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 02-JUN-2021, entry version 130. 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 -!- 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 SMR; P09652; -. DR ChEMBL; CHEMBL4295707; -. DR iPTMnet; P09652; -. DR GeneID; 431043; -. DR KEGG; gga:431043; -. DR CTD; 10381; -. DR OMA; NDGEENF; -. 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:0003924; F:GTPase activity; IEA:InterPro. 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: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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR037103; Tubulin/FtsZ_C_sf. 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 NP_BIND 140..146 FT /note="GTP" FT /evidence="ECO:0000255" FT REGION 421..449 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..449 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //