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TBB_HALDI
ID   TBB_HALDI               Reviewed;         341 AA.
AC   P41386;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Beta-tubulin;
DE   Flags: Fragment;
OS   Haliotis discus (Abalone) (Nordotis discus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=36094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Kuro / Numazu;
RA   Naganuma T., Akutsu T., Ishida T., Kato C., Horikoshi K.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
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; D37946; BAA07160.1; -; mRNA.
DR   AlphaFoldDB; P41386; -.
DR   SMR; P41386; -.
DR   PRIDE; P41386; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN           <1..>341
FT                   /note="Tubulin beta chain"
FT                   /id="PRO_0000048298"
FT   BINDING         66..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         341
SQ   SEQUENCE   341 AA;  38179 MW;  96C0753BBEFD0213 CRC64;
     SVRSGPFGQI FRPDNFVFGQ SGAGNNWAKG HYTEGAELVD SVLDVVRKEA ESCDCLQGFQ
     LTHSLGGGTG SGMGTLLISK IREEYPDRIM NTFSVVPSPK VSDTVVEPYN ATLSVHQLVE
     NTDETYCIDN EALYDICFRT LKLTTPTYGD LNHLVSATMS GVTTCLRFPG QLNADLRKLA
     VNMVPFPRLH FFMPGFAPLT SRGSQQYRAL TVPELTQQMF DAKNMMAACD PRHGRYLTVA
     AIFRGRMSMK EVDEQMLNVQ NKNSSYFVEW IPNNVKTAVC DIPPRGLKMS ATFIGNSTAI
     QELFKRISEQ FTAMFRRKAF LHWYTGEGMD EMEFTEAESN M
 
 
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