GACP3_ARATH
ID GACP3_ARATH Reviewed; 838 AA.
AC Q9FG37;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Gamma-tubulin complex component 3;
DE Short=AtGCP3;
DE Short=GCP-3;
DE AltName: Full=Spindle pole body component 98;
DE Short=AtSPC98;
GN Name=GCP3; Synonyms=SPC98; OrderedLocusNames=At5g06680; ORFNames=MPH15.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12006626; DOI=10.1242/jcs.115.11.2423;
RA Erhardt M., Stoppin-Mellet V., Campagne S., Canaday J., Mutterer J.,
RA Fabian T., Sauter M., Muller T., Peter C., Lambert A.M., Schmit A.C.;
RT "The plant Spc98p homologue colocalizes with gamma-tubulin at microtubule
RT nucleation sites and is required for microtubule nucleation.";
RL J. Cell Sci. 115:2423-2431(2002).
RN [5]
RP SUBCELLULAR LOCATION, SUBUNIT, AND NUCLEUS ENVELOPE LOCALIZATION REGION.
RX PubMed=17714428; DOI=10.1111/j.1365-313x.2007.03240.x;
RA Seltzer V., Janski N., Canaday J., Herzog E., Erhardt M., Evrard J.L.,
RA Schmit A.C.;
RT "Arabidopsis GCP2 and GCP3 are part of a soluble gamma-tubulin complex and
RT have nuclear envelope targeting domains.";
RL Plant J. 52:322-331(2007).
RN [6]
RP INTERACTION WITH GCP2.
RX PubMed=19509058; DOI=10.1242/jcs.044131;
RA Nakamura M., Hashimoto T.;
RT "A mutation in the Arabidopsis gamma-tubulin-containing complex causes
RT helical growth and abnormal microtubule branching.";
RL J. Cell Sci. 122:2208-2217(2009).
RN [7]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20935636; DOI=10.1038/ncb2110;
RA Nakamura M., Ehrhardt D.W., Hashimoto T.;
RT "Microtubule and katanin-dependent dynamics of microtubule nucleation
RT complexes in the acentrosomal Arabidopsis cortical array.";
RL Nat. Cell Biol. 12:1064-1070(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22110647; DOI=10.1371/journal.pone.0027423;
RA Ambrose C., Wasteneys G.O.;
RT "Cell edges accumulate gamma tubulin complex components and nucleate
RT microtubules following cytokinesis in Arabidopsis thaliana.";
RL PLoS ONE 6:E27423-E27423(2011).
RN [9]
RP FUNCTION IN NEMATODE INFECTION, SUBCELLULAR LOCATION, AND INDUCTION BY
RP NEMATODES.
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).
RN [10]
RP INTERACTION WITH GIP1 AND GIP2, AND SUBCELLULAR LOCATION.
RX PubMed=22427335; DOI=10.1105/tpc.111.094904;
RA Janski N., Masoud K., Batzenschlager M., Herzog E., Evrard J.L., Houlne G.,
RA Bourge M., Chaboute M.E., Schmit A.C.;
RT "The GCP3-interacting proteins GIP1 and GIP2 are required for gamma-tubulin
RT complex protein localization, spindle integrity, and chromosomal
RT stability.";
RL Plant Cell 24:1171-1187(2012).
RN [11]
RP INTERACTION WITH GIP1 AND GIP2.
RX PubMed=22404201; DOI=10.1111/j.1365-313x.2012.04988.x;
RA Nakamura M., Yagi N., Kato T., Fujita S., Kawashima N., Ehrhardt D.W.,
RA Hashimoto T.;
RT "Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component
RT of the gamma-tubulin-containing microtubule nucleating complex.";
RL Plant J. 71:216-225(2012).
CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC at the microtubule organizing centers (MTOCs). Required for the
CC positioning of the gamma-tubulin-containing complex on pre-existing
CC microtubules and for the proper organization of cortical arrays.
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 -!- SUBUNIT: Part of the gamma-tubulin complex. Gamma-tubulin complex is
CC composed of gamma-tubulin and GCP proteins. Interacts directly with
CC GCP2, GIP1 and GIP2. {ECO:0000269|PubMed:17714428,
CC ECO:0000269|PubMed:19509058, ECO:0000269|PubMed:20935636,
CC ECO:0000269|PubMed:22404201, ECO:0000269|PubMed:22427335}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm.
CC Cytoplasm, cell cortex. Cytoplasm, cytoskeleton, spindle.
CC Note=Associated to motile complexes in the cytosol that transiently
CC stabilized at fixed locations in the cell cortex (e.g. along the outer
CC periclinal edge of newly formed crosswalls) from which microtubules
CC grow away prior to microtubules nucleation. Colocalizes with gamma-
CC tubulin at the nuclear surface where microtubules are nucleated.
CC Localizes to both cortical cytoplasm and mitotic microtubule arrays of
CC the nematode feeding giant cells.
CC -!- INDUCTION: Up-regulated in galls upon nematode infection.
CC {ECO:0000269|PubMed:22144887}.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
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DR EMBL; AP002032; BAB09802.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91049.1; -; Genomic_DNA.
DR EMBL; AY099727; AAM20578.1; -; mRNA.
DR EMBL; BT010545; AAQ65168.1; -; mRNA.
DR RefSeq; NP_196286.1; NM_120751.4.
DR AlphaFoldDB; Q9FG37; -.
DR SMR; Q9FG37; -.
DR BioGRID; 15836; 6.
DR IntAct; Q9FG37; 1.
DR STRING; 3702.AT5G06680.1; -.
DR PaxDb; Q9FG37; -.
DR PRIDE; Q9FG37; -.
DR ProteomicsDB; 230052; -.
DR EnsemblPlants; AT5G06680.1; AT5G06680.1; AT5G06680.
DR GeneID; 830557; -.
DR Gramene; AT5G06680.1; AT5G06680.1; AT5G06680.
DR KEGG; ath:AT5G06680; -.
DR Araport; AT5G06680; -.
DR TAIR; locus:2170164; AT5G06680.
DR eggNOG; KOG2000; Eukaryota.
DR HOGENOM; CLU_003736_2_0_1; -.
DR InParanoid; Q9FG37; -.
DR OMA; MRMMSVC; -.
DR OrthoDB; 480444at2759; -.
DR PhylomeDB; Q9FG37; -.
DR PRO; PR:Q9FG37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG37; baseline and differential.
DR Genevisible; Q9FG37; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:TAIR.
DR GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; ISS:TAIR.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IDA:UniProtKB.
DR GO; GO:0009624; P:response to nematode; IDA:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Reference proteome.
FT CHAIN 1..838
FT /note="Gamma-tubulin complex component 3"
FT /id="PRO_0000428970"
FT REGION 1..199
FT /note="Mediates interactions with GIP1 and GIP2"
FT REGION 200..256
FT /note="Triggers nucleus envelope localization"
SQ SEQUENCE 838 AA; 94647 MW; 5FC621D56AE7E144 CRC64;
MEDDDQQKAA DLVQELVLRL VSQNPQTPNL DPNSPAFLKT LRYAFRILSS RLTPSVLPDA
TAIAESLKRR LATQGKSSDA LAFADLYTKF ASKTGPGSVN NKWALVYLLK IVSDDRKSAI
NGLDSSVLLP NLGIGDTGNG VLSRGEAKKK DWSNGVLLVS KDPENLRDIA FREYAILVKE
ENEVTEEVLV RDVLYASQGI DGKYVKFNSE IDGYAVQESV KVPRATRIMV RMLSELGWLF
RKVKTFITES MDRFPAEDVG TVGQAFCAAL QDELSDYYKL LAVLEAQAMN PIPLVSESAS
SNNYLSLRRL SVWFAEPMVK MRLMAVLVDK CKVLRGGAMA GAIHLHAQHG DPLVHDFMMS
LLRCVCSPLF EMVRSWVLEG ELEDTFGEFF VVGQPVKVDL LWREGYKLHP AMLPSFISPS
LAQRILRTGK SINFLRVCCD DHGWADAASE AAAASGTTTR RGGLGYGETD ALEHLVTEAA
KRIDKHLLDV LYKRYKFKEH CLAIKRYLLL GQGDFVQYLM DIVGPKLSEP ANNISSFELA
GFLEAAIRAS NAQYDDRDML DRLRVKMMPH GSGDRGWDVF SLEYEARVPL DTVFTESVLS
KYLRVFNFLW KLKRVEHALI GIWKTMKPNC ITSNSFVKLQ SSVKLQLLSA LRRCQVLWNE
MNHFVTNFQY YIMFEVLEVS WSNFSKEMEA AKDLDDLLAA HEKYLNAIVG KSLLGEQSQT
IRESLFVLFE LILRFRSHAD RLYEGIHELQ IRSKESGREK NKSQEPGSWI SEGRKGLTQR
AGEFLQSMSQ DMDSIAKEYT SSLDGFLSLL PLQQSVDLKF LFFRLDFTEF YSRLHSKG
