ID TYB4_HUMAN Reviewed; 44 AA. AC P62328; P01253; P01254; Q546P5; Q63576; Q9UE55; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Thymosin beta-4 {ECO:0000303|PubMed:3500230}; DE Short=T beta-4; DE AltName: Full=Fx {ECO:0000303|PubMed:1999398}; DE Contains: DE RecName: Full=Hemoregulatory peptide AcSDKP {ECO:0000305}; DE AltName: Full=Ac-Ser-Asp-Lys-Pro {ECO:0000303|PubMed:7694679}; DE AltName: Full=N-acetyl-SDKP; DE Short=AcSDKP {ECO:0000303|PubMed:7694679}; DE AltName: Full=Seraspenide {ECO:0000303|PubMed:7694679}; GN Name=TMSB4X; Synonyms=TB4X, THYB4, TMSB4; 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], INDUCTION, AND TISSUE SPECIFICITY. RC TISSUE=Peripheral blood leukocyte; RX PubMed=3500230; RA Gondo H., Kudo J., White J.W., Barr C., Selvanayagam P., Saunders G.F.; RT "Differential expression of the human thymosin-beta 4 gene in lymphocytes, RT macrophages, and granulocytes."; RL J. Immunol. 139:3840-3848(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16010977; DOI=10.1007/s11010-005-7642-4; RA Yang S.P., Lee H.J., Su Y.; RT "Molecular cloning and structural characterization of the functional human RT thymosin beta4 gene."; RL Mol. Cell. Biochem. 272:97-105(2005). 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 vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 2-44, FUNCTION, INTERACTION WITH ACTIN, CLEAVAGE OF RP INITIATOR METHIONINE, AND ACETYLATION AT SER-2. RX PubMed=1999398; DOI=10.1016/s0021-9258(20)64278-8; RA Safer D., Elzinga M., Nachmias V.T.; RT "Thymosin beta 4 and Fx, an actin-sequestering peptide, are RT indistinguishable."; RL J. Biol. Chem. 266:4029-4032(1991). RN [5] RP PROTEIN SEQUENCE OF 2-44, IDENTIFICATION BY MASS SPECTROMETRY, AND RP ACETYLATION AT SER-2. RC TISSUE=Tear; RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179; RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., RA Suarez T., Elortza F.; RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed RT by in silico and in vitro analyses for antimicrobial peptide RT identification."; RL J. Proteome Res. 14:2649-2658(2015). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-44, AND INDUCTION. RX PubMed=6548414; DOI=10.1016/0092-8674(84)90270-8; RA Friedman R.L., Manly S.P., McMahon M., Kerr I.M., Stark G.R.; RT "Transcriptional and posttranscriptional regulation of interferon-induced RT gene expression in human cells."; RL Cell 38:745-755(1984). RN [7] RP DEGRADATION (HEMOREGULATORY PEPTIDE ACSDKP). RX PubMed=8257427; DOI=10.1042/bj2960373; RA Rieger K.J., Saez-Servent N., Papet M.P., Wdzieczak-Bakala J., Morgat J.L., RA Thierry J., Voelter W., Lenfant M.; RT "Involvement of human plasma angiotensin I-converting enzyme in the RT degradation of the haemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl- RT proline."; RL Biochem. J. 296:373-378(1993). RN [8] RP FUNCTION (HEMOREGULATORY PEPTIDE ACSDKP). RX PubMed=7694679; RA Bonnet D., Lemoine F.M., Pontvert-Delucq S., Baillou C., Najman A., RA Guigon M.; RT "Direct and reversible inhibitory effect of the tetrapeptide acetyl-N-Ser- RT Asp-Lys-Pro (Seraspenide) on the growth of human CD34+ subpopulations in RT response to growth factors."; RL Blood 82:3307-3314(1993). RN [9] RP DEGRADATION (HEMOREGULATORY PEPTIDE ACSDKP). RX PubMed=7876104; DOI=10.1074/jbc.270.8.3656; RA Rousseau A., Michaud A., Chauvet M.T., Lenfant M., Corvol P.; RT "The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and RT specific substrate of the N-terminal active site of human angiotensin- RT converting enzyme."; RL J. Biol. Chem. 270:3656-3661(1995). RN [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-12; LYS-26; LYS-32 AND RP LYS-39, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-23; SER-31 AND THR-34, RP 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS RP 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). RN [18] RP STRUCTURE BY NMR OF WILD-TYPE AND OF MUTANTS LYS-12; SER-16 AND LEU-18 IN RP COMPLEX WITH ACTIN, AND FUNCTION. RX PubMed=10848969; DOI=10.1046/j.1432-1327.2000.01380.x; RA Simenel C., Van Troys M., Vandekerckhove J., Ampe C., Delepierre M.; RT "Structural requirements for thymosin beta4 in its contact with actin. An RT NMR-analysis of thymosin beta4 mutants in solution and correlation with RT their biological activity."; RL Eur. J. Biochem. 267:3530-3538(2000). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-44 IN COMPLEX WITH ACTA1; GSN RP AND COBL, AND SUBUNIT. RX PubMed=23009842; DOI=10.1016/j.bpj.2012.07.030; RA Durer Z.A., Kudryashov D.S., Sawaya M.R., Altenbach C., Hubbell W., RA Reisler E.; RT "Structural states and dynamics of the D-loop in actin."; RL Biophys. J. 103:930-939(2012). CC -!- FUNCTION: Plays an important role in the organization of the CC cytoskeleton (PubMed:1999398, PubMed:10848969). Binds to and sequesters CC actin monomers (G actin) and therefore inhibits actin polymerization CC (PubMed:1999398, PubMed:10848969). {ECO:0000269|PubMed:10848969, CC ECO:0000269|PubMed:1999398}. CC -!- FUNCTION: [Hemoregulatory peptide AcSDKP]: Potent inhibitor of bone CC marrow derived stem cell differentiation (PubMed:7694679). Acts by CC inhibits the entry of hematopoietic pluripotent stem cells into the S- CC phase (By similarity). {ECO:0000250|UniProtKB:P62326, CC ECO:0000269|PubMed:7694679}. CC -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND CC TMSB4X (PubMed:23009842). Interacts with SERPINB1 (By similarity). CC {ECO:0000250|UniProtKB:P62326, ECO:0000269|PubMed:23009842}. CC -!- INTERACTION: CC P62328; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-712598, EBI-357530; CC P62328; P05067: APP; NbExp=3; IntAct=EBI-712598, EBI-77613; CC P62328; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-712598, EBI-3866319; CC P62328; Q13643: FHL3; NbExp=3; IntAct=EBI-712598, EBI-741101; CC P62328; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-712598, EBI-5916454; CC P62328; O75031: HSF2BP; NbExp=3; IntAct=EBI-712598, EBI-7116203; CC P62328; Q15323: KRT31; NbExp=3; IntAct=EBI-712598, EBI-948001; CC P62328; O76011: KRT34; NbExp=3; IntAct=EBI-712598, EBI-1047093; CC P62328; O76013-2: KRT36; NbExp=3; IntAct=EBI-712598, EBI-11958506; CC P62328; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-712598, EBI-10261141; CC P62328; P40692: MLH1; NbExp=16; IntAct=EBI-712598, EBI-744248; CC P62328; Q8TAS1-2: UHMK1; NbExp=3; IntAct=EBI-712598, EBI-12157345; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:1999398}. CC -!- TISSUE SPECIFICITY: Expressed in several hemopoietic cell lines and CC lymphoid malignant cells. Decreased levels in myeloma cells. CC {ECO:0000269|PubMed:3500230}. CC -!- INDUCTION: By alpha interferons. Decreased levels in THP-1 cells after CC treatment with recombinant interferon-lambda. CC {ECO:0000269|PubMed:3500230, ECO:0000269|PubMed:6548414}. CC -!- PTM: [Hemoregulatory peptide AcSDKP]: AcSDKP is inactivated by ACE, CC which removes the dipeptide Lys-Pro from its C-terminus. CC {ECO:0000269|PubMed:7876104, ECO:0000269|PubMed:8257427}. CC -!- SIMILARITY: Belongs to the thymosin beta 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; M17733; AAA36745.1; -; mRNA. DR EMBL; AJ295158; CAC43317.1; -; Genomic_DNA. DR EMBL; BT007090; AAP35753.1; -; mRNA. DR EMBL; X02493; CAA26323.1; -; mRNA. DR CCDS; CCDS35202.1; -. DR PIR; I56000; A38682. DR RefSeq; NP_066932.1; NM_021109.3. DR PDB; 3TU5; X-ray; 3.00 A; B=21-44. DR PDB; 4PL7; X-ray; 2.30 A; A/B=2-44. DR PDB; 4PL8; X-ray; 2.00 A; H=2-44. DR PDBsum; 3TU5; -. DR PDBsum; 4PL7; -. DR PDBsum; 4PL8; -. DR AlphaFoldDB; P62328; -. DR BMRB; P62328; -. DR SMR; P62328; -. DR BioGRID; 112969; 52. DR IntAct; P62328; 46. DR MINT; P62328; -. DR STRING; 9606.ENSP00000370010; -. DR MoonDB; P62328; Curated. DR MoonProt; P62328; -. DR GlyGen; P62328; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62328; -. DR PhosphoSitePlus; P62328; -. DR BioMuta; TMSB4X; -. DR DMDM; 78103211; -. DR DOSAC-COBS-2DPAGE; P62328; -. DR EPD; P62328; -. DR jPOST; P62328; -. DR MassIVE; P62328; -. DR MaxQB; P62328; -. DR PaxDb; 9606-ENSP00000370010; -. DR PeptideAtlas; P62328; -. DR ProteomicsDB; 57395; -. DR Pumba; P62328; -. DR TopDownProteomics; P62328; -. DR Antibodypedia; 8508; 301 antibodies from 28 providers. DR DNASU; 7114; -. DR Ensembl; ENST00000380633.1; ENSP00000370007.1; ENSG00000205542.11. DR Ensembl; ENST00000380635.5; ENSP00000370009.1; ENSG00000205542.11. DR Ensembl; ENST00000380636.1; ENSP00000370010.1; ENSG00000205542.11. DR Ensembl; ENST00000451311.7; ENSP00000414376.2; ENSG00000205542.11. DR GeneID; 7114; -. DR KEGG; hsa:7114; -. DR MANE-Select; ENST00000451311.7; ENSP00000414376.2; NM_021109.4; NP_066932.1. DR UCSC; uc004cvf.4; human. DR AGR; HGNC:11881; -. DR CTD; 7114; -. DR DisGeNET; 7114; -. DR GeneCards; TMSB4X; -. DR HGNC; HGNC:11881; TMSB4X. DR HPA; ENSG00000205542; Low tissue specificity. DR MIM; 300159; gene. DR neXtProt; NX_P62328; -. DR OpenTargets; ENSG00000205542; -. DR PharmGKB; PA36581; -. DR VEuPathDB; HostDB:ENSG00000205542; -. DR eggNOG; KOG4794; Eukaryota. DR GeneTree; ENSGT00940000154433; -. DR HOGENOM; CLU_208046_0_0_1; -. DR InParanoid; P62328; -. DR OrthoDB; 4727927at2759; -. DR PhylomeDB; P62328; -. DR PathwayCommons; P62328; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; P62328; -. DR BioGRID-ORCS; 7114; 9 hits in 709 CRISPR screens. DR ChiTaRS; TMSB4X; human. DR GeneWiki; Thymosin_beta-4; -. DR GenomeRNAi; 7114; -. DR Pharos; P62328; Tbio. DR PRO; PR:P62328; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000205542; Expressed in monocyte and 96 other cell types or tissues. DR ExpressionAtlas; P62328; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:CAFA. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0003785; F:actin monomer binding; IDA:CAFA. DR GO; GO:0019899; F:enzyme binding; IPI:CAFA. DR GO; GO:0140311; F:protein sequestering activity; IMP:CAFA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007015; P:actin filament organization; IEA:InterPro. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IMP:CAFA. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:CAFA. DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IDA:CAFA. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:CAFA. DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IDA:CAFA. DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; IDA:CAFA. DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central. DR GO; GO:0042989; P:sequestering of actin monomers; IDA:CAFA. DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:CAFA. DR CDD; cd22059; WH2_BetaT; 1. DR DisProt; DP00357; -. DR Gene3D; 1.20.5.520; Single helix bin; 1. DR InterPro; IPR001152; Beta-thymosin. DR InterPro; IPR038386; Beta-thymosin_sf. DR PANTHER; PTHR12021; THYMOSIN BETA; 1. DR PANTHER; PTHR12021:SF3; THYMOSIN BETA-4; 1. DR Pfam; PF01290; Thymosin; 1. DR PIRSF; PIRSF001828; Thymosin_beta; 1. DR SMART; SM00152; THY; 1. DR PROSITE; PS00500; THYMOSIN_B4; 1. DR Genevisible; P62328; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1999398, FT ECO:0000269|PubMed:25946035, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895" FT CHAIN 2..44 FT /note="Thymosin beta-4" FT /evidence="ECO:0000269|PubMed:25946035" FT /id="PRO_0000045920" FT PEPTIDE 2..5 FT /note="Hemoregulatory peptide AcSDKP" FT /evidence="ECO:0000305|PubMed:7694679" FT /id="PRO_0000034295" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:1999398, FT ECO:0000269|PubMed:25946035, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 4 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 12 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 23 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 26 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 32 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 34 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 39 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 12 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 12 FT /note="K->P: Very weak actin binding; no inhibition of FT actin polymerization." FT MUTAGEN 16 FT /note="S->A: Binds actin 2.5-fold less than wild-type; FT little change in inhibition of actin polymerization." FT MUTAGEN 16 FT /note="S->AS: Very weak actin binding; no inhibition of FT actin polymerization." FT MUTAGEN 18 FT /note="L->A,P: Very weak actin binding; no inhibition of FT actin polymerization." FT HELIX 6..11 FT /evidence="ECO:0007829|PDB:4PL8" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:4PL8" FT HELIX 32..39 FT /evidence="ECO:0007829|PDB:4PL7" SQ SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64; MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES //