ID TBCC_HUMAN Reviewed; 346 AA. AC Q15814; Q53Y43; Q5T787; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 29-MAY-2024, entry version 173. DE RecName: Full=Tubulin-specific chaperone C; DE AltName: Full=Tubulin-folding cofactor C; DE Short=CFC; GN Name=TBCC; 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], AND VARIANT ALA-65. RX PubMed=8706133; DOI=10.1016/s0092-8674(00)80100-2; RA Tian G., Huang Y., Rommelaere H., Vandekerckhove J., Ampe C., Cowan N.J.; RT "Pathway leading to correctly folded beta-tubulin."; RL Cell 86:287-296(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-65. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-65. 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]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-65. RC TISSUE=Eye, and Lung; 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 FUNCTION, AND MUTAGENESIS OF ARG-262. RX PubMed=11847227; DOI=10.1074/jbc.m200128200; RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., RA Cowan N.J.; RT "Functional overlap between retinitis pigmentosa 2 protein and the tubulin- RT specific chaperone cofactor C."; RL J. Biol. Chem. 277:14629-14634(2002). RN [7] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12417528; DOI=10.1093/hmg/11.24.3065; RA Grayson C., Bartolini F., Chapple J.P., Willison K.R., Bhamidipati A., RA Lewis S.A., Luthert P.J., Hardcastle A.J., Cowan N.J., Cheetham M.E.; RT "Localization in the human retina of the X-linked retinitis pigmentosa RT protein RP2, its homologue cofactor C and the RP2 interacting protein RT Arl3."; RL Hum. Mol. Genet. 11:3065-3074(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, 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 [9] RP IDENTIFICATION BY MASS 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-168, AND RP 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 [15] RP STRUCTURE BY NMR OF 181-346. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C-terminal region in human tubulin folding RT cofactor C."; RL Submitted (APR-2008) to the PDB data bank. RN [16] RP VARIANT ASP-86. RX PubMed=22100072; DOI=10.1016/j.ajhg.2011.10.011; RA Aldahmesh M.A., Mohamed J.Y., Alkuraya H.S., Verma I.C., Puri R.D., RA Alaiya A.A., Rizzo W.B., Alkuraya F.S.; RT "Recessive mutations in ELOVL4 cause ichthyosis, intellectual disability, RT and spastic quadriplegia."; RL Am. J. Hum. Genet. 89:745-750(2011). CC -!- FUNCTION: Tubulin-folding protein; involved in the final step of the CC tubulin folding pathway. {ECO:0000269|PubMed:11847227}. CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D CC function by capturing and stabilizing tubulin in a quasi-native CC conformation. Cofactor E binds to the cofactor D-tubulin complex; CC interaction with cofactor C then causes the release of tubulin CC polypeptides that are committed to the native state. CC -!- INTERACTION: CC Q15814; P28329-3: CHAT; NbExp=3; IntAct=EBI-15695297, EBI-25837549; CC Q15814; P22607: FGFR3; NbExp=3; IntAct=EBI-15695297, EBI-348399; CC Q15814; P06396: GSN; NbExp=3; IntAct=EBI-15695297, EBI-351506; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12417528}. CC Note=Detected predominantly in the photoreceptor connecting cilium. CC -!- TISSUE SPECIFICITY: Expressed in the retina. Expressed in the rod and CC cone photoreceptors, extending from the inner segments (IS), through CC the outer nuclear layer (ONL) and into the synapses in the outer CC plexiform layer (OPL). Strongly expressed to the photoreceptor CC connecting cilium at the tips of the IS (at protein level). CC {ECO:0000269|PubMed:12417528}. CC -!- SIMILARITY: Belongs to the TBCC 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; U61234; AAB17539.1; -; mRNA. DR EMBL; BT007002; AAP35648.1; -; mRNA. DR EMBL; AK312681; BAG35561.1; -; mRNA. DR EMBL; AL353716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017479; AAH17479.1; -; mRNA. DR EMBL; BC020170; AAH20170.1; -; mRNA. DR CCDS; CCDS4872.1; -. DR RefSeq; NP_003183.1; NM_003192.2. DR PDB; 2L3L; NMR; -; A=26-135. DR PDB; 2YUH; NMR; -; A=181-346. DR PDBsum; 2L3L; -. DR PDBsum; 2YUH; -. DR AlphaFoldDB; Q15814; -. DR BMRB; Q15814; -. DR SMR; Q15814; -. DR BioGRID; 112766; 13. DR DIP; DIP-46388N; -. DR IntAct; Q15814; 5. DR STRING; 9606.ENSP00000361967; -. DR iPTMnet; Q15814; -. DR PhosphoSitePlus; Q15814; -. DR BioMuta; TBCC; -. DR DMDM; 313104020; -. DR jPOST; Q15814; -. DR MassIVE; Q15814; -. DR PaxDb; 9606-ENSP00000361967; -. DR PeptideAtlas; Q15814; -. DR ProteomicsDB; 60773; -. DR Pumba; Q15814; -. DR Antibodypedia; 30171; 384 antibodies from 27 providers. DR DNASU; 6903; -. DR Ensembl; ENST00000372876.2; ENSP00000361967.1; ENSG00000124659.7. DR GeneID; 6903; -. DR KEGG; hsa:6903; -. DR MANE-Select; ENST00000372876.2; ENSP00000361967.1; NM_003192.3; NP_003183.2. DR UCSC; uc003osl.4; human. DR AGR; HGNC:11580; -. DR CTD; 6903; -. DR DisGeNET; 6903; -. DR GeneCards; TBCC; -. DR HGNC; HGNC:11580; TBCC. DR HPA; ENSG00000124659; Low tissue specificity. DR MIM; 602971; gene. DR neXtProt; NX_Q15814; -. DR OpenTargets; ENSG00000124659; -. DR PharmGKB; PA36344; -. DR VEuPathDB; HostDB:ENSG00000124659; -. DR eggNOG; KOG2512; Eukaryota. DR GeneTree; ENSGT00940000162058; -. DR HOGENOM; CLU_032612_2_1_1; -. DR InParanoid; Q15814; -. DR OMA; YFQHEIT; -. DR OrthoDB; 127089at2759; -. DR PhylomeDB; Q15814; -. DR TreeFam; TF105832; -. DR PathwayCommons; Q15814; -. DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway. DR SignaLink; Q15814; -. DR BioGRID-ORCS; 6903; 594 hits in 1124 CRISPR screens. DR ChiTaRS; TBCC; human. DR EvolutionaryTrace; Q15814; -. DR GenomeRNAi; 6903; -. DR Pharos; Q15814; Tbio. DR PRO; PR:Q15814; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q15814; Protein. DR Bgee; ENSG00000124659; Expressed in oocyte and 184 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005874; C:microtubule; TAS:ProtInc. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; TAS:ProtInc. DR GO; GO:0015631; F:tubulin binding; IEA:InterPro. DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IDA:UniProtKB. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central. DR Gene3D; 2.160.20.70; -; 1. DR Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1. DR InterPro; IPR017901; C-CAP_CF_C-like. DR InterPro; IPR016098; CAP/MinC_C. DR InterPro; IPR006599; CARP_motif. DR InterPro; IPR027684; TBCC. DR InterPro; IPR031925; TBCC_N. DR InterPro; IPR038397; TBCC_N_sf. DR InterPro; IPR012945; Tubulin-bd_cofactor_C_dom. DR PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1. DR PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1. DR Pfam; PF07986; TBCC; 1. DR Pfam; PF16752; TBCC_N; 1. DR SMART; SM00673; CARP; 2. DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1. DR EPD; Q15814; -. DR MaxQB; Q15814; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Phosphoprotein; KW Reference proteome. FT CHAIN 1..346 FT /note="Tubulin-specific chaperone C" FT /id="PRO_0000080046" FT DOMAIN 171..323 FT /note="C-CAP/cofactor C-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 140..171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT VARIANT 65 FT /note="V -> A (in dbSNP:rs2234026)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8706133, FT ECO:0000269|Ref.2" FT /id="VAR_026822" FT VARIANT 86 FT /note="E -> D (in dbSNP:rs144361927)" FT /evidence="ECO:0000269|PubMed:22100072" FT /id="VAR_067423" FT VARIANT 157 FT /note="G -> D (in dbSNP:rs7742995)" FT /id="VAR_026823" FT VARIANT 169 FT /note="P -> S (in dbSNP:rs2234027)" FT /id="VAR_020448" FT VARIANT 180 FT /note="P -> S (in dbSNP:rs2234028)" FT /id="VAR_024653" FT VARIANT 279 FT /note="A -> T (in dbSNP:rs12175072)" FT /id="VAR_026824" FT MUTAGEN 262 FT /note="R->A: Inhibits stimulation of tubulin GTPase FT activity." FT /evidence="ECO:0000269|PubMed:11847227" FT HELIX 32..37 FT /evidence="ECO:0007829|PDB:2L3L" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:2L3L" FT HELIX 49..55 FT /evidence="ECO:0007829|PDB:2L3L" FT HELIX 56..77 FT /evidence="ECO:0007829|PDB:2L3L" FT HELIX 81..100 FT /evidence="ECO:0007829|PDB:2L3L" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:2L3L" FT HELIX 107..131 FT /evidence="ECO:0007829|PDB:2L3L" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:2YUH" FT HELIX 198..201 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 276..283 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:2YUH" FT HELIX 300..306 FT /evidence="ECO:0007829|PDB:2YUH" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:2YUH" SQ SEQUENCE 346 AA; 39248 MW; 32732BB3411FCD20 CRC64; MESVSCSAAA VRTGDMESQR DLSLVPERLQ RREQERQLEV ERRKQKRQNQ EVEKENSHFF VATFVRERAA VEELLERAES VERLEEAASR LQGLQKLIND SVFFLAAYDL RQGQEALARL QAALAERRRG LQPKKRFAFK TRGKDAASST KVDAAPGIPP AVESIQDSPL PKKAEGDLGP SWVCGFSNLE SQVLEKRASE LHQRDVLLTE LSNCTVRLYG NPNTLRLTKA HSCKLLCGPV STSVFLEDCS DCVLAVACQQ LRIHSTKDTR IFLQVTSRAI VEDCSGIQFA PYTWSYPEID KDFESSGLDR SKNNWNDVDD FNWLARDMAS PNWSILPEEE RNIQWD //