TBCC_HUMAN
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 03-AUG-2022, entry version 164.
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}.
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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; 6.
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 EPD; Q15814; -.
DR jPOST; Q15814; -.
DR MassIVE; Q15814; -.
DR MaxQB; Q15814; -.
DR PaxDb; Q15814; -.
DR PeptideAtlas; Q15814; -.
DR PRIDE; Q15814; -.
DR ProteomicsDB; 60773; -.
DR Antibodypedia; 30171; 342 antibodies from 26 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 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; CQQLRLH; -.
DR OrthoDB; 1618114at2759; -.
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; 560 hits in 1048 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 182 other tissues.
DR Genevisible; Q15814; HS.
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:0051087; F:chaperone binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
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; 1.20.58.1250; -; 1.
DR Gene3D; 2.160.20.70; -; 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; PTHR15139; 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.
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
