GenomeNet

Database: UniProt
Entry: Q15814
LinkDB: Q15814
Original site: Q15814 
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   11-DEC-2019, entry version 151.
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   -!- 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}.
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   SMR; Q15814; -.
DR   BioGrid; 112766; 2.
DR   DIP; DIP-46388N; -.
DR   IntAct; Q15814; 2.
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   DNASU; 6903; -.
DR   Ensembl; ENST00000372876; ENSP00000361967; ENSG00000124659.
DR   GeneID; 6903; -.
DR   KEGG; hsa:6903; -.
DR   UCSC; uc003osl.4; human.
DR   CTD; 6903; -.
DR   DisGeNET; 6903; -.
DR   EuPathDB; HostDB:ENSG00000124659.6; -.
DR   GeneCards; TBCC; -.
DR   HGNC; HGNC:11580; TBCC.
DR   HPA; HPA035073; -.
DR   HPA; HPA035074; -.
DR   MIM; 602971; gene.
DR   neXtProt; NX_Q15814; -.
DR   OpenTargets; ENSG00000124659; -.
DR   PharmGKB; PA36344; -.
DR   eggNOG; KOG2512; Eukaryota.
DR   eggNOG; ENOG410Y28B; LUCA.
DR   GeneTree; ENSGT00940000162058; -.
DR   HOGENOM; HOG000030935; -.
DR   InParanoid; Q15814; -.
DR   KO; K21766; -.
DR   OMA; CQQLRLH; -.
DR   OrthoDB; 1618114at2759; -.
DR   PhylomeDB; Q15814; -.
DR   TreeFam; TF105832; -.
DR   Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
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 216 organ(s), highest expression level in oocyte.
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:0000902; P:cell morphogenesis; 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   PIRSF; PIRSF037947; Protein_XRP2_; 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   Polymorphism; 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   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:22223895,
FT                   ECO:0000244|PubMed:22814378"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|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:0000244|PDB:2L3L"
FT   HELIX           40..43
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   HELIX           49..55
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   HELIX           56..77
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   HELIX           81..100
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   TURN            102..104
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   HELIX           107..131
FT                   /evidence="ECO:0000244|PDB:2L3L"
FT   STRAND          183..185
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          193..196
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   HELIX           198..201
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          205..208
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          215..218
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          225..229
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          234..236
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          244..248
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          253..255
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          259..265
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          270..272
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          276..283
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          285..290
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   HELIX           300..306
FT                   /evidence="ECO:0000244|PDB:2YUH"
FT   STRAND          338..340
FT                   /evidence="ECO:0000244|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
//
DBGET integrated database retrieval system