TBB4_CHICK
ID TBB4_CHICK Reviewed; 449 AA.
AC P09652;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tubulin beta-4 chain;
DE AltName: Full=Beta-tubulin class-III;
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 [GENOMIC DNA].
RX PubMed=6490718; DOI=10.1083/jcb.99.5.1754;
RA Sullivan K.F., Cleveland D.W.;
RT "Sequence of a highly divergent beta tubulin gene reveals regional
RT heterogeneity in the beta tubulin polypeptide.";
RL J. Cell Biol. 99:1754-1760(1984).
RN [2]
RP PHOSPHORYLATION AT SER-444.
RX PubMed=3350148; DOI=10.1016/0014-5793(88)80658-6;
RA Luduena R.F., Zimmermann H.-P., Little M.;
RT "Identification of the phosphorylated beta-tubulin isotype in
RT differentiated neuroblastoma cells.";
RL FEBS Lett. 230:142-146(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 -!- TISSUE SPECIFICITY: Neuron specific.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15052; AAA49119.1; -; Genomic_DNA.
DR PIR; A29161; A29161.
DR RefSeq; NP_001026769.1; NM_001031598.1.
DR AlphaFoldDB; P09652; -.
DR SMR; P09652; -.
DR ChEMBL; CHEMBL4295707; -.
DR iPTMnet; P09652; -.
DR GeneID; 431043; -.
DR KEGG; gga:431043; -.
DR CTD; 10381; -.
DR VEuPathDB; HostDB:geneid_431043; -.
DR PhylomeDB; P09652; -.
DR PRO; PR:P09652; -.
DR Proteomes; UP000000539; Unplaced.
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:0007411; P:axon guidance; 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 Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin beta-4 chain"
FT /id="PRO_0000048266"
FT REGION 421..449
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 COMPBIAS 431..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3350148"
SQ SEQUENCE 449 AA; 50421 MW; CECD9B729E0F9A84 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV
PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTRRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEMYEDD EEESEQGAK
