TBA_DICDI
ID TBA_DICDI Reviewed; 457 AA.
AC P32255; A0AAL2; Q54JU4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tubulin alpha chain;
DE AltName: Full=Alpha-tubulin;
GN Name=tubA; ORFNames=DDB_G0287689;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=8227212; DOI=10.1242/jcs.105.4.903;
RA Trivinos-Lagos L., Ohmachi T., Albrightson C., Burns R.G., Ennis H.L.,
RA Chisholm R.L.;
RT "The highly divergent alpha- and beta-tubulins from Dictyostelium
RT discoideum are encoded by single genes.";
RL J. Cell Sci. 105:903-911(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-428.
RC STRAIN=V34;
RX PubMed=17068267; DOI=10.1126/science.1130670;
RA Schaap P., Winckler T., Nelson M., Alvarez-Curto E., Elgie B., Hagiwara H.,
RA Cavender J., Milano-Curto A., Rozen D.E., Dingermann T., Mutzel R.,
RA Baldauf S.L.;
RT "Molecular phylogeny and evolution of morphology in the social amoebas.";
RL Science 314:661-663(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; L13999; AAC37343.1; -; mRNA.
DR EMBL; AAFI02000104; EAL63491.1; -; Genomic_DNA.
DR EMBL; AM168454; CAJ44836.1; -; Genomic_DNA.
DR RefSeq; XP_637058.1; XM_631966.1.
DR AlphaFoldDB; P32255; -.
DR SMR; P32255; -.
DR IntAct; P32255; 1.
DR STRING; 44689.DDB0191380; -.
DR PaxDb; P32255; -.
DR PRIDE; P32255; -.
DR EnsemblProtists; EAL63491; EAL63491; DDB_G0287689.
DR GeneID; 8626312; -.
DR KEGG; ddi:DDB_G0287689; -.
DR dictyBase; DDB_G0287689; tubA.
DR eggNOG; KOG1376; Eukaryota.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P32255; -.
DR OMA; KVGICYQ; -.
DR PhylomeDB; P32255; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-5617833; Cilium Assembly.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR Reactome; R-DDI-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P32255; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005813; C:centrosome; TAS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:dictyBase.
DR GO; GO:0005874; C:microtubule; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:dictyBase.
DR GO; GO:0007059; P:chromosome segregation; IDA:dictyBase.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..457
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048157"
FT BINDING 148..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 457
FT /note="Involved in polymerization"
FT VARIANT 209..210
FT /note="FM -> LV (in strain: V34)"
FT VARIANT 288
FT /note="A -> Y (in strain: V34)"
FT VARIANT 427..428
FT /note="FA -> GL (in strain: V34)"
SQ SEQUENCE 457 AA; 50961 MW; D1F2F588BF3859E6 CRC64;
MGREIISIHI GQAGVQVGNS CWELYCLEHG IERDGSIPAD RKQSSDVNNL NKDLGTFFSE
STNGKKVVPR AIFLDLEPTV IDEIRTGDYK NLFHPEQLIT GKEDAANNYA RGHYTVGKEL
IDVCVDRIRR LADQCDGLQG FLVFHSVGGG TGSGFGSLLL QKLALDYGGK KSKLDFCVYP
SPQVSTSVVE PYNSVLSTHS LLEHTDVSFM LDNEAIYNIC KNSLDIEKPT YTNLNRLIAQ
VISSLTSSLR FPGQLNLDIN DIQTNLVPFP RLHFVLCSYA PVISREKAHH ETITVDNITS
AVFSEKNIMA KCQPNLGKYM ACCLMYRGDI VPKEAQKAVQ NIRSEKSRNV SFVDWSPTGF
KCGINNQAPV STKDSEMAEV KKSVCMLSNT TAISQVFSRI NHKFDLMFVK RAFVHWYVGE
GMEEGEFAEA RDDLLALEKD YESVSASTEG EEQEEEY
