TBA_TETTH
ID TBA_TETTH Reviewed; 449 AA.
AC P41351;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tubulin alpha chain;
DE AltName: Full=Alpha-tubulin;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha chain;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8020112; DOI=10.1002/cm.970270308;
RA McGrath K.E., Yu S.M., Heruth D.P., Kelly A.A., Gorovsky M.A.;
RT "Regulation and evolution of the single alpha-tubulin gene of the ciliate
RT Tetrahymena thermophila.";
RL Cell Motil. Cytoskeleton 27:272-283(1994).
RN [2]
RP ACETYLATION AT LYS-40.
RX PubMed=7775576; DOI=10.1083/jcb.129.5.1301;
RA Gaertig J., Cruz M.A., Bowen J., Gu L., Pennock D.G., Gorovsky M.A.;
RT "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena
RT thermophila.";
RL J. Cell Biol. 129:1301-1310(1995).
RN [3]
RP GLUTAMYLATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [4]
RP GLYCYLATION.
RX PubMed=19531357; DOI=10.1016/j.devcel.2009.04.008;
RA Wloga D., Webster D.M., Rogowski K., Bre M.-H., Levilliers N.,
RA Jerka-Dziadosz M., Janke C., Dougan S.T., Gaertig J.;
RT "TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia.";
RL Dev. Cell 16:867-876(2009).
RN [5]
RP ACETYLATION AT LYS-40, AND MUTAGENESIS OF LYS-40.
RX PubMed=20829795; DOI=10.1038/nature09324;
RA Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
RA Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
RT "MEC-17 is an alpha-tubulin acetyltransferase.";
RL Nature 467:218-222(2010).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL),
CC respectively. {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Some glutamate residues at the C-terminus are either
CC polyglutamylated or polyglycylated. These 2 modifications occur
CC exclusively on glutamate residues and result in either polyglutamate or
CC polyglycine chains on the gamma-carboxyl group. Both modifications can
CC coexist on the same protein on adjacent residues, and lowering
CC polyglycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but they
CC regulate the assembly and dynamics of axonemal microtubules.
CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and
CC affects affinity and processivity of microtubule motors. This
CC modification has a role in multiple cellular functions, ranging from
CC cell motility, cell cycle progression or cell differentiation to
CC intracellular trafficking and signaling. {ECO:0000269|PubMed:20829795,
CC ECO:0000269|PubMed:7775576}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M86723; AAA21350.1; -; Genomic_DNA.
DR PDB; 5UBQ; EM; 5.70 A; A/C/E=1-441.
DR PDB; 5UCY; EM; 4.60 A; A=1-441.
DR PDB; 6U0H; EM; 4.30 A; A=1-449.
DR PDB; 6U0T; EM; 4.16 A; C/D/E/F/G/H=1-449.
DR PDB; 6U0U; EM; 4.16 A; C/D/E/F/G/H=1-449.
DR PDB; 7MOQ; EM; 8.00 A; R/S/W/r/s/w=1-449.
DR PDB; 7MWG; EM; 3.50 A; A=1-449.
DR PDB; 7N32; EM; 4.50 A; a/c/e/g/i/k/m/o/q/s/u/w=1-449.
DR PDB; 7PJE; X-ray; 1.75 A; A/C=1-449.
DR PDBsum; 5UBQ; -.
DR PDBsum; 5UCY; -.
DR PDBsum; 6U0H; -.
DR PDBsum; 6U0T; -.
DR PDBsum; 6U0U; -.
DR PDBsum; 7MOQ; -.
DR PDBsum; 7MWG; -.
DR PDBsum; 7N32; -.
DR PDBsum; 7PJE; -.
DR AlphaFoldDB; P41351; -.
DR SMR; P41351; -.
DR iPTMnet; P41351; -.
DR OMA; KVGICYQ; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR DisProt; DP01460; -.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding.
FT CHAIN 1..449
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048231"
FT CHAIN 1..448
FT /note="Detyrosinated tubulin alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P68369,
FT ECO:0000250|UniProtKB:Q71U36"
FT /id="PRO_0000437408"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 449
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20829795,
FT ECO:0000269|PubMed:7775576"
FT MUTAGEN 40
FT /note="K->R: Produces faster growing cells in medium with
FT paclitaxel, a microtubule-stabilizing drug."
FT /evidence="ECO:0000269|PubMed:20829795"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7MWG"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:7MWG"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:7MWG"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:7MWG"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7MWG"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7MWG"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:7PJE"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:7PJE"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7PJE"
FT HELIX 416..435
FT /evidence="ECO:0007829|PDB:7PJE"
SQ SEQUENCE 449 AA; 49587 MW; CE21C107A5DDA0B9 CRC64;
MREVISIHVG QGGIQVGNAC WELFCLEHGI QPDGQMPSDK TIGGGDDAFN TFFSETGAGK
HVPRAVFLDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEIVDLCLD
RIRKLADNCT GLQGFLVFNS VGGGTGSGLG SLLLERLSVD YGKKSKLGFT IYPSPQVSTA
VVEPYNSILS THSLLEHTDV AVMLDNEAIY DICRRNLDIE RPTYTNLNRL IAQVISSLTA
SLRFDGALNV DITEFQTNLV PYPRIHFMLS SYAPIISAEK AYHEQLSVAE ITNSAFEPAN
MMAKCDPRHG KYMACSMMYR GDVVPKDVNA SIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VMRAVCMISN STAIAEVFSR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGIETA EGEGEEEGY
