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Tubulin beta-3 chain (Neuron-specific class III beta-tubulin)

 TBB3_RAT                Reviewed;         450 AA.
Q4QRB4; Q8K5B6;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
20-JUN-2018, entry version 113.
RecName: Full=Tubulin beta-3 chain;
AltName: Full=Neuron-specific class III beta-tubulin;
Name=Tubb3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=12234689; DOI=10.1016/S0378-1119(02)00801-6;
Dennis K., Uittenbogaard M., Chiaramello A., Moody S.A.;
"Cloning and characterization of the 5'-flanking region of the rat
neuron-specific class III beta-tubulin gene.";
Gene 294:269-277(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 104-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
-!- FUNCTION: Tubulin is the major constituent of microtubules. It
binds two moles of GTP, one at an exchangeable site on the beta
chain and one at a non-exchangeable site on the alpha chain. TUBB3
plays a critical role in proper axon guidance and mantainance (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
a hollow water-filled tube with an outer diameter of 25 nm and an
inner diameter of 15 nM. Alpha-beta heterodimers associate head-
to-tail to form protofilaments running lengthwise along the
microtubule wall with the beta-tubulin subunit facing the
microtubule plus end conferring a structural polarity.
Microtubules usually have 13 protofilaments but different
protofilament numbers can be found in some organisms and
specialized cells.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
-!- DOMAIN: The highly acidic C-terminal region may bind cations such
as calcium.
-!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
resulting in polyglycine chains on the gamma-carboxyl group.
Glycylation is mainly limited to tubulin incorporated into
axonemes (cilia and flagella) whereas glutamylation is prevalent
in neuronal cells, centrioles, axonemes, and the mitotic spindle.
Both modifications can coexist on the same protein on adjacent
residues, and lowering polyglycylation levels increases
polyglutamylation, and reciprocally. The precise function of
polyglycylation is still unclear. {ECO:0000250|UniProtKB:P68369}.
-!- PTM: Some glutamate residues at the C-terminus are
polyglutamylated, resulting in polyglutamate chains on the gamma-
carboxyl group (By similarity). Polyglutamylation plays a key role
in microtubule severing by spastin (SPAST). SPAST preferentially
recognizes and acts on microtubules decorated with short
polyglutamate tails: severing activity by SPAST increases as the
number of glutamates per tubulin rises from one to eight, but
decreases beyond this glutamylation threshold (By similarity).
{ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
-!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
metaphase to telophase, but not in interphase. This
phosphorylation inhibits tubulin incorporation into microtubules.
{ECO:0000250|UniProtKB:Q13509}.
-!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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EMBL; AF459021; AAM28438.1; -; mRNA.
EMBL; BC097281; AAH97281.1; -; mRNA.
RefSeq; NP_640347.2; NM_139254.2.
UniGene; Rn.43958; -.
ProteinModelPortal; Q4QRB4; -.
SMR; Q4QRB4; -.
BioGrid; 251505; 2.
IntAct; Q4QRB4; 6.
MINT; Q4QRB4; -.
STRING; 10116.ENSRNOP00000023452; -.
iPTMnet; Q4QRB4; -.
PhosphoSitePlus; Q4QRB4; -.
PaxDb; Q4QRB4; -.
PRIDE; Q4QRB4; -.
Ensembl; ENSRNOT00000023452; ENSRNOP00000023452; ENSRNOG00000017209.
GeneID; 246118; -.
KEGG; rno:246118; -.
UCSC; RGD:628595; rat.
CTD; 10381; -.
RGD; 628595; Tubb3.
eggNOG; KOG1375; Eukaryota.
eggNOG; COG5023; LUCA.
GeneTree; ENSGT00760000119061; -.
HOGENOM; HOG000165710; -.
HOVERGEN; HBG000089; -.
InParanoid; Q4QRB4; -.
KO; K07375; -.
OMA; DEMEGEC; -.
OrthoDB; EOG091G06U2; -.
PhylomeDB; Q4QRB4; -.
TreeFam; TF300298; -.
Reactome; R-RNO-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-RNO-2132295; MHC class II antigen presentation.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-5620924; Intraflagellar transport.
Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-RNO-68877; Mitotic Prometaphase.
Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-RNO-8955332; Carboxyterminal post-translational modifications of tubulin.
Reactome; R-RNO-983189; Kinesins.
PRO; PR:Q4QRB4; -.
Proteomes; UP000002494; Chromosome 19.
Bgee; ENSRNOG00000017209; -.
Genevisible; Q4QRB4; RN.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0042277; F:peptide binding; IPI:RGD.
GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:RGD.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
GO; GO:0000278; P:mitotic cell cycle; IMP:RGD.
GO; GO:0030182; P:neuron differentiation; IMP:RGD.
Gene3D; 1.10.287.600; -; 1.
Gene3D; 3.30.1330.20; -; 1.
Gene3D; 3.40.50.1440; -; 1.
InterPro; IPR013838; Beta-tubulin_BS.
InterPro; IPR002453; Beta_tubulin.
InterPro; IPR008280; Tub_FtsZ_C.
InterPro; IPR000217; Tubulin.
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
InterPro; IPR037103; Tubulin/FtsZ_C_sf.
InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
InterPro; IPR023123; Tubulin_C.
InterPro; IPR017975; Tubulin_CS.
InterPro; IPR003008; Tubulin_FtsZ_GTPase.
PANTHER; PTHR11588; PTHR11588; 1.
PANTHER; PTHR11588:SF256; PTHR11588:SF256; 1.
Pfam; PF00091; Tubulin; 1.
Pfam; PF03953; Tubulin_C; 1.
PRINTS; PR01163; BETATUBULIN.
PRINTS; PR01161; TUBULIN.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 1.
PROSITE; PS00227; TUBULIN; 1.
PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
GTP-binding; Isopeptide bond; Microtubule; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 450 Tubulin beta-3 chain.
/FTId=PRO_0000233027.
NP_BIND 140 146 GTP. {ECO:0000255}.
MOD_RES 172 172 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q13509}.
MOD_RES 438 438 5-glutamyl polyglutamate.
{ECO:0000250|UniProtKB:Q2T9S0}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q2T9S0}.
CONFLICT 249 249 D -> H (in Ref. 1; AAM28438).
{ECO:0000305}.
CONFLICT 390 390 Missing (in Ref. 1; AAM28438).
{ECO:0000305}.
CONFLICT 401 401 E -> Q (in Ref. 1; AAM28438).
{ECO:0000305}.
CONFLICT 446 446 A -> R (in Ref. 1; AAM28438).
{ECO:0000305}.
SEQUENCE 450 AA; 50419 MW; 4B9D9B7DBA102949 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 DEESEAQGPK


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