TBG2_ARATH
ID TBG2_ARATH Reviewed; 474 AA.
AC P38558; A4IJ36;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Tubulin gamma-2 chain;
DE AltName: Full=Gamma-2-tubulin;
GN Name=TUBG2; OrderedLocusNames=At5g05620; ORFNames=MJJ3.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8148650; DOI=10.2307/3869647;
RA Liu B., Joshi H.C., Wilson T.J., Silflow C.D., Palevitz B.A., Snustad D.P.;
RT "Gamma-tubulin in Arabidopsis: gene sequence, immunoblot, and
RT immunofluorescence studies.";
RL Plant Cell 6:303-314(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION IN NEMATODE INFECTION, DISRUPTION PHENOTYPE, INDUCTION BY
RP NEMATODES, AND SUBUNIT.
RX PubMed=22144887; DOI=10.1371/journal.ppat.1002343;
RA Banora M.Y., Rodiuc N., Baldacci-Cresp F., Smertenko A., Bleve-Zacheo T.,
RA Mellilo M.T., Karimi M., Hilson P., Evrard J.L., Favery B., Engler G.,
RA Abad P., de Almeida Engler J.;
RT "Feeding cells induced by phytoparasitic nematodes require gamma-tubulin
RT ring complex for microtubule reorganization.";
RL PLoS Pathog. 7:E1002343-E1002343(2011).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles, suggesting that it is involved in the minus-end
CC nucleation of microtubule assembly. {ECO:0000269|PubMed:22144887}.
CC -!- FUNCTION: Gamma-tubulin complex is essential for the control of
CC microtubular network remodeling in the course of initiation and
CC development of giant-feeding cells, and for the successful reproduction
CC of nematodes (e.g. Meloidogyne spp.) in their plant hosts.
CC {ECO:0000269|PubMed:22144887}.
CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin and GCP
CC proteins. {ECO:0000269|PubMed:22144887}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:P38557}. Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Note=Present in
CC discrete dots in the cytoplasm and cell cortex. {ECO:0000250}.
CC -!- INDUCTION: Up-regulated in galls upon nematode infection.
CC {ECO:0000269|PubMed:22144887}.
CC -!- DISRUPTION PHENOTYPE: Alteration of the morphology of feeding site and
CC failure of nematode life cycle completion.
CC {ECO:0000269|PubMed:22144887}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; U03990; AAA20654.1; -; Genomic_DNA.
DR EMBL; AB005237; BAB09656.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90900.1; -; Genomic_DNA.
DR EMBL; BT030394; ABO45697.1; -; mRNA.
DR PIR; T50558; T50558.
DR RefSeq; NP_196181.1; NM_120644.3.
DR AlphaFoldDB; P38558; -.
DR SMR; P38558; -.
DR BioGRID; 15724; 6.
DR STRING; 3702.AT5G05620.1; -.
DR PaxDb; P38558; -.
DR PRIDE; P38558; -.
DR ProteomicsDB; 232989; -.
DR EnsemblPlants; AT5G05620.1; AT5G05620.1; AT5G05620.
DR GeneID; 830445; -.
DR Gramene; AT5G05620.1; AT5G05620.1; AT5G05620.
DR KEGG; ath:AT5G05620; -.
DR Araport; AT5G05620; -.
DR TAIR; locus:2166469; AT5G05620.
DR eggNOG; KOG1374; Eukaryota.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P38558; -.
DR OMA; RRESMFK; -.
DR OrthoDB; 687389at2759; -.
DR PhylomeDB; P38558; -.
DR PRO; PR:P38558; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P38558; baseline and differential.
DR Genevisible; P38558; AT.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0051641; P:cellular localization; IMP:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0000212; P:meiotic spindle organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IMP:TAIR.
DR GO; GO:0046785; P:microtubule polymerization; IMP:TAIR.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0009624; P:response to nematode; IDA:UniProtKB.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IMP:TAIR.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002454; Gamma_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; 2.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
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.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..474
FT /note="Tubulin gamma-2 chain"
FT /id="PRO_0000048446"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 474 AA; 53277 MW; 2986B84CBA57F429 CRC64;
MPREIITLQV GQCGNQIGME FWKQLCLEHG ISKDGILEDF ATQGGDRKDV FFYQADDQHY
IPRALLIDLE PRVINGIQNG EYRNLYNHEN IFLSDHGGGA GNNWASGYHQ GKGVEEEIMD
MIDREADGSD SLEGFVLCHS IAGGTGSGMG SYLLETLNDR YSKKLVQTYS VFPNQMETSD
VVVQPYNSLL TLKRLTLNAD CVVVLDNTAL NRIAVERLHL TNPTFAQTNS LVSTVMSAST
TTLRYPGYMN NDLVGLLASL IPTPRCHFLM TGYTPLTVER QANVIRKTTV LDVMRRLLQT
KNIMVSSYAR NKEASQAKYI SILNIIQGEV DPTQVHESLQ RIRERKLVNF IDWGPASIQV
ALSKKSPYVQ TSHRVSGLML ASHTSIRHLF SRCLSQYDKL RKKQAFLDNY RKFPMFADND
LSEFDESRDI IESLVDEYKA CESPDYIKWG MEDPGQLMTG EGNASGVADP KLAF
