TBB_SCHCO
ID TBB_SCHCO Reviewed; 445 AA.
AC P30668;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
GN Name=TUB-2;
OS Schizophyllum commune (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=5334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44200 / CBS 341.81 / 4-39;
RX PubMed=1398097; DOI=10.1016/0378-1119(92)90269-u;
RA Russo P., Juuti J.T., Raudaskoski M.;
RT "Cloning, sequence and expression of a beta-tubulin-encoding gene in the
RT homobasidiomycete Schizophyllum commune.";
RL Gene 119:175-182(1992).
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; X63372; CAA44972.1; -; Genomic_DNA.
DR PIR; JC1312; JC1312.
DR AlphaFoldDB; P30668; -.
DR SMR; P30668; -.
DR PRIDE; P30668; -.
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_0000048429"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 49915 MW; EC29376DB612A0EE CRC64;
MREIVHLQTG QCGNQIGAKF WEVVSDEHGI EADGLYKGTN DQQLERISVY YNEIGANKYV
PRAILVDLEP GTMDSVRSGP LGGLFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDAVLDVV
RKEAEGTDCL QGFQITHSLG GGTGAGMGTL LISKIREEYP DRMMCTFSVV PSPKVSDTVV
EPYNATLSVH QLVENSDETF CIDNEALYDI CFRTLKLSTP TYGDLNHLVS FVMSGITTSL
RFPGQLNSDL RKLAVNLVPF PRLHFFMTGF APLTARGSQQ YRAVTVPELT QQMFDAKNMM
AASDPRHGRY LTVAAMFRGK VSMKEVEEQM QNVQNKNSAY FVEWIPNNVL ASQCDIAPRG
LRMSVTFLGN STAIQELFKR VSDQFTAMFK RKAFLHWYTQ EGMDEMEFTE AESNMQDLVA
EYQQYQDATV EEEGEYEEEV IEDQE
