ID Q26901_TELCI Unreviewed; 448 AA.
AC Q26901;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Tubulin beta chain {ECO:0000256|RuleBase:RU000352};
OS Teladorsagia circumcincta (Brown stomach worm) (Ostertagia circumcincta).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae;
OC Teladorsagia.
OX NCBI_TaxID=45464 {ECO:0000313|EMBL:CAA93249.1};
RN [1] {ECO:0000313|EMBL:CAA93249.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Benzimidazole-susceptible strain {ECO:0000313|EMBL:CAA93249.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:CAA93249.1};
RX PubMed=8855563; DOI=10.1016/0166-6851(96)02664-3;
RA Elard L., Comes A.M., Humbert J.F.;
RT "Sequences of beta-tubulin cDNA from benzimidazole-susceptible and
RT -resistant strains of Teladorsagia circumcincta, a nematode parasite of
RT small ruminants.";
RL Mol. Biochem. Parasitol. 79:249-253(1996).
RN [2] {ECO:0000313|EMBL:CAA93249.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Benzimidazole-susceptible strain {ECO:0000313|EMBL:CAA93249.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:CAA93249.1};
RA Humbert J.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC consisting of laterally associated linear protofilaments composed of
CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition
CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap
CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to
CC GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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. {ECO:0000256|RuleBase:RU000352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}.
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DR EMBL; Z69258; CAA93249.1; -; mRNA.
DR AlphaFoldDB; Q26901; -.
DR SMR; Q26901; -.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 1.
DR PANTHER; PTHR11588:SF429; TUBULIN BETA-1 CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000352}.
FT DOMAIN 47..244
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 246..383
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 49933 MW; 82FAA1B20A3A36B6 CRC64;
MREIVHVQAG QCGNQIGSKF WEVISDEHGI QPDGTYKGES ALQLERINVY YNEAHGGKYV
PRAVLVDLEP GTMDSVRSGP YGQLFRPDNY VFGQSGAGNN WAKGHYTEGA ELVDNVLDVV
RKEAEGCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMASFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS VTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLSAKGAQA YRASTVAELT QQMFDAKNMM
AACDPRHGRY LTVAAMFRGR MSMREVDDQM MSVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAATFVGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLIS
EYQQYQEATA DDMGDLDAEG AEEPYPEE
//
