ID 1433T_HUMAN Reviewed; 245 AA. AC P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 24-JUN-2015, entry version 169. DE RecName: Full=14-3-3 protein theta; DE AltName: Full=14-3-3 protein T-cell; DE AltName: Full=14-3-3 protein tau; DE AltName: Full=Protein HS1; GN Name=YWHAQ; 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]. RC TISSUE=T-cell; RX PubMed=2015305; DOI=10.1016/0167-4781(91)90136-A; RA Nielsen P.J.; RT "Primary structure of a human protein kinase regulator protein."; RL Biochim. Biophys. Acta 1088:425-428(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT vector."; RL Submitted (OCT-2004) 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., 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]. RC TISSUE=Placenta, Skin, and Uterus; 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 PROTEIN SEQUENCE OF 1-18. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Hepatoma; RA Bienvenut W.V., Dhillon A.S., Kolch W.; RL Submitted (FEB-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP PHOSPHORYLATION AT SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882; RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., RA Morrice N., Moelling K., Aitken A.; RT "14-3-3 is phosphorylated by casein kinase I on residue 233. RT Phosphorylation at this site in vivo regulates Raf/14-3-3 RT interaction."; RL J. Biol. Chem. 272:28882-28888(1997). RN [10] RP TISSUE SPECIFICITY. RX PubMed=11080204; DOI=10.1046/j.1471-4159.2000.0752511.x; RA Malaspina A., Kaushik N., de Belleroche J.; RT "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal RT cord."; RL J. Neurochem. 75:2511-2520(2000). RN [11] RP INTERACTION WITH CDKN1B. RX PubMed=12042314; DOI=10.1074/jbc.M203668200; RA Fujita N., Sato S., Katayama K., Tsuruo T.; RT "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 RT and cytoplasmic localization."; RL J. Biol. Chem. 277:28706-28713(2002). RN [12] RP FUNCTION, AND INTERACTION WITH PDPK1. RX PubMed=12177059; DOI=10.1074/jbc.M205141200; RA Sato S., Fujita N., Tsuruo T.; RT "Regulation of kinase activity of 3-phosphoinositide-dependent protein RT kinase-1 by binding to 14-3-3."; RL J. Biol. Chem. 277:39360-39367(2002). RN [13] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [14] 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [16] RP IDENTIFICATION BY 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION RP 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 [18] 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND RP LYS-115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [20] RP IDENTIFICATION BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] 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., RA Buerckstuemmer T., 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [23] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=7603573; DOI=10.1038/376188a0; RA Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., RA Gamblin S.J.; RT "Structure of a 14-3-3 protein and implications for coordination of RT multiple signalling pathways."; RL Nature 376:188-191(1995). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC Negatively regulates the kinase activity of PDPK1. CC {ECO:0000269|PubMed:12177059}. CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity). CC Interacts with SSH1. Interacts with CDKN1B ('Thr-198' CC phosphorylated form); the interaction translocates CDKN1B to the CC cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' CC phosphorylated form of PDPK1. {ECO:0000250, CC ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:12177059, CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:17085597, CC ECO:0000269|PubMed:19172738}. CC -!- INTERACTION: CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267; CC P49407:ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313; CC P32121:ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559; CC P22681:CBL; NbExp=6; IntAct=EBI-359854, EBI-518228; CC O94921:CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945; CC P46527:CDKN1B; NbExp=4; IntAct=EBI-359854, EBI-519280; CC P67828:CSNK1A1 (xeno); NbExp=2; IntAct=EBI-359854, EBI-7540603; CC P00533:EGFR; NbExp=6; IntAct=EBI-359854, EBI-297353; CC P23945:FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239; CC Q14678:KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221; CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812; CC Q5S007:LRRK2; NbExp=8; IntAct=EBI-359854, EBI-5323863; CC P04049:RAF1; NbExp=3; IntAct=EBI-359854, EBI-365996; CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359854, EBI-6930266; CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387; CC A1L4B6:TRIM42; NbExp=3; IntAct=EBI-359854, EBI-10172216; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally CC transported to the nerve terminals. CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and CC pancreas, and at lower levels in kidney and placenta. Up-regulated CC in the lumbar spinal cord from patients with sporadic amyotrophic CC lateral sclerosis (ALS) compared with controls, with highest CC levels of expression in individuals with predominant lower motor CC neuron involvement. {ECO:0000269|PubMed:11080204}. CC -!- PTM: Ser-232 is probably phosphorylated by CK1. CC {ECO:0000269|PubMed:9360956}. CC -!- SIMILARITY: Belongs to the 14-3-3 family. {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; X56468; CAA39840.1; -; mRNA. DR EMBL; X57347; CAA40622.1; -; mRNA. DR EMBL; BT020014; AAV38817.1; -; mRNA. DR EMBL; CH471053; EAX00977.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00979.1; -; Genomic_DNA. DR EMBL; BC050601; AAH50601.1; -; mRNA. DR EMBL; BC056867; AAH56867.1; -; mRNA. DR EMBL; BC093019; AAH93019.1; -; mRNA. DR EMBL; AF070556; AAC28640.1; -; mRNA. DR CCDS; CCDS1666.1; -. DR PIR; S15076; S15076. DR RefSeq; NP_006817.1; NM_006826.3. DR UniGene; Hs.74405; -. DR PDB; 2BTP; X-ray; 2.80 A; A/B=1-234. DR PDBsum; 2BTP; -. DR ProteinModelPortal; P27348; -. DR SMR; P27348; 1-230. DR BioGrid; 116168; 395. DR DIP; DIP-27584N; -. DR IntAct; P27348; 88. DR MINT; MINT-121282; -. DR STRING; 9606.ENSP00000238081; -. DR PhosphoSite; P27348; -. DR DMDM; 112690; -. DR OGP; P27348; -. DR REPRODUCTION-2DPAGE; IPI00018146; -. DR MaxQB; P27348; -. DR PaxDb; P27348; -. DR PeptideAtlas; P27348; -. DR PRIDE; P27348; -. DR DNASU; 10971; -. DR Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308. DR Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308. DR GeneID; 10971; -. DR KEGG; hsa:10971; -. DR UCSC; uc002qzx.3; human. DR CTD; 10971; -. DR GeneCards; GC02M009724; -. DR H-InvDB; HIX0077146; -. DR HGNC; HGNC:12854; YWHAQ. DR HPA; CAB010286; -. DR HPA; HPA007925; -. DR MIM; 609009; gene. DR neXtProt; NX_P27348; -. DR PharmGKB; PA37443; -. DR eggNOG; COG5040; -. DR GeneTree; ENSGT00760000119116; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P27348; -. DR KO; K16197; -. DR OMA; SGDDRKQ; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P27348; -. DR TreeFam; TF102002; -. DR Reactome; REACT_147867; Translocation of GLUT4 to the plasma membrane. DR Reactome; REACT_355377; TP53 Regulates Metabolic Genes. DR Reactome; REACT_355542; RHO GTPases activate PKNs. DR Reactome; REACT_407; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Reactome; REACT_549; Activation of BAD and translocation to mitochondria. DR SignaLink; P27348; -. DR ChiTaRS; YWHAQ; human. DR EvolutionaryTrace; P27348; -. DR GeneWiki; YWHAQ; -. DR GenomeRNAi; 10971; -. DR NextBio; 41686; -. DR PMAP-CutDB; P27348; -. DR PRO; PR:P27348; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; P27348; -. DR CleanEx; HS_YWHAQ; -. DR ExpressionAtlas; P27348; baseline and differential. DR Genevisible; P27348; HS. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043234; C:protein complex; IDA:MGI. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0012501; P:programmed cell death; TAS:Reactome. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Nitration; Phosphoprotein; KW Reference proteome. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058636. FT SITE 56 56 Interaction with phosphoserine on FT interacting protein. FT SITE 127 127 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000269|PubMed:19608861, FT ECO:0000269|PubMed:22814378, FT ECO:0000269|Ref.7}. FT MOD_RES 3 3 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 49 49 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 68 68 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 82 82 Nitrated tyrosine. FT {ECO:0000250|UniProtKB:Q9CQV8}. FT MOD_RES 104 104 Nitrated tyrosine. FT {ECO:0000250|UniProtKB:Q9CQV8}. FT MOD_RES 115 115 N6-acetyllysine. FT {ECO:0000269|PubMed:19608861}. FT MOD_RES 232 232 Phosphoserine. FT {ECO:0000269|PubMed:18669648, FT ECO:0000269|PubMed:9360956}. FT CONFLICT 136 136 D -> N (in Ref. 3; AAV38817). FT {ECO:0000305}. FT HELIX 3 15 {ECO:0000244|PDB:2BTP}. FT HELIX 19 31 {ECO:0000244|PDB:2BTP}. FT HELIX 38 68 {ECO:0000244|PDB:2BTP}. FT HELIX 75 103 {ECO:0000244|PDB:2BTP}. FT TURN 104 108 {ECO:0000244|PDB:2BTP}. FT HELIX 112 132 {ECO:0000244|PDB:2BTP}. FT HELIX 135 159 {ECO:0000244|PDB:2BTP}. FT HELIX 165 180 {ECO:0000244|PDB:2BTP}. FT HELIX 185 201 {ECO:0000244|PDB:2BTP}. FT TURN 202 205 {ECO:0000244|PDB:2BTP}. FT HELIX 208 227 {ECO:0000244|PDB:2BTP}. SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN //