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 22-JAN-2014, entry version 97. 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 Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia; OC Theropoda; Coelurosauria; Aves; Neognathae; 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 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 -!- SIMILARITY: Belongs to the tubulin family. 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; 1-427. DR PaxDb; P09652; -. DR GeneID; 431043; -. DR KEGG; gga:431043; -. DR CTD; 10381; -. DR eggNOG; COG5023; -. DR HOGENOM; HOG000165710; -. DR HOVERGEN; HBG000089; -. DR InParanoid; P09652; -. DR KO; K07375; -. DR NextBio; 20830657; -. 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 GO; GO:0051258; P:protein polymerization; 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; Microtubule; KW Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1 449 Tubulin beta-4 chain. FT /FTId=PRO_0000048266. FT NP_BIND 140 146 GTP (Potential). FT MOD_RES 444 444 Phosphoserine. 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 //