CLASP_ARATH
ID CLASP_ARATH Reviewed; 1439 AA.
AC Q8RWY6; Q0WVK2; Q9SK81; Q9SL62;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=CLIP-associated protein;
DE Short=AtCLASP;
GN Name=CLASP; OrderedLocusNames=At2g20190/At2g20200;
GN ORFNames=T2G17.1/F11A3.25;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] OF 1-1031.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18042620; DOI=10.1242/jcs.024950;
RA Kirik V., Herrmann U., Parupalli C., Sedbrook J.C., Ehrhardt D.W.,
RA Huelskamp M.;
RT "CLASP localizes in two discrete patterns on cortical microtubules and is
RT required for cell morphogenesis and cell division in Arabidopsis.";
RL J. Cell Sci. 120:4416-4425(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17873093; DOI=10.1105/tpc.107.053777;
RA Ambrose J.C., Shoji T., Kotzer A.M., Pighin J.A., Wasteneys G.O.;
RT "The Arabidopsis CLASP gene encodes a microtubule-associated protein
RT involved in cell expansion and division.";
RL Plant Cell 19:2763-2775(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18716054; DOI=10.1091/mbc.e08-06-0665;
RA Ambrose J.C., Wasteneys G.O.;
RT "CLASP modulates microtubule-cortex interaction during self-organization of
RT acentrosomal microtubules.";
RL Mol. Biol. Cell 19:4730-4737(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21847104; DOI=10.1038/ncomms1444;
RA Ambrose C., Allard J.F., Cytrynbaum E.N., Wasteneys G.O.;
RT "A CLASP-modulated cell edge barrier mechanism drives cell-wide cortical
RT microtubule organization in Arabidopsis.";
RL Nat. Commun. 2:430-430(2011).
RN [11]
RP RETRACTED PAPER.
RX PubMed=22500804; DOI=10.1016/j.cell.2012.02.051;
RA Dhonukshe P., Weits D.A., Cruz-Ramirez A., Deinum E.E., Tindemans S.H.,
RA Kakar K., Prasad K., Maehoenen A.P., Ambrose C., Sasabe M., Wachsmann G.,
RA Luijten M., Bennett T., Machida Y., Heidstra R., Wasteneys G., Mulder B.M.,
RA Scheres B.;
RT "A PLETHORA-auxin transcription module controls cell division plane
RT rotation through MAP65 and CLASP.";
RL Cell 149:383-396(2012).
RN [12]
RP RETRACTION NOTICE OF PUBMED:22500804.
RX PubMed=24267897; DOI=10.1016/j.cell.2013.10.040;
RA Dhonukshe P., Weits D.A., Cruz-Ramirez A., Deinum E.E., Tindemans S.H.,
RA Kakar K., Prasad K., Maehoenen A.P., Ambrose C., Sasabe M., Wachsmann G.,
RA Luijten M., Bennett T., Machida Y., Heidstra R., Wasteneys G., Mulder B.M.,
RA Scheres B.;
RL Cell 155:1189-1189(2013).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Cortical microtubule plus-end tracking protein required for
CC cell morphogenesis and cell division. Promotes the stabilization of
CC dynamic microtubules during mitosis. Regulates microtubule-cortex
CC attachment, thereby contributing to self-organization of cortical
CC microtubules and subsequent cell shape. {ECO:0000269|PubMed:17873093,
CC ECO:0000269|PubMed:18042620, ECO:0000269|PubMed:18716054,
CC ECO:0000269|PubMed:21847104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17873093, ECO:0000269|PubMed:18042620}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:17873093}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:17873093}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:21847104}. Note=Associates with
CC cortical microtubules. {ECO:0000269|PubMed:18042620}.
CC -!- TISSUE SPECIFICITY: Expressed at a low level in all tissues, mostly in
CC young developing tissues. {ECO:0000269|PubMed:18042620}.
CC -!- DISRUPTION PHENOTYPE: Various plant growth reductions (e.g. dwarf),
CC cell form defects (e.g. reduced trichome branches number) and reduced
CC mitotic activity. Less root cortical microtubule arrays hypersensitive
CC to microtubule-destabilizing drugs. Aberrant microtubule preprophase
CC bands, mitotic spindles, and phragmoplasts.
CC {ECO:0000269|PubMed:17873093, ECO:0000269|PubMed:18042620,
CC ECO:0000269|PubMed:18716054}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- CAUTION: An article reported an auxin transcription module controlling
CC cell division plane rotation through CLASP; however, this paper was
CC later retracted. {ECO:0000305|PubMed:22500804,
CC ECO:0000305|PubMed:24267897}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21767.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20190 and At2g20200.; Evidence={ECO:0000305};
CC Sequence=AAD24379.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20190 and At2g20200.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006081; AAD24379.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006569; AAD21767.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06980.1; -; Genomic_DNA.
DR EMBL; AY091025; AAM13846.1; -; mRNA.
DR EMBL; AK226745; BAE98846.1; -; mRNA.
DR PIR; B84586; B84586.
DR PIR; C84586; C84586.
DR RefSeq; NP_849997.2; NM_179666.5.
DR AlphaFoldDB; Q8RWY6; -.
DR SMR; Q8RWY6; -.
DR BioGRID; 1893; 1.
DR STRING; 3702.AT2G20190.1; -.
DR iPTMnet; Q8RWY6; -.
DR PaxDb; Q8RWY6; -.
DR PRIDE; Q8RWY6; -.
DR ProteomicsDB; 246709; -.
DR EnsemblPlants; AT2G20190.1; AT2G20190.1; AT2G20190.
DR GeneID; 816539; -.
DR Gramene; AT2G20190.1; AT2G20190.1; AT2G20190.
DR KEGG; ath:AT2G20190; -.
DR Araport; AT2G20190; -.
DR TAIR; locus:2061599; AT2G20190.
DR eggNOG; KOG2956; Eukaryota.
DR HOGENOM; CLU_002943_0_0_1; -.
DR InParanoid; Q8RWY6; -.
DR OMA; MFMDTHT; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q8RWY6; -.
DR PRO; PR:Q8RWY6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWY6; baseline and differential.
DR Genevisible; Q8RWY6; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005876; C:spindle microtubule; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:TAIR.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:TAIR.
DR GO; GO:0050821; P:protein stabilization; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 2.
DR Pfam; PF02985; HEAT; 1.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Repeat.
FT CHAIN 1..1439
FT /note="CLIP-associated protein"
FT /id="PRO_0000421378"
FT REPEAT 1..32
FT /note="HEAT 1"
FT REPEAT 36..74
FT /note="HEAT 2"
FT REPEAT 77..115
FT /note="HEAT 3"
FT REPEAT 154..192
FT /note="HEAT 4"
FT REPEAT 281..319
FT /note="HEAT 5"
FT REPEAT 325..363
FT /note="HEAT 6"
FT REPEAT 366..401
FT /note="HEAT 7"
FT REPEAT 402..439
FT /note="HEAT 8"
FT REPEAT 486..525
FT /note="HEAT 9"
FT REPEAT 809..830
FT /note="HEAT 10"
FT REPEAT 831..869
FT /note="HEAT 11"
FT REPEAT 872..910
FT /note="HEAT 12"
FT REPEAT 912..950
FT /note="HEAT 13"
FT REPEAT 954..992
FT /note="HEAT 14"
FT REPEAT 994..1031
FT /note="HEAT 15"
FT REPEAT 1201..1239
FT /note="HEAT 16"
FT REPEAT 1246..1284
FT /note="HEAT 17"
FT REPEAT 1287..1325
FT /note="HEAT 18"
FT REPEAT 1327..1360
FT /note="HEAT 19"
FT REPEAT 1364..1402
FT /note="HEAT 20"
FT REPEAT 1405..1439
FT /note="HEAT 21"
FT REGION 238..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1439 AA; 158951 MW; 95F849CCFBE07B13 CRC64;
MEEALEMARA KDTKERMAAV ERLHQLLEAS RKSLSPAEVT SLVDSCLDLL KDSNFRVSQG
ALQALASAAV LAGEHLKLHL NALVPAVVER LGDSKQPVRD AARRLLTTLM EVSSPTIIVE
RAGSYAWMHK SWRVREEFAR TVTSAIGLFA STELPLQRVI LAPILQMLND PNQAVREAAI
LCIEEMYMQG GSQFREELQR HHLPSYMVKD INARLERIEP QLRSTDGRSA HHVVNEVKAS
SVNPKKSSPR AKAPTRENSL FGGDADITEK PIEPIKVYSE KELIREFEKI AATLVPEKDW
SMRISAMRRV EGLVAGGATD YSCFRGLLKQ LVGPLSTQLA DRRSTIVKQA CHLLCLLSKE
LLGDFEACAE TFIPVLFKLV VITVLVIAES ADNCIKTMLR NCKAARVLPR IAESAKHDRN
AILRARCCEY ALLTLEHWPD APEIQRSVDL YEDLIRCCVA DAMSEVRATA RMCYRMFAKT
WPDRSRRLFS SFDPVIQRLI NEEDGGIHRR HASPSVRERH SQPSFSQTSA PSNLPGYGTS
AIVAMDRSSN LSSGGSLSSG LLLSQSKDVN KGSERSLESV LQSSKQKVSA IESMLRGLHI
SDRQNPAALR SSSLDLGVDP PSSRDPPFHA VAPASNSHTS SAAAESTHSI NKGSNRNGGL
GLSDIITQIQ ASKDSGRSSY RGNLLSESHP TFSSLTAKRG SERNERSSLE ESNDAREVRR
FMAGHFDRQQ MDTAYRDLTF RESNASHVPN FQRPLLRKNV GGRMSAGRRR SFDDSQLQIG
DISNFVDGPA SLNEALNDGL NSSSDWCARV AAFNFLQTLL QQGPKGAQEV IQSFEKVMKL
FLRHLDDPHH KVAQAALSTL ADLIPSCRKP FESYMERVLP HVFSRLIDPK EVVRQPCSST
LEIVSKTYSV DSLLPALLRS LDEQRSPKAK LAVIEFAINS FNRYAGNPEI SGNSGILKLW
LAKLTPLTRD KNTKLKEASI TCIISVYNHY DSAGLLNYIL SLSVEEQNSL RRALKQYTPR
IEVDLLNYMQ SKKEKQRIKS YDPSDAIGTS SEEGYAGASK KNIFLGRYSG GSIDSDSGRK
WSSSQEPTMI TGGVGQNVSS GTQEKLYQNV RTGISSASDL LNPKDSDYTF ASAGQNSISR
TSPNGSSENI EILDDLSPPH LEKNGLNLTS VDSLEGRHEN EVSRELDLGH YMLTSIKVNT
TPESGPSIPQ ILHMINGSDG SPSSSKKSGL QQLIEASVAN EESVWTKYFN QILTVVLEVL
DDEDFSIKEL ALSLISEMLK SQKDAMEDSV EIVIEKLLHV SKDTVPKVST EAEQCLTTVL
SQYDPFRCLS VIVPLLVTED EKTLVACINC LTKLVGRLSQ EELMDQLSSF LPAVFEAFGS
QSADVRKTVV FCLVDIYIML GKAFLPYLEG LNSTQVRLVT IYANRISQAR NGAPIDADT
