TBB3_MACFA
ID TBB3_MACFA Reviewed; 450 AA.
AC Q60HC2; Q4R582;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tubulin beta-3 chain;
DE AltName: Full=Tubulin beta-4 chain;
GN Name=TUBB3; Synonyms=TUBB4; ORFNames=QccE-11995, QccE-15186;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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 (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). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000250|UniProtKB:Q9ERD7}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AB125205; BAD51993.1; -; mRNA.
DR EMBL; AB169662; BAE01743.1; -; mRNA.
DR RefSeq; NP_001270374.1; NM_001283445.1.
DR AlphaFoldDB; Q60HC2; -.
DR SMR; Q60HC2; -.
DR STRING; 9541.XP_005592892.1; -.
DR Ensembl; ENSMFAT00000016874; ENSMFAP00000042590; ENSMFAG00000033629.
DR GeneID; 101925940; -.
DR CTD; 10381; -.
DR VEuPathDB; HostDB:ENSMFAG00000033629; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000159115; -.
DR OMA; EMEGECV; -.
DR OrthoDB; 962471at2759; -.
DR Proteomes; UP000233100; Chromosome 20.
DR Bgee; ENSMFAG00000033629; Expressed in temporal lobe and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000048253"
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:0000250|UniProtKB:Q2T9S0"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
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
