TBB_PLAFA
ID TBB_PLAFA Reviewed; 445 AA.
AC P14140;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2181306; DOI=10.1016/0166-6851(90)90056-r;
RA Sen K., Godson G.N.;
RT "Isolation of alpha- and beta-tubulin genes of Plasmodium falciparum using
RT a single oligonucleotide probe.";
RL Mol. Biochem. Parasitol. 39:173-182(1990).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules (By
CC similarity). It binds two moles of GTP, one at an exchangeable site on
CC the beta chain and one at a non-exchangeable site on the alpha chain
CC (Probable). {ECO:0000250|UniProtKB:Q7KQL5, ECO:0000305}.
CC -!- SUBUNIT: Dimer of alpha and beta chains (By similarity). 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q7KQL5, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7KQL5}. Note=Localizes to the parasite surface
CC in subpellicular regions in trophozoites and schizonts (By similarity).
CC In merozoites, localize to the apical end of the parasite (By
CC similarity). {ECO:0000250|UniProtKB:Q7KQL5}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M28398; AAA29780.1; -; Genomic_DNA.
DR PIR; A44949; A44949.
DR AlphaFoldDB; P14140; -.
DR SMR; P14140; -.
DR VEuPathDB; PlasmoDB:PF3D7_1008700; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000294400; -.
DR VEuPathDB; PlasmoDB:Pf7G8_100013100; -.
DR VEuPathDB; PlasmoDB:PfCD01_100013900; -.
DR VEuPathDB; PlasmoDB:PfDd2_100014000; -.
DR VEuPathDB; PlasmoDB:PfGA01_100014000; -.
DR VEuPathDB; PlasmoDB:PfGB4_100013700; -.
DR VEuPathDB; PlasmoDB:PfGN01_100014300; -.
DR VEuPathDB; PlasmoDB:PfHB3_100013100; -.
DR VEuPathDB; PlasmoDB:PfIT_100012700; -.
DR VEuPathDB; PlasmoDB:PfKE01_100014000; -.
DR VEuPathDB; PlasmoDB:PfKH01_100013300; -.
DR VEuPathDB; PlasmoDB:PfKH02_100014100; -.
DR VEuPathDB; PlasmoDB:PfML01_100013000; -.
DR VEuPathDB; PlasmoDB:PfNF135_100014200; -.
DR VEuPathDB; PlasmoDB:PfNF166_100013700; -.
DR VEuPathDB; PlasmoDB:PfNF54_100013900; -.
DR VEuPathDB; PlasmoDB:PfSD01_100013400; -.
DR VEuPathDB; PlasmoDB:PfSN01_100014100; -.
DR VEuPathDB; PlasmoDB:PfTG01_100013900; -.
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; 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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT CHAIN 1..445
FT /note="Tubulin beta chain"
FT /id="PRO_0000048311"
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; 49814 MW; FA37B0ECEDDE05B3 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGTYSGDS DLQLERVDVF YNEATGGRYV
PRAILMDLEP GTMDSVRAGP FGQLFRPDNF VFGQTGAGNN WAKGHYTEGA ELIDAVLDVL
RKEAEGCDCL QGFQITHSLG GGTGSGMGTL LISKIREEYP DRIMETFSVF PSPKVSDTVV
EPYNATLSVH QLVENADEVQ VIDNEALYDI CFRTLKLTTP TYGDLNHLVS AAMSGVTCSL
RFPGQLNSDL RKLAVNLIPF PRLHFFMYGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
CTSDPRHGRY LTACAMFRGR MSTKEVDEQM LNVQNKNSSY FVEWIPHNTK SSVCDIPPLG
LKMAVTFVGN STAIQEMFKR VSDQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEFEEEE GDVEA
