TBA_PLAYO
ID TBA_PLAYO Reviewed; 453 AA.
AC P12543; Q7RQE4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Tubulin alpha chain;
GN ORFNames=PY01155;
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL;
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 254-450.
RX PubMed=2459618; DOI=10.1016/0166-6851(88)90109-0;
RA Akella R., Arasu P., Vaidya A.B.;
RT "Molecular clones of alpha-tubulin genes of Plasmodium yoelii reveal an
RT unusual feature of the carboxy terminus.";
RL Mol. Biochem. Parasitol. 30:165-174(1988).
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; AABL01000303; EAA20444.1; -; Genomic_DNA.
DR EMBL; M29816; AAA29779.1; -; mRNA.
DR AlphaFoldDB; P12543; -.
DR SMR; P12543; -.
DR STRING; 73239.P12543; -.
DR PRIDE; P12543; -.
DR EnsemblProtists; EAA20444; EAA20444; EAA20444.
DR InParanoid; P12543; -.
DR OMA; VDNEACY; -.
DR Proteomes; UP000008553; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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 Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..453
FT /note="Tubulin alpha chain"
FT /id="PRO_0000048218"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 453
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
FT CONFLICT 276
FT /note="V -> I (in Ref. 2; AAA29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="N -> S (in Ref. 2; AAA29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="T -> S (in Ref. 2; AAA29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..393
FT /note="MDQ -> IWP (in Ref. 2; AAA29779)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="K -> M (in Ref. 2; AAA29779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50207 MW; FEAC58ECE62DB035 CRC64;
MREVISIHVG QAGIQVGNAC WELFCLEHGI QPDGQMPPDQ AGRANDDAFN TFFSETGAGK
HVPRCVFVDL EPTVVDEVRT GTYRQLFHPE QLISGKEDAA NNFARGHYTI GKEVIDVCLD
RIRKLADNCT GLQGFLMFSA VGGGTGSGFG CLMLERLSVD YGKKSKLNFC CWPSPQVSTA
VVEPYNSVLS THSLLEHTDV AIMLDNEAIY DICKKNLDIE RPTYTNLNRL IAQVISSLTA
SLRFDGALNV DVTEFQTNLV PYPRIHFMLS SYAPVVSAEK AYHEQLSVSE ITNSAFEPAN
MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVATIKTKRT IQFVDWCPTG FKCGINYQPP
TVVPGGDLAK VMRAVCMISN STAIAEVFSR MDQKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGIETN DGEGEDEGYE ADY
