ID   TBB3_ECHMU              Reviewed;         443 AA.
AC   Q9NFZ5;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Beta-3-tubulin;
GN   Name=TUB-3;
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H-95;
RX   PubMed=10779606; DOI=10.1016/s0166-6851(00)00178-x;
RA   Brehm K., Kronthaler K., Jura H., Frosch M.;
RT   "Cloning and characterization of beta-tubulin genes from Echinococcus
RT   multilocularis.";
RL   Mol. Biochem. Parasitol. 107:297-302(2000).
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 (By similarity).
CC       {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; AJ249550; CAB91642.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NFZ5; -.
DR   SMR; Q9NFZ5; -.
DR   PRIDE; Q9NFZ5; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   OMA; QSCTILE; -.
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..443
FT                   /note="Tubulin beta-3 chain"
FT                   /id="PRO_0000048292"
FT   BINDING         140..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   443 AA;  49714 MW;  7C7C0D1963F1AAAE CRC64;
     MRELVHMQAG QCGNQIGSKF WETISQEHGI DEMGSYHGDS DLQLERINVY YNEGQGGKYV
     PRALLIDLEP GTMDSVRSGP LGKLFRPDNF IFGQSGAGNN WAKGHYTEGA ELIEEVLDVV
     RKECEACDCL QGFQLCHSLG GGTGSGMGTL LIAKIREEYP DRIMTSFSVV PSPKVSDTVV
     EPYNATLSVH QLVESTDETF CIDNEALYDI CFRTLKLPNP NYSDLNHLVS LTMSGVTTSL
     RFPGQLNSDL RKLAVNMVPF PRLHFFVPGF APLASRTSQS YQSCTILELT RQMFDAKNMM
     AACDPSHGRY LTVAAMYRGR VSMKEVEDRI LETQTRNSTY FVEWIPNNVK TAVCDIPPID
     FKVAGTFIGN TTAIQELFTR VSDQFSAMFR RRAFLHFFTS EGMDEMEFSE AESNMNDLIS
     EYQQYQEVGI DDDYGEEEAA PEE