TBB6_CHICK
ID TBB6_CHICK Reviewed; 446 AA.
AC P09207;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Tubulin beta-6 chain;
DE AltName: Full=Beta-tubulin class-VI;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2888766; DOI=10.1016/s0021-9258(18)47938-0;
RA Murphy D.B., Wallis K.T., Machlin P.S., Ratrie H. III, Cleveland D.W.;
RT "The sequence and expression of the divergent beta-tubulin in chicken
RT erythrocytes.";
RL J. Biol. Chem. 262:14305-14312(1987).
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 -!- TISSUE SPECIFICITY: Highly expressed in bone marrow.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. The precise function of polyglycylation is still unclear.
CC {ECO:0000250|UniProtKB:A2AQ07}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group (By
CC similarity). Polyglutamylation plays a key role in microtubule severing
CC by spastin (SPAST). SPAST preferentially recognizes and acts on
CC microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). {ECO:0000250|UniProtKB:A2AQ07,
CC ECO:0000250|UniProtKB:Q71U36}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; J02828; AAA49120.1; -; mRNA.
DR PIR; A27424; A27424.
DR RefSeq; NP_990776.1; NM_205445.1.
DR PDB; 3BEW; X-ray; 2.60 A; C/F=324-333.
DR PDBsum; 3BEW; -.
DR AlphaFoldDB; P09207; -.
DR SMR; P09207; -.
DR BioGRID; 676676; 1.
DR STRING; 9031.ENSGALP00000012034; -.
DR PaxDb; P09207; -.
DR PRIDE; P09207; -.
DR Ensembl; ENSGALT00000012048; ENSGALP00000012034; ENSGALG00000007447.
DR GeneID; 396427; -.
DR KEGG; gga:396427; -.
DR CTD; 81027; -.
DR VEuPathDB; HostDB:geneid_396427; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000159809; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P09207; -.
DR OMA; NTDACFC; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P09207; -.
DR TreeFam; TF300298; -.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-GGA-5620924; Intraflagellar transport.
DR Reactome; R-GGA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-GGA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-9646399; Aggrephagy.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-GGA-983189; Kinesins.
DR EvolutionaryTrace; P09207; -.
DR PRO; PR:P09207; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000007447; Expressed in spleen and 13 other tissues.
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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..446
FT /note="Tubulin beta-6 chain"
FT /id="PRO_0000048268"
FT REGION 419..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3BEW"
SQ SEQUENCE 446 AA; 50154 MW; 187D5611F54560BB CRC64;
MREIVHLQIG QCGNQIGAKF WEVISDEHGI DIAGNYCGNA SLQLERINVY FNEAYSHKYV
PRSILVDLEP GTMDSVRSSK IGPLFRPDNF IHGNSGAGNN WAKGHYTEGA ELIENVMDVV
RNECESCDCL QGFQLIHSLG GGTGSGMGTL LINKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNAILSIH QLIENTDETF CIDNEALYDI CFRTLKLTNP TYGDLNHLVS LTMSGVTTSL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALSVPELT QQMFDARNMM
AACDPRRGRY LTVACIFRGR MSTREVDEQL LSVQTKNSSY FVEWIPNNVK VAVCDIPPRG
LKMAATFIGN NTAIQELFIR VSEQFSAMFR RKAFLHWYTG EGMDEMEFSE AEGNTNDLVS
EYQQYQDATA DVEEYEEAEA SPEKET
