TBA_XENTR
ID TBA_XENTR Reviewed; 449 AA.
AC Q28IX8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Tubulin alpha chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha chain;
GN Name=tuba; Synonyms=tuba1; ORFNames=TNeu063j16.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P68363}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. The precise function of polyglycylation is still unclear.
CC {ECO:0000250|UniProtKB:P68369}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group (By
CC similarity). Polyglutamylation plays a key role in microtubule severing
CC by spastin (SPAST). SPAST preferentially recognizes and acts on
CC microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC microtubule lumen. This modification has been correlated with increased
CC microtubule stability, intracellular transport and ciliary assembly.
CC {ECO:0000250|UniProtKB:Q71U36}.
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 (vash1 or vash2) and tubulin tyrosine ligase
CC (TTL), respectively. {ECO:0000250|UniProtKB:P68369,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Tubulin alpha chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly microtubule plus-end tracking proteins.
CC Tyrosinated tubulins regulate the initiation of dynein-driven motility.
CC {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
CC -!- PTM: [Detyrosinated tubulin alpha chain]: Detyrosination is involved in
CC metaphase plate congression by guiding chromosomes during mitosis (By
CC similarity). Detyrosination increases microtubules-dependent
CC mechanotransduction in dystrophic cardiac and skeletal muscle. In
CC cardiomyocytes, detyrosinated microtubules are required to resist to
CC contractile compression during contraction (By similarity).
CC {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; CR760170; CAJ82880.1; -; mRNA.
DR RefSeq; NP_001016694.1; NM_001016694.2.
DR AlphaFoldDB; Q28IX8; -.
DR SMR; Q28IX8; -.
DR PaxDb; Q28IX8; -.
DR GeneID; 549448; -.
DR KEGG; xtr:549448; -.
DR CTD; 80086; -.
DR Xenbase; XB-GENE-489927; tuba4b.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q28IX8; -.
DR OMA; ICHLHIG; -.
DR OrthoDB; 514396at2759; -.
DR TreeFam; TF300314; -.
DR Reactome; R-XTR-114608; Platelet degranulation.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-XTR-5620924; Intraflagellar transport.
DR Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR Reactome; R-XTR-9013407; RHOH GTPase cycle.
DR Reactome; R-XTR-9646399; Aggrephagy.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond;
KW Microtubule; Nucleotide-binding; Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin alpha chain"
FT /id="PRO_0000260088"
FT CHAIN 1..448
FT /note="Detyrosinated tubulin alpha chain"
FT /evidence="ECO:0000250|UniProtKB:Q71U36"
FT /id="PRO_0000437411"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000250|UniProtKB:P68363"
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:0000250|UniProtKB:P41351,
FT ECO:0000250|UniProtKB:Q71U36"
FT MOD_RES 443
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
SQ SEQUENCE 449 AA; 50004 MW; A77D9DF62F92B6D2 CRC64;
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFSETGAGK
HVPRAVFVDL EPTVIDEVRA GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVSE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRT IQFVDWCPTG FKVGINYQPP
TAVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGIDSY EDEDEGEEY
