TBA3_CAEEL
ID TBA3_CAEEL Reviewed; 450 AA.
AC P91910; O01907; Q7JQD4; Q9TYG0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Tubulin alpha-3 chain;
DE AltName: Full=Mechanosensory abnormality protein 12;
DE Short=MEC-12;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-3 chain;
GN Name=mec-12; Synonyms=tba-3; ORFNames=C44B11.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-450,
RP FUNCTION, TISSUE SPECIFICITY, AND ACETYLATION AT LYS-40.
RC STRAIN=Bristol N2;
RX PubMed=9885292; DOI=10.1242/jcs.112.3.395;
RA Fukushige T., Siddiqui Z.K., Chou M., Culotti J.G., Gogonea C.B.,
RA Siddiqui S.S., Hamelin M.;
RT "MEC-12, an alpha-tubulin required for touch sensitivity in C. elegans.";
RL J. Cell Sci. 112:395-403(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19652181; DOI=10.1534/genetics.109.105726;
RA Bounoutas A., Zheng Q., Nonet M.L., Chalfie M.;
RT "mec-15 encodes an F-box protein required for touch receptor neuron
RT mechanosensation, synapse formation and development.";
RL Genetics 183:607-617(2009).
RN [4]
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 (Probable).
CC It binds two moles of GTP, one at an exchangeable site on the beta
CC chain and one at a non-exchangeable site on the alpha chain (Probable).
CC Component of the large-diameter neuronal microtubules which contains 15
CC protofilaments (PubMed:9885292). Plays a role in mechanosensory
CC transduction (touch sensitivity) (PubMed:9885292, PubMed:19652181).
CC {ECO:0000269|PubMed:19652181, ECO:0000269|PubMed:9885292, ECO:0000305}.
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 -!- TISSUE SPECIFICITY: Specifically expressed in neurons.
CC {ECO:0000269|PubMed:9885292}.
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: 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 -!- DISRUPTION PHENOTYPE: Touch insensitive phenotype, which may be due to
CC defective touch receptor neuron synaptic transmission.
CC {ECO:0000269|PubMed:19652181}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; U65429; AAB48241.1; -; mRNA.
DR EMBL; AB017190; BAA32600.1; -; mRNA.
DR EMBL; D21134; BAA22203.1; -; Genomic_DNA.
DR EMBL; FO080849; CCD67209.1; -; Genomic_DNA.
DR PIR; T15271; T15271.
DR RefSeq; NP_497663.1; NM_065262.5.
DR AlphaFoldDB; P91910; -.
DR SMR; P91910; -.
DR BioGRID; 40664; 19.
DR STRING; 6239.C44B11.3; -.
DR iPTMnet; P91910; -.
DR EPD; P91910; -.
DR PaxDb; P91910; -.
DR PeptideAtlas; P91910; -.
DR EnsemblMetazoa; C44B11.3.1; C44B11.3.1; WBGene00003175.
DR GeneID; 175419; -.
DR KEGG; cel:CELE_C44B11.3; -.
DR UCSC; C44B11.3; c. elegans.
DR CTD; 175419; -.
DR WormBase; C44B11.3; CE24843; WBGene00003175; mec-12.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000154457; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P91910; -.
DR OMA; FNEMGAG; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; P91910; -.
DR PRO; PR:P91910; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003175; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:WormBase.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IMP:UniProtKB.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IMP:WormBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1905789; P:positive regulation of detection of mechanical stimulus involved in sensory perception of touch; IGI:UniProtKB.
DR GO; GO:1905792; P:positive regulation of mechanosensory behavior; IGI:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:WormBase.
DR GO; GO:0001966; P:thigmotaxis; IMP:WormBase.
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 Acetylation; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin alpha-3 chain"
FT /id="PRO_0000403477"
FT CHAIN 1..449
FT /note="Detyrosinated tubulin alpha-3 chain"
FT /evidence="ECO:0000250|UniProtKB:P68369,
FT ECO:0000250|UniProtKB:Q71U36"
FT /id="PRO_0000437403"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 450
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20829795,
FT ECO:0000269|PubMed:9885292"
FT MUTAGEN 40
FT /note="K->Q,R: Reduces the touch responsiveness of the
FT worm."
FT /evidence="ECO:0000269|PubMed:20829795"
SQ SEQUENCE 450 AA; 50113 MW; CA62ABC963771DB4 CRC64;
MREVISIHIG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK SLGGSDDSFS TFFSETGSGR
HVPRAVMVDL EPTVIDEIRT GTYRSLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLTLD
RIRRLADNCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKAKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC SFMVDNEAIY DICRRNLDIE RPSYTNLNRL IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TFSPVISAEK AYHEQLSVAE ITNMCFEPHN
QMVKCDPRHG KYMAVCLLFR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VPRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGVDSM EDNGEEGDEY
