GACP2_ARATH
ID GACP2_ARATH Reviewed; 678 AA.
AC Q9C5H9; F4KGZ8; Q9LF43;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Gamma-tubulin complex component 2;
DE Short=AtGCP2;
DE Short=GCP-2;
DE AltName: Full=Protein SPIRAL 3;
DE AltName: Full=Spindle pole body protein Spc97 homolog;
DE Short=AtSpc97;
GN Name=GCP2; Synonyms=SPC97, SPR3; OrderedLocusNames=At5g17410;
GN ORFNames=T10B6.70;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 SUBCELLULAR LOCATION, SUBUNIT, AND NUCLEUS ENVELOPE LOCALIZATION REGIONS.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH GCP3, AND MUTAGENESIS OF
RP GLY-305.
RC STRAIN=cv. Wassilewskija;
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 [6]
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 [7]
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).
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 {ECO:0000269|PubMed:19509058, ECO:0000269|PubMed:20935636}.
CC -!- SUBUNIT: Part of the gamma-tubulin complex. Gamma-tubulin complex is
CC composed of gamma-tubulin and GCP proteins (e.g. GCP2 and GCP3).
CC Interacts directly with GCP3. {ECO:0000269|PubMed:17714428,
CC ECO:0000269|PubMed:19509058, ECO:0000269|PubMed:20935636}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center {ECO:0000250|UniProtKB:Q9BSJ2}. Nucleus envelope. Cytoplasm.
CC Cytoplasm, cell cortex. Note=Associated to motile complexes in the
CC cytosol that transiently stabilized at fixed locations in the cell
CC cortex (e.g. along the outer periclinal edge of newly formed
CC crosswalls) from which microtubules grow away prior to microtubules
CC nucleation. Colocalizes with gamma-tubulin at the nuclear surface where
CC microtubules are nucleated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5H9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5H9-2; Sequence=VSP_054536;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. Impaired development of male
CC and female gametophytes. {ECO:0000269|PubMed:19509058}.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01736.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391142; CAC01736.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92422.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92423.1; -; Genomic_DNA.
DR EMBL; AF360238; AAK25948.1; -; mRNA.
DR EMBL; AY040037; AAK64095.1; -; mRNA.
DR PIR; T51578; T51578.
DR RefSeq; NP_568346.1; NM_121747.4. [Q9C5H9-1]
DR RefSeq; NP_850838.1; NM_180507.2. [Q9C5H9-2]
DR AlphaFoldDB; Q9C5H9; -.
DR SMR; Q9C5H9; -.
DR BioGRID; 16883; 2.
DR IntAct; Q9C5H9; 1.
DR STRING; 3702.AT5G17410.2; -.
DR PaxDb; Q9C5H9; -.
DR PRIDE; Q9C5H9; -.
DR ProteomicsDB; 230443; -. [Q9C5H9-1]
DR EnsemblPlants; AT5G17410.1; AT5G17410.1; AT5G17410. [Q9C5H9-1]
DR EnsemblPlants; AT5G17410.2; AT5G17410.2; AT5G17410. [Q9C5H9-2]
DR GeneID; 831607; -.
DR Gramene; AT5G17410.1; AT5G17410.1; AT5G17410. [Q9C5H9-1]
DR Gramene; AT5G17410.2; AT5G17410.2; AT5G17410. [Q9C5H9-2]
DR KEGG; ath:AT5G17410; -.
DR Araport; AT5G17410; -.
DR TAIR; locus:2178930; AT5G17410.
DR eggNOG; KOG2001; Eukaryota.
DR HOGENOM; CLU_007738_1_1_1; -.
DR OMA; SKLMTCC; -.
DR OrthoDB; 679187at2759; -.
DR PhylomeDB; Q9C5H9; -.
DR PRO; PR:Q9C5H9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5H9; baseline and differential.
DR Genevisible; Q9C5H9; 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:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:UniProtKB.
DR GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; 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:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0033566; P:gamma-tubulin complex localization; IMP:UniProtKB.
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: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 Alternative splicing; Cytoplasm; Cytoskeleton; Developmental protein;
KW Microtubule; Nucleus; Reference proteome.
FT CHAIN 1..678
FT /note="Gamma-tubulin complex component 2"
FT /id="PRO_0000428969"
FT REGION 63..116
FT /note="Triggers nucleus envelope localization"
FT REGION 118..180
FT /note="Triggers nucleus envelope localization"
FT REGION 290..318
FT /note="Triggers nucleus envelope localization"
FT REGION 472..548
FT /note="Triggers nucleus envelope localization"
FT REGION 587..622
FT /note="Triggers nucleus envelope localization"
FT VAR_SEQ 45
FT /note="D -> DS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054536"
FT MUTAGEN 305
FT /note="G->R: In spr3; right-handed helical growth due to
FT anisotropic cell expansion and abnormal microtubule
FT branching characterized by wider and divergently
FT distributed nucleating angles. Impaired interaction with
FT GCP3."
FT /evidence="ECO:0000269|PubMed:19509058"
SQ SEQUENCE 678 AA; 76946 MW; 02D4392BFA8B0ADA CRC64;
MESMTPISCP TTPRWNQDRP FLTGRFHQET RASSKFADSK RFTLDSSSSG VEQAIGCYDT
PVQELIVIDD LLSALVGIEG RYISIKRFHG KEDSIAFQVD PSMDLALQEL AKRIFPLCEY
YLLIDQFVES SSQFKNGLVN HAFAAALRAL LLDYQAMVAQ LEHQFRLGRL SIQGLWFYCQ
PMMGSMRALA AVIQQASTKQ FVGSGVLNLL QSQAKAMAGD NSVRSLLEKM TECASNAYLS
ILERWVYEGI IDDPYGEFFI AENRSLKKES LSQDSTAKYW SQRYSLKDTI PGFLANIAAT
ILTTGKYLNV MRECGHNVQV PISERSKLTI FGSNHHYLEC IKAAHEFASI ELVNLIKDKY
DLVGRLRSIK HYLLLDQGDF LVHFMDIARE ELNKKVHEIS VEKLQSLLDL ALRTTAAAAD
PRHEDLTCCV DRASLLTTLG MHKDTDSNSI EDPMSITGLE TFSLSYKVQW PLSIVISKKA
LSKYQLIFRF LFHCKHVERQ LCGAWQIHQG IRSMNSKGTA ILRSSLLCRS MLKFISSLLH
YLTFEVLEPN WHVMHDRLQS TRSVDEVIQH HDFFLDKCLR GCLLLLPDVL KKMEKLKSVC
LQYAAATQWL ISSSIDINSQ SHPQKTMIRD TTVTESIFNF EREFNSELQS LGPVLSKGSQ
AEPYLTHLSQ WILGVSKE
