ID   TBB7_MAIZE              Reviewed;         445 AA.
AC   Q41784;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Tubulin beta-7 chain;
DE   AltName: Full=Beta-7-tubulin;
GN   Name=TUBB7; Synonyms=TUB7;
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. 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; L10634; AAA19708.1; -; mRNA.
DR   PIR; S43328; S43328.
DR   RefSeq; NP_001105688.1; NM_001112218.1.
DR   AlphaFoldDB; Q41784; -.
DR   SMR; Q41784; -.
DR   STRING; 4577.GRMZM2G043822_P02; -.
DR   PaxDb; Q41784; -.
DR   PRIDE; Q41784; -.
DR   ProMEX; Q41784; -.
DR   EnsemblPlants; Zm00001eb390190_T001; Zm00001eb390190_P001; Zm00001eb390190.
DR   GeneID; 542705; -.
DR   Gramene; Zm00001eb390190_T001; Zm00001eb390190_P001; Zm00001eb390190.
DR   KEGG; zma:542705; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   OrthoDB; 962471at2759; -.
DR   Proteomes; UP000007305; Chromosome 9.
DR   ExpressionAtlas; Q41784; 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..445
FT                   /note="Tubulin beta-7 chain"
FT                   /id="PRO_0000048361"
FT   REGION          421..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..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;  50094 MW;  21111A6245ABB383 CRC64;
     MREILHIQGG QCGNQIGAKF WEVICDEHGI DHTGKYAGDS DLQLERINVY YNEASGGRFV
     PRAVLMDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELIDSVLDVV
     RKEAENCDCL QGFQVCHSLG GGTGSGMGTL LISKIREEYP DRMMLTFSVF PSPKVSDTVV
     EPYNATLSVH QLVENADECM VLDNEALYDI CFRTLKLATP TFGDLNHLIS ATMSGVTCCL
     RFPGQLNSDL RKLAVNLIPF PRLHFFMVGF APLTSRGSQQ YRALTVPELT QQMWDSKNMM
     CAADPRHGRY LTASAMFRGK MSTKEVDEQM LNVQNKNSSY FVEWIPNNVK SSVCDIPPIG
     LKMSSTFVGN STSIQEMFRR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVA
     EYQQYQDATA EDEEYEEEEE EEEET