TBB_PLAF7
ID TBB_PLAF7 Reviewed; 445 AA.
AC Q7KQL5; A0A143ZWL7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN ORFNames=PF10_0084, PF3D7_1008700;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=33633135; DOI=10.1038/s41598-021-83513-5;
RA Chakrabarti M., Joshi N., Kumari G., Singh P., Shoaib R., Munjal A.,
RA Kumar V., Behl A., Abid M., Garg S., Gupta S., Singh S.;
RT "Interaction of Plasmodium falciparum apicortin with alpha- and beta-
RT tubulin is critical for parasite growth and survival.";
RL Sci. Rep. 11:4688-4688(2021).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules
CC (PubMed:33633135). It binds two moles of GTP, one at an exchangeable
CC site on the beta chain and one at a non-exchangeable site on the alpha
CC chain (Probable). {ECO:0000269|PubMed:33633135, ECO:0000305}.
CC -!- SUBUNIT: Dimer of alpha and beta chains (Probable). A typical
CC microtubule is a hollow water-filled tube with an outer diameter of 25
CC nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate
CC head-to-tail to form protofilaments running lengthwise along the
CC microtubule wall with the beta-tubulin subunit facing the microtubule
CC plus end conferring a structural polarity. Microtubules usually have 13
CC protofilaments but different protofilament numbers can be found in some
CC organisms and specialized cells (Probable). Interacts with
CC DCX/apicortin; the interaction stabilizes microtubule assembly
CC (PubMed:33633135). {ECO:0000269|PubMed:33633135, ECO:0000305,
CC ECO:0000305|PubMed:33633135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:33633135}. Note=Localizes to the parasite surface
CC in subpellicular regions in trophozoites and schizonts
CC (PubMed:33633135). In merozoites, localize to the apical end of the
CC parasite (PubMed:33633135). {ECO:0000269|PubMed:33633135}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC including in trophozoites, schizonts and free merozoites (at protein
CC level). {ECO:0000269|PubMed:33633135}.
CC -!- MISCELLANEOUS: Tamoxifen used to treat breast cancer blocks the
CC interaction between apicortin and, alpha-tubulin 1 and beta-tubulin
CC resulting in microtubule destabilization.
CC {ECO:0000269|PubMed:33633135}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; LN999944; CZT98336.1; -; Genomic_DNA.
DR RefSeq; XP_001347369.1; XM_001347333.1.
DR AlphaFoldDB; Q7KQL5; -.
DR SMR; Q7KQL5; -.
DR BioGRID; 1205665; 2.
DR IntAct; Q7KQL5; 2.
DR STRING; 5833.PF10_0084; -.
DR DrugBank; DB11638; Artenimol.
DR SwissPalm; Q7KQL5; -.
DR PRIDE; Q7KQL5; -.
DR EnsemblProtists; CZT98336; CZT98336; PF3D7_1008700.
DR GeneID; 810242; -.
DR KEGG; pfa:PF3D7_1008700; -.
DR VEuPathDB; PlasmoDB:PF3D7_1008700; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q7KQL5; -.
DR OMA; VCSVAPK; -.
DR PhylomeDB; Q7KQL5; -.
DR Reactome; R-PFA-5617833; Cilium Assembly.
DR Reactome; R-PFA-6798695; Neutrophil degranulation.
DR Reactome; R-PFA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-PFA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000001450; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISS:GeneDB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:GeneDB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:GeneDB.
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; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PR01163; BETATUBULIN.
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.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Tubulin beta chain"
FT /id="PRO_0000233402"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 49751 MW; 15A33134F357FFDE CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGTYCGDS DLQLERVDVF YNEATGGRYV
PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDAVLDVV
RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKIREEYP DRIMETFSVF PSPKVSDTVV
EPYNATLSVH QLVENADEVQ VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCSL
RFPGQLNSDL RKLAVNLIPF PRLHFFMIGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
CASDPRHGRY LTACAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPHNTK SSVCDIPPKG
LKMAVTFVGN STAIQEMFKR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEE GDVEA
