ID   TBB_BOMMO               Reviewed;         450 AA.
AC   P41385;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Kinshu X Showa; TISSUE=Testis;
RX   PubMed=7557453; DOI=10.1016/0378-1119(95)00346-8;
RA   Mita K., Nenoi M., Morimyo M., Tsuji H., Ichimura S., Sawai M., Hamana K.;
RT   "Expression of the Bombyx mori beta-tubulin-encoding gene in testis.";
RL   Gene 162:329-330(1995).
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; X74951; CAA52906.1; -; mRNA.
DR   PIR; S37177; S37177.
DR   RefSeq; NP_001037492.1; NM_001044027.1.
DR   AlphaFoldDB; P41385; -.
DR   SMR; P41385; -.
DR   STRING; 7091.BGIBMGA003296-TA; -.
DR   PRIDE; P41385; -.
DR   GeneID; 693049; -.
DR   KEGG; bmor:693049; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   OrthoDB; 962471at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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;
KW   Reference proteome.
FT   CHAIN           1..450
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048275"
FT   REGION          427..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..450
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:0000250"
SQ   SEQUENCE   450 AA;  50335 MW;  0EAB32D17CE96CA1 CRC64;
     MREIVHVQVG RCGNQIGSKF WEVISDEHGI DPCGRYHGDS DLQLERINVY YNEAFGAKYV
     PRAVLVDLEP STMDSIRGGP YGSLYRPDNV VCGASGAGNN WAKGHYTEGA DLLETVLDVV
     RKEAEGCDCL QGFQLVHSLG GGTGSGMGTL LLANLTDEYP DRITATYSVV PSPTVSETVV
     EPYNATLSVN QLIENSIQSY CIDNEALYYI CHRTLKLMAP TYGALNHLVS LTMSGVTTCL
     RFPGQLNADL RKLAVNMIPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     AACDPHRGRY LTVATVFRGR MSMKEIDEQI LNVQKKNKDF FVEWIPNNVQ TAVCDIPPRG
     MKMSATFIGN TTAIQEIFKR ISEQFAAMFS RKAFLHWYTG EGMEEGDFAE ADNNVSDLLS
     EYQQYQDATI DQEFEDEEEV EEQNDDSDEQ