TBB4_MAIZE
ID TBB4_MAIZE Reviewed; 447 AA.
AC Q41782; Q43696;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Tubulin beta-4 chain;
DE AltName: Full=Beta-4-tubulin;
GN Name=TUBB4; Synonyms=TUB4;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. A188; TISSUE=Pollen;
RX PubMed=8275104; DOI=10.1046/j.1365-313x.1993.04050875.x;
RA Rogers H.J., Greenland A.J., Hussey P.J.;
RT "Four members of the maize beta-tubulin gene family are expressed in the
RT male gametophyte.";
RL Plant J. 4:875-882(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73; TISSUE=Seedling shoot;
RX PubMed=8111033; DOI=10.1007/bf00020169;
RA Villemur R., Haas N.A., Joyce C.M., Snustad D.P., Silflow C.D.;
RT "Characterization of four new beta-tubulin genes and their expression
RT during male flower development in maize (Zea mays L.).";
RL Plant Mol. Biol. 24:295-315(1994).
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 -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X74655; CAA52719.1; -; mRNA.
DR EMBL; L10635; AAA19707.1; -; mRNA.
DR PIR; S43326; S43326.
DR RefSeq; NP_001105457.1; NM_001111987.1.
DR RefSeq; NP_001167653.1; NM_001174182.1.
DR AlphaFoldDB; Q41782; -.
DR SMR; Q41782; -.
DR STRING; 4577.GRMZM2G066191_P03; -.
DR PaxDb; Q41782; -.
DR PRIDE; Q41782; -.
DR GeneID; 542417; -.
DR KEGG; zma:542417; -.
DR eggNOG; KOG1375; Eukaryota.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41782; baseline and differential.
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: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; 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 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta-4 chain"
FT /id="PRO_0000048358"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..447
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"
FT CONFLICT 304
FT /note="S -> A (in Ref. 2; AAA19707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50132 MW; D878A64653013A0E CRC64;
MREILHIQGG QCGNQIGAKF WEVICGEHCV DSTGRYSGTS SQQLELERIN VYYNEAGGGR
YVPRAVLMDL EPGTMESIRA GPFGGIFRPD NFVYGQSGAG NNWAKGHYTE GAELIDSVLD
VVRKEAENCD CLQGFQVCHS LGGGTGSGMG TLLISKIREE YPDRMMLTFS VFPSPKVSDT
VVEPYNATLS VHQLVENADE CMVLDNEALY DICFRTLKLT NPSFGDLNHL ISATMSGVTC
CLRFPGQLNS DLRKLAVNLI PFPRLHFFMV GFAPLTSRGS QQYRALTVPE LTQQMWDAKN
MMCSADPRHG RYLTASAMFR GKMSTKEVDE QMINVQNKNS SYFVEWIPNN VKSSVCDIPP
VGLPMASTFV GNSTSIQEMF RRVSEQFTAM FRRKAFLHWY TSEGMDEMEF TEAESNMNDL
VAEYQQYQDA TAEEYEEEEH DGEEEHA