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 30-NOV-2016, entry version 117. 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; OC Phasianidae; 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 CC binds two moles of GTP, one at an exchangeable site on the beta CC chain and one at a non-exchangeable site on the alpha chain. CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is CC a hollow water-filled tube with an outer diameter of 25 nm and an CC inner diameter of 15 nM. Alpha-beta heterodimers associate head- CC to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the CC microtubule plus end conferring a structural polarity. CC Microtubules usually have 13 protofilaments but different CC 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 CC axonemes (cilia and flagella) whereas glutamylation is prevalent CC in neuronal cells, centrioles, axonemes, and the mitotic spindle. CC Both modifications can coexist on the same protein on adjacent CC residues, and lowering polyglycylation levels increases CC polyglutamylation, and reciprocally. The precise function of CC polyglycylation is still unclear. {ECO:0000250|UniProtKB:A2AQ07}. CC -!- PTM: Some glutamate residues at the C-terminus are CC polyglutamylated, resulting in polyglutamate chains on the gamma- CC carboxyl group (By similarity). Polyglutamylation plays a key role CC in microtubule severing by spastin (SPAST). SPAST preferentially CC recognizes and acts on microtubules decorated with short CC polyglutamate tails: severing activity by SPAST increases as the CC number of glutamates per tubulin rises from one to eight, but CC decreases beyond this glutamylation threshold (By similarity). CC {ECO:0000250|UniProtKB:A2AQ07, 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 UniGene; Gga.31960; -. DR ProteinModelPortal; P09652; -. DR SMR; P09652; -. DR iPTMnet; P09652; -. DR PRIDE; P09652; -. DR GeneID; 431043; -. DR KEGG; gga:431043; -. DR CTD; 10381; -. DR HOGENOM; HOG000165710; -. DR HOVERGEN; HBG000089; -. DR KO; K07375; -. DR PhylomeDB; P09652; -. DR PRO; PR:P09652; -. DR Proteomes; UP000000539; Unplaced. DR GO; GO:0005623; C:cell; IDA:AgBase. 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: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 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; 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 Complete proteome; Cytoplasm; Cytoskeleton; GTP-binding; KW Isopeptide bond; Microtubule; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1 449 Tubulin beta-4 chain. FT /FTId=PRO_0000048266. FT NP_BIND 140 146 GTP. {ECO:0000255}. FT MOD_RES 438 438 5-glutamyl polyglutamate. FT {ECO:0000250|UniProtKB:Q2T9S0}. FT MOD_RES 444 444 Phosphoserine. FT {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 //