MZT1A_ARATH
ID MZT1A_ARATH Reviewed; 67 AA.
AC Q9C9T3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Mitotic-spindle organizing protein 1A;
DE AltName: Full=GCP3-interacting protein 2;
DE Short=AtGIP2;
DE AltName: Full=Mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1A;
DE Short=AtGIP1A;
GN Name=GIP2; Synonyms=GIP1A; OrderedLocusNames=At1g73790; ORFNames=F25P22.21;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH GIP1.
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: Part of the gamma-tubulin complex. Interacts with GIP1 and
CC GCP3. {ECO:0000269|PubMed:22404201, ECO:0000269|PubMed:22427335,
CC ECO:0000269|PubMed:24348487}.
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, 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; AC012679; AAG52087.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35509.1; -; Genomic_DNA.
DR EMBL; BT002967; AAO22776.1; -; mRNA.
DR EMBL; BT004410; AAO42404.1; -; mRNA.
DR EMBL; AY086832; AAM63880.1; -; mRNA.
DR PIR; C96765; C96765.
DR RefSeq; NP_565072.1; NM_106038.2.
DR AlphaFoldDB; Q9C9T3; -.
DR SMR; Q9C9T3; -.
DR BioGRID; 28933; 7.
DR IntAct; Q9C9T3; 5.
DR STRING; 3702.AT1G73790.1; -.
DR PaxDb; Q9C9T3; -.
DR PRIDE; Q9C9T3; -.
DR DNASU; 843714; -.
DR EnsemblPlants; AT1G73790.1; AT1G73790.1; AT1G73790.
DR GeneID; 843714; -.
DR Gramene; AT1G73790.1; AT1G73790.1; AT1G73790.
DR KEGG; ath:AT1G73790; -.
DR Araport; AT1G73790; -.
DR TAIR; locus:2027859; AT1G73790.
DR HOGENOM; CLU_160285_3_0_1; -.
DR InParanoid; Q9C9T3; -.
DR OMA; GREDSCP; -.
DR PhylomeDB; Q9C9T3; -.
DR PRO; PR:Q9C9T3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9T3; baseline and differential.
DR Genevisible; Q9C9T3; AT.
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:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
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: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 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..67
FT /note="Mitotic-spindle organizing protein 1A"
FT /id="PRO_0000365719"
SQ SEQUENCE 67 AA; 7359 MW; 24DC967E19735FB6 CRC64;
MNQEAAETAR ESLELVFRMS NILETGLDRH TLSVLIALCD IGLNPEALAT LVKELRRDSA
TTTTTVD
