ID   TBB_ENTDO               Reviewed;         447 AA.
AC   P35394;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Enteroctopus.
OX   NCBI_TaxID=267067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=8241265; DOI=10.1016/0167-4781(93)90151-3;
RA   Tomarev S.I., Zinovieva R.D., Piatigorsky J.;
RT   "Primary structure and lens-specific expression of genes for an
RT   intermediate filament protein and a beta-tubulin in cephalopods.";
RL   Biochim. Biophys. Acta 1216:245-254(1993).
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: Lens specific.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; L10111; AAA16611.1; -; mRNA.
DR   PIR; S43426; S43426.
DR   AlphaFoldDB; P35394; -.
DR   SMR; P35394; -.
DR   PRIDE; P35394; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           1..447
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048304"
FT   REGION          424..447
FT                   /note="Disordered"
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   447 AA;  50448 MW;  517CF40A2B31DE15 CRC64;
     MREIVHIQAG QCGNQIGSKF WEVISEEHGI DPSGVYQGKL STQLERSYVY FNEASSGKYV
     PRAVLLDLEP GTMDSVRSGP YGSLFRPDNY VFGQSGAGNN WAKGHYTEGA ELVDTVLDVI
     RKECEGCECI QGFQMTHSLG GGTGAGMGTL LISKYREEYP DRIMTTFSVM PSPKVSDTVV
     EPYNATLSIH QLVENTDETF CIDNEALYDI SLRTLKLPNP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQD YRMHSVSDLT QQLFDAKNMM
     TACDPRHGRY LTVAAVFRGK MSMKEVDEQM FSIQNKMSPY FVEWIPNNVK TAVCDIPPTG
     LEMSATFIGN STAIQEIFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQEARS TDSDEYDNEE YYNQQEE