MZT1B_ARATH
ID MZT1B_ARATH Reviewed; 71 AA.
AC Q9M0N8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Mitotic-spindle organizing protein 1B;
DE AltName: Full=GCP3-interacting protein 1;
DE Short=AtGIP1;
DE AltName: Full=Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1B;
DE Short=AtGIP1B;
GN Name=GIP1; Synonyms=GIP1B; OrderedLocusNames=At4g09550; ORFNames=T15G18.30;
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;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH TUBB2/TUBB3 AND GCP3.
RX PubMed=18178112; DOI=10.1016/j.cellbi.2007.11.006;
RA Janski N., Herzog E., Schmit A.C.;
RT "Identification of a novel small Arabidopsis protein interacting with
RT gamma-tubulin complex protein 3.";
RL Cell Biol. Int. 32:546-548(2008).
RN [6]
RP SUBUNIT, INTERACTION WITH GCP3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
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 [7]
RP DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH GCP3, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
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).
RN [8]
RP 3D-STRUCTURE MODELING, INTERACTION WITH TSA1 AND GIP2, AND SUBUNIT.
RX PubMed=24348487; DOI=10.3389/fpls.2013.00480;
RA Batzenschlager M., Masoud K., Janski N., Houlne G., Herzog E., Evrard J.L.,
RA Baumberger N., Erhardt M., Nomine Y., Kieffer B., Schmit A.C.,
RA Chaboute M.E.;
RT "The GIP gamma-tubulin complex-associated proteins are involved in nuclear
RT architecture in Arabidopsis thaliana.";
RL Front. Plant Sci. 4:480-480(2013).
CC -!- FUNCTION: Required for gamma-tubulin complex recruitment to the
CC microtubule organizing centers (MTOCs) (By similarity). During mitosis,
CC modulates gamma-tubulin complex localization, spindle stability and
CC chromosomal segregation. Necessary for gametophyte development and
CC embryogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Homo- and heteromultimer. Part of the gamma-tubulin complex.
CC Interacts with TUBB2/TUBB3, GIP2, GCP3 and TSA1 (via C-terminal
CC domain). {ECO:0000269|PubMed:18178112, ECO:0000269|PubMed:22404201,
CC ECO:0000269|PubMed:22427335, ECO:0000269|PubMed:24348487}.
CC -!- INTERACTION:
CC Q9M0N8; P29512: TUBB3; NbExp=3; IntAct=EBI-1573928, EBI-1573912;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:Q08AG7}. Cytoplasm, cytoskeleton,
CC spindle. Nucleus. Cytoplasm, cytoskeleton, phragmoplast. Nucleus
CC envelope. Note=Reorganized from the nucleus to the prospindle and the
CC preprophase band in late G2. After nuclear envelope breakdown,
CC localized on spindle and phragmoplast microtubules (MTs) and on the
CC reforming nuclear envelope of daughter cells. Present in mitotic
CC microtubule arrays. In interphase cortical arrays, gamma-tubulin
CC complexes are preferentially recruited to existing microtubules, from
CC which new microtubules are efficiently nucleated.
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques and flowers, and, to a
CC lower extent, in leaves, roots and seedlings, with highest levels in
CC young tissues and meristematic cells, and the vasculature.
CC {ECO:0000269|PubMed:22404201, ECO:0000269|PubMed:22427335}.
CC -!- DISRUPTION PHENOTYPE: In the gip1 gip2 double mutants, embryonic
CC lethality and impaired development of male gametophytes, severe growth
CC defects and sterility, characterized by microtubule (MT)
CC misorganization and abnormal spindle polarity, resulting in ploidy
CC defects. {ECO:0000269|PubMed:22404201, ECO:0000269|PubMed:22427335}.
CC -!- SIMILARITY: Belongs to the MOZART1 family. {ECO:0000305}.
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DR EMBL; AL161515; CAB78078.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82764.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66685.1; -; Genomic_DNA.
DR EMBL; BT010618; AAQ89640.1; -; mRNA.
DR EMBL; AK175417; BAD43180.1; -; mRNA.
DR PIR; E85097; E85097.
DR RefSeq; NP_001328567.1; NM_001340622.1.
DR RefSeq; NP_192693.1; NM_117023.4.
DR AlphaFoldDB; Q9M0N8; -.
DR PCDDB; Q9M0N8; -.
DR SMR; Q9M0N8; -.
DR BioGRID; 11838; 4.
DR IntAct; Q9M0N8; 1.
DR STRING; 3702.AT4G09550.1; -.
DR PaxDb; Q9M0N8; -.
DR PRIDE; Q9M0N8; -.
DR ProteomicsDB; 251011; -.
DR DNASU; 826539; -.
DR EnsemblPlants; AT4G09550.1; AT4G09550.1; AT4G09550.
DR EnsemblPlants; AT4G09550.2; AT4G09550.2; AT4G09550.
DR GeneID; 826539; -.
DR Gramene; AT4G09550.1; AT4G09550.1; AT4G09550.
DR Gramene; AT4G09550.2; AT4G09550.2; AT4G09550.
DR KEGG; ath:AT4G09550; -.
DR Araport; AT4G09550; -.
DR TAIR; locus:2133687; AT4G09550.
DR eggNOG; ENOG502S6UI; Eukaryota.
DR HOGENOM; CLU_160285_3_0_1; -.
DR InParanoid; Q9M0N8; -.
DR OMA; LSICVGM; -.
DR OrthoDB; 1645115at2759; -.
DR PhylomeDB; Q9M0N8; -.
DR PRO; PR:Q9M0N8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0N8; baseline and differential.
DR Genevisible; Q9M0N8; AT.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:TAIR.
DR GO; GO:0000931; C:gamma-tubulin large complex; IEA:InterPro.
DR GO; GO:0031021; C:interphase microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:TAIR.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:TAIR.
DR GO; GO:0072686; C:mitotic spindle; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IPI:TAIR.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IGI:TAIR.
DR GO; GO:0034508; P:centromere complex assembly; IGI:TAIR.
DR GO; GO:0033566; P:gamma-tubulin complex localization; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0051415; P:microtubule nucleation by interphase microtubule organizing center; IBA:GO_Central.
DR GO; GO:0051418; P:microtubule nucleation by microtubule organizing center; IDA:TAIR.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:TAIR.
DR InterPro; IPR022214; MZT1.
DR PANTHER; PTHR28520; PTHR28520; 1.
DR Pfam; PF12554; MOZART1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Reference proteome.
FT CHAIN 1..71
FT /note="Mitotic-spindle organizing protein 1B"
FT /id="PRO_0000365720"
SQ SEQUENCE 71 AA; 7835 MW; 9E0E18D6B61E22D1 CRC64;
MDEEASRTAR ESLELVFRMS NILDTGLDRH TLSVLIALCD LGVNPEALAT VVKELRRESI
PDSVTTTPSI H
