TBA2_CAEEL
ID TBA2_CAEEL Reviewed; 448 AA.
AC P34690; Q95QR1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tubulin alpha-2 chain;
GN Name=tba-2; ORFNames=C47B2.3;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Bristol N2;
RX PubMed=8263934; DOI=10.1006/jmbi.1993.1685;
RA Fukushige T., Yasuda H., Siddiqui S.S.;
RT "Molecular cloning and developmental expression of the alpha-2 tubulin gene
RT of Caenorhabditis elegans.";
RL J. Mol. Biol. 234:1290-1300(1993).
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).
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 -!- TISSUE SPECIFICITY: Expressed in intestine, pharyngeal muscle cells,
CC and a subset of neurons. {ECO:0000269|PubMed:8263934}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during the early (L1-L3) larval
CC stages, lower expression levels are seen in L4 larvae, adults, and
CC embryos. {ECO:0000269|PubMed:8263934}.
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}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; D14965; BAA03610.1; -; Genomic_DNA.
DR EMBL; Z99709; CAB16856.1; -; Genomic_DNA.
DR PIR; S40439; S40439.
DR RefSeq; NP_001021050.1; NM_001025879.3.
DR PDB; 6E88; EM; 4.80 A; A/C/H/I/L/M=1-434.
DR PDBsum; 6E88; -.
DR AlphaFoldDB; P34690; -.
DR SMR; P34690; -.
DR BioGRID; 38564; 23.
DR IntAct; P34690; 2.
DR STRING; 6239.C47B2.3.1; -.
DR EPD; P34690; -.
DR PaxDb; P34690; -.
DR PeptideAtlas; P34690; -.
DR PRIDE; P34690; -.
DR EnsemblMetazoa; C47B2.3.1; C47B2.3.1; WBGene00006529.
DR EnsemblMetazoa; C47B2.3.2; C47B2.3.2; WBGene00006529.
DR GeneID; 173167; -.
DR KEGG; cel:CELE_C47B2.3; -.
DR UCSC; C47B2.3.2; c. elegans.
DR CTD; 173167; -.
DR WormBase; C47B2.3; CE17563; WBGene00006529; tba-2.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000169069; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P34690; -.
DR OMA; DGTMPTQ; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; P34690; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-5617833; Cilium Assembly.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR Reactome; R-CEL-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P34690; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006529; Expressed in germ line (C elegans) and 4 other tissues.
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:0051642; P:centrosome localization; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:WormBase.
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 GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI: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 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..448
FT /note="Tubulin alpha-2 chain"
FT /id="PRO_0000048144"
FT REGION 428..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 448
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 448 AA; 49913 MW; 4B9A4A36BE12D64A CRC64;
MREVISIHVG QAGVQIGNAC WELYCLEHGI QPDGTMPTQS TNEGESFTTF FSDTGSGRYV
PRSIFVDLEP TVVDEIRTGT YKKLFHPEQM ITGKEDAANN YARGHYTVGK ELIDTVLDRI
RRLADNCSGL QGFFVFHSFG GGTGSGFTSL LMERLSVDYG KKSKLEFSIY PAPQVSTAVV
EPYNSILTTH TTLEHSDCAF MVDNEAIYDI CRRNLDVERP SYTNLNRIIS QVVSSITASL
RFDGALNVDL NEFQTNLVPY PRIHFPLAAY TPLISAEKAY HEALSVSDIT NSCFEPANQM
VKCDPRHGKY MAVCLLYRGD VVPKDVNTAI AAIKTKRTIQ FVDWCPTGFK VGINYQPPTV
VPGGDLAKVP RAVCMLSNTT AIAEAWSRLD YKFDLMYAKR AFVHWYVGEG MEEGEFTEAR
EDLAALEKDY EEVGADSNEG GEEEGEEY
