ID   TBB_STRPU               Reviewed;         292 AA.
AC   P18700;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
DE   Flags: Fragment;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3133488; DOI=10.1007/bf02099730;
RA   Harlow P., Litwin S., Nemer M.;
RT   "Synonymous nucleotide substitution rates of beta-tubulin and histone genes
RT   conform to high overall genomic rates in rodents but not in sea urchins.";
RL   J. Mol. Evol. 27:56-64(1988).
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; X07502; CAA30385.1; -; mRNA.
DR   PIR; S02327; S02327.
DR   AlphaFoldDB; P18700; -.
DR   SMR; P18700; -.
DR   STRING; 7668.SPU_000062-tr; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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; 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; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..292
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048313"
FT   REGION          265..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   292 AA;  33345 MW;  B7132E92B94E1692 CRC64;
     REEYPDRIMN TFSVVPSPKV SDTVVEPYNA TLSVHQLVEN TDETYCIDNE ALYDICFRTL
     KLTTPTYGDL NHLVSATMSG VTTCLRFPGQ LNADLRKLAV NMVPFPRLHF FMPGFAPLTS
     RGSQQYRALT VPELTQQMFD AKNMMAACDP RHGRYLTVAA IFRGRMSMKE VDEQMLNVQN
     KNSSYFVEWI PNNVKTAVCD IPPRGLKMSA TFIGNSTAIQ ELFKRISEQF TAMFRRKAFL
     HWYTGEGMDE MEFTEAESNM NDLVSEYQQY QDATAEEEGE FDEEEEGDEE AA