BioGrid; 120578; 34. DR STRING; 9606.ENSP00000220659; -. DR iPTMnet; Q9HAW0; -. DR PhosphoSitePlus; Q9HAW0; -. DR BioMuta; BRF2; -. DR DMDM; 74734246; -. DR jPOST; Q9HAW0; -. DR MaxQB; Q9HAW0; -. DR PaxDb; Q9HAW0; -. DR PeptideAtlas; Q9HAW0; -. DR PRIDE; Q9HAW0; -. DR ProteomicsDB; 81450; -. DR DNASU; 55290; -. DR Ensembl; ENST00000220659; ENSP00000220659; ENSG00000104221. [Q9HAW0-1] DR GeneID; 55290; -. DR KEGG; hsa:55290; -. DR UCSC; uc003xkk.4; human. [Q9HAW0-1] DR CTD; 55290; -. DR DisGeNET; 55290; -. DR GeneCards; BRF2; -. DR HGNC; HGNC:17298; BRF2. DR HPA; CAB019269; -. DR HPA; HPA023378; -. DR MIM; 607013; gene. DR neXtProt; NX_Q9HAW0; -. DR OpenTargets; ENSG00000104221; -. DR PharmGKB; PA164741329; -. DR eggNOG; KOG1598; Eukaryota. DR eggNOG; COG1405; LUCA. DR GeneTree; ENSGT00390000002288; -. DR HOGENOM; HOG000095260; -. DR InParanoid; Q9HAW0; -. DR KO; K15197; -. DR OMA; CMLKPPK; -. DR OrthoDB; 1518547at2759; -. DR PhylomeDB; Q9HAW0; -. DR TreeFam; TF331596; -. 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 ChiTaRS; BRF2; human. DR GeneWiki; BRF2_(gene); -. DR GenomeRNAi; 55290; -. DR PRO; PR:Q9HAW0; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000104221; Expressed in 223 organ(s), highest expression level in skeletal muscle tissue. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; IDA:UniProtKB. DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0008134; F:transcription factor 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:0070898; P:RNA polymerase III preinitiation complex assembly; IBA:GO_Central. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618; PTHR11618; 1. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR SUPFAM; SSF47954; SSF47954; 1. DR PROSITE; PS51134; ZF_TFIIB; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Complete proteome; KW Metal-binding; Nucleus; Oxidation; Phosphoprotein; Reference proteome; KW Repeat; Stress response; Transcription; Transcription regulation; KW Zinc; Zinc-finger. FT CHAIN 1 419 Transcription factor IIIB 50 kDa subunit. FT /FTId=PRO_0000337187. FT REPEAT 72 157 1. FT REPEAT 173 249 2. FT ZN_FING 2 36 TFIIB-type. {ECO:0000255|PROSITE- FT ProRule:PRU00469}. FT REGION 108 114 Interaction with target DNA. FT {ECO:0000244|PDB:4ROC, FT ECO:0000244|PDB:4ROD, FT ECO:0000244|PDB:4ROE, FT ECO:0000269|PubMed:26638071}. FT REGION 357 363 Required for the formation of a ternary FT complex with DNA and TBP; not required FT for interaction with TBP in the absence FT of DNA. {ECO:0000269|PubMed:26638071}. FT REGION 365 419 Required for interaction with TBP and FT formation of a ternary complex with DNA FT and TBP. {ECO:0000269|PubMed:26638071}. FT METAL 7 7 Zinc. {ECO:0000250|UniProtKB:Q00403}. FT METAL 28 28 Zinc. {ECO:0000250|UniProtKB:Q00403}. FT METAL 31 31 Zinc. {ECO:0000250|UniProtKB:Q00403}. FT MOD_RES 353 353 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 361 361 Cysteine sulfenic acid (-SOH). FT {ECO:0000269|PubMed:26638071}. FT VAR_SEQ 10 32 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056834. FT MUTAGEN 110 110 R->A: Decreases affinity for DNA. FT {ECO:0000269|PubMed:26638071}. FT MUTAGEN 361 361 C->A: Abolishes response to oxidative FT stress. Abolishes the decrease in the FT formation of a ternary complex with DNA FT and TBP in response to oxidative stress. FT {ECO:0000269|PubMed:26638071}. FT MUTAGEN 361 361 C->D: Impairs formation of a ternary FT complex with DNA and TBP. FT {ECO:0000269|PubMed:26638071}. FT CONFLICT 153 153 Y -> C (in Ref. 3; BAA91975). FT {ECO:0000305}. FT CONFLICT 376 376 S -> F (in Ref. 2; AAG35669). FT {ECO:0000305}. FT CONFLICT 379 379 T -> I (in Ref. 3; BAG57607). FT {ECO:0000305}. FT HELIX 67 82 {ECO:0000244|PDB:4ROC}. FT HELIX 87 101 {ECO:0000244|PDB:4ROC}. FT HELIX 104 107 {ECO:0000244|PDB:4ROC}. FT HELIX 111 128 {ECO:0000244|PDB:4ROC}. FT HELIX 135 142 {ECO:0000244|PDB:4ROC}. FT HELIX 146 159 {ECO:0000244|PDB:4ROC}. FT HELIX 169 178 {ECO:0000244|PDB:4ROC}. FT HELIX 191 193 {ECO:0000244|PDB:4ROC}. FT HELIX 197 213 {ECO:0000244|PDB:4ROC}. FT HELIX 223 237 {ECO:0000244|PDB:4ROC}. FT HELIX 239 242 {ECO:0000244|PDB:4ROC}. FT HELIX 247 253 {ECO:0000244|PDB:4ROC}. FT HELIX 262 277 {ECO:0000244|PDB:4ROC}. FT HELIX 281 284 {ECO:0000244|PDB:4ROC}. FT TURN 285 287 {ECO:0000244|PDB:4ROE}. FT TURN 290 293 {ECO:0000244|PDB:4ROC}. FT HELIX 294 296 {ECO:0000244|PDB:4ROC}. FT HELIX 297 302 {ECO:0000244|PDB:4ROC}. FT HELIX 304 313 {ECO:0000244|PDB:4ROC}. FT TURN 360 362 {ECO:0000244|PDB:4ROC}. FT HELIX 386 390 {ECO:0000244|PDB:4ROC}. FT HELIX 396 406 {ECO:0000244|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 //