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Protein

Tubulin alpha-3 chain

Gene

mec-12

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). Component of the large-diameter neuronal microtubules which contains 15 protofilaments.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei450Involved in polymerization1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi142 – 148GTPSequence analysis7

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • structural constituent of cytoskeleton Source: WormBase

GO - Biological processi

  • mechanosensory behavior Source: WormBase
  • microtubule-based process Source: WormBase
  • response to mechanical stimulus Source: WormBase
  • thigmotaxis Source: WormBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-3 chain
Alternative name(s):
Mechanosensory abnormality protein 12
Short name:
MEC-12
Cleaved into the following chain:
Gene namesi
Name:mec-12
Synonyms:tba-3
ORF Names:C44B11.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiC44B11.3; CE24843; WBGene00003175; mec-12.

Subcellular locationi

GO - Cellular componenti

  • axon Source: WormBase
  • microtubule Source: WormBase
  • neuronal cell body Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40K → Q or R: Reduces the touch responsiveness of the worm. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004034771 – 450Tubulin alpha-3 chainAdd BLAST450
ChainiPRO_00004374031 – 449Detyrosinated tubulin alpha-3 chainBy similarityAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-acetyllysine2 Publications1

Post-translational modificationi

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.By similarity
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP91910.
PaxDbiP91910.
PeptideAtlasiP91910.
PRIDEiP91910.

Expressioni

Tissue specificityi

Specifically expressed in neurons.1 Publication

Gene expression databases

BgeeiWBGene00003175.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Protein-protein interaction databases

STRINGi6239.C44B11.3.

Structurei

3D structure databases

ProteinModelPortaliP91910.
SMRiP91910.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
InParanoidiP91910.
KOiK07374.
OMAiFSENNIM.
OrthoDBiEOG091G0736.
PhylomeDBiP91910.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P91910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREVISIHIG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK SLGGSDDSFS
60 70 80 90 100
TFFSETGSGR HVPRAVMVDL EPTVIDEIRT GTYRSLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLTLD RIRRLADNCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKAKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
SFMVDNEAIY DICRRNLDIE RPSYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TFSPVISAEK AYHEQLSVAE ITNMCFEPHN
310 320 330 340 350
QMVKCDPRHG KYMAVCLLFR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VPRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSM EDNGEEGDEY
Length:450
Mass (Da):50,113
Last modified:May 1, 1997 - v1
Checksum:iCA62ABC963771DB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65429 mRNA. Translation: AAB48241.1.
AB017190 mRNA. Translation: BAA32600.1.
D21134 Genomic DNA. Translation: BAA22203.1.
FO080849 Genomic DNA. Translation: CCD67209.1.
PIRiT15271.
RefSeqiNP_497663.1. NM_065262.5.
UniGeneiCel.17899.

Genome annotation databases

EnsemblMetazoaiC44B11.3; C44B11.3; WBGene00003175.
GeneIDi175419.
KEGGicel:CELE_C44B11.3.
UCSCiC44B11.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65429 mRNA. Translation: AAB48241.1.
AB017190 mRNA. Translation: BAA32600.1.
D21134 Genomic DNA. Translation: BAA22203.1.
FO080849 Genomic DNA. Translation: CCD67209.1.
PIRiT15271.
RefSeqiNP_497663.1. NM_065262.5.
UniGeneiCel.17899.

3D structure databases

ProteinModelPortaliP91910.
SMRiP91910.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C44B11.3.

Proteomic databases

EPDiP91910.
PaxDbiP91910.
PeptideAtlasiP91910.
PRIDEiP91910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC44B11.3; C44B11.3; WBGene00003175.
GeneIDi175419.
KEGGicel:CELE_C44B11.3.
UCSCiC44B11.3. c. elegans.

Organism-specific databases

CTDi175419.
WormBaseiC44B11.3; CE24843; WBGene00003175; mec-12.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
InParanoidiP91910.
KOiK07374.
OMAiFSENNIM.
OrthoDBiEOG091G0736.
PhylomeDBiP91910.

Miscellaneous databases

PROiP91910.

Gene expression databases

BgeeiWBGene00003175.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTBA3_CAEEL
AccessioniPrimary (citable) accession number: P91910
Secondary accession number(s): O01907, Q7JQD4, Q9TYG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.