TBB3_BOVIN
ID TBB3_BOVIN Reviewed; 450 AA.
AC Q2T9S0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tubulin beta-3 chain;
GN Name=TUBB3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 437-450, GLUTAMYLATION AT GLU-438, AND PHOSPHORYLATION
RP AT SER-444.
RX PubMed=2052551; DOI=10.1073/pnas.88.11.4685;
RA Alexander J.E., Hunt D.F., Lee M.K., Shabanowitz J., Michel H.,
RA Berlin S.C., MacDonald T.L., Sundberg R.J., Rebhun L.I., Frankfurter A.;
RT "Characterization of posttranslational modifications in neuron-specific
RT class III beta-tubulin by mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4685-4689(1991).
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. TUBB3 plays a critical
CC role in proper axon guidance and maintenance (By similarity). Binding
CC of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of
CC UNC5C from polymerized TUBB3 in microtubules and thereby lead to
CC increased microtubule dynamics and axon repulsion (By similarity).
CC Plays a role in dorsal root ganglion axon projection towards the spinal
CC cord (By similarity). {ECO:0000250|UniProtKB:Q13509,
CC ECO:0000250|UniProtKB:Q9ERD7}.
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. Interacts with UNC5C (via cytoplasmic domain); this
CC interaction is decreased by NTN1/Netrin-1 (By similarity). Interacts
CC with NLRP5/MATER at cytoskeleton microtubules (By similarity).
CC Interacts with DPYSL5 (By similarity). {ECO:0000250|UniProtKB:Q13509,
CC ECO:0000250|UniProtKB:Q9ERD7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q9ERD7}.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC calcium.
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: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000250|UniProtKB:Q13509}.
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. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm
CC motility. {ECO:0000250|UniProtKB:Q9ERD7}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:2052551). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on 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). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000250|UniProtKB:Q9ERD7, ECO:0000269|PubMed:2052551}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BC111295; AAI11296.1; -; mRNA.
DR RefSeq; NP_001070595.1; NM_001077127.1.
DR PDB; 7ALR; X-ray; 1.93 A; B=1-450.
DR PDB; 7ODN; X-ray; 2.33 A; B=1-450.
DR PDBsum; 7ALR; -.
DR PDBsum; 7ODN; -.
DR AlphaFoldDB; Q2T9S0; -.
DR SMR; Q2T9S0; -.
DR IntAct; Q2T9S0; 1.
DR STRING; 9913.ENSBTAP00000000568; -.
DR iPTMnet; Q2T9S0; -.
DR PaxDb; Q2T9S0; -.
DR PeptideAtlas; Q2T9S0; -.
DR PRIDE; Q2T9S0; -.
DR Ensembl; ENSBTAT00000000568; ENSBTAP00000000568; ENSBTAG00000023730.
DR GeneID; 768070; -.
DR KEGG; bta:768070; -.
DR CTD; 10381; -.
DR VEuPathDB; HostDB:ENSBTAG00000023730; -.
DR VGNC; VGNC:107005; TUBB3.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000159115; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q2T9S0; -.
DR OMA; EMEGECV; -.
DR OrthoDB; 962471at2759; -.
DR TreeFam; TF300298; -.
DR Reactome; R-BTA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-BTA-5610787; Hedgehog 'off' state.
DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-BTA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-BTA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-BTA-983189; Kinesins.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000023730; Expressed in Ammon's horn and 93 other tissues.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:1990890; F:netrin receptor binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
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 GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
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; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Isopeptide bond; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000233024"
FT REGION 425..450
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..450
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 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q13509"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:2052551"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2052551"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:7ALR"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:7ALR"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 222..241
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:7ALR"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:7ALR"
FT TURN 391..395
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:7ALR"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:7ALR"
FT HELIX 405..427
FT /evidence="ECO:0007829|PDB:7ALR"
SQ SEQUENCE 450 AA; 50433 MW; 4B9CDE7DBA102949 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 APLTARGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEMYEDD EEESEAQGPK
