TBB1_MAIZE
ID TBB1_MAIZE Reviewed; 446 AA.
AC P18025;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=TUBB1; Synonyms=TUB1;
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 [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 22;
RX PubMed=2103487; DOI=10.1007/bf00039438;
RA Hussey P.J., Haas N., Hunsperger J., Larkin J., Snustad D.P., Silflow C.D.;
RT "The beta-tubulin gene family in Zea mays: two differentially expressed
RT beta-tubulin genes.";
RL Plant Mol. Biol. 15:957-972(1990).
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 -!- TISSUE SPECIFICITY: Found in areas of rapidly dividing tissues.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X52878; CAA37060.1; -; Genomic_DNA.
DR PIR; S14701; S14701.
DR AlphaFoldDB; P18025; -.
DR SMR; P18025; -.
DR STRING; 4577.GRMZM2G164696_P01; -.
DR PaxDb; P18025; -.
DR ProMEX; P18025; -.
DR MaizeGDB; 24940; -.
DR eggNOG; KOG1375; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P18025; 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; 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; 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..446
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048355"
FT REGION 422..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
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 446 AA; 49962 MW; 9A32D43927A21297 CRC64;
MREILHIQGG QCGNQIGAKF WEVVCAEHGI DATGRYGGDS DLQLERVNVY YNEASCGRFV
PRAVLMDLEP GTMDSVRSGP YGHIFRPDNF VFGQSGAGNN SAKGHYTEGA ELIDSVLDVV
RKEAENCDCL QGFQVCHSLG GGTGSAMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLTTP SFGDLNHLIS ATMSGVTCCL
RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDAKNMM
CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK STVCDIPPHG
LKMASTFIGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA DEEGEYEDEE EGDLQD