KTNA1_ARATH
ID KTNA1_ARATH Reviewed; 523 AA.
AC Q9SEX2; Q8S9E4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000255|HAMAP-Rule:MF_03023};
DE AltName: Full=CAD ATPase;
DE AltName: Full=Katanin-1 {ECO:0000303|PubMed:11283338};
DE Short=AtKTN1 {ECO:0000303|PubMed:11283338};
DE AltName: Full=Katanin-like microtubule-severing protein {ECO:0000303|PubMed:12571277};
DE Short=AtKSS {ECO:0000303|PubMed:12571277};
DE AltName: Full=Protein BOTERO 1 {ECO:0000303|PubMed:11169190};
DE AltName: Full=Protein ECTOPIC ROOT HAIR 3 {ECO:0000303|PubMed:11782406};
DE AltName: Full=Protein FAT ROOT {ECO:0000303|Ref.3};
DE AltName: Full=Protein FRAGILE FIBER 2 {ECO:0000303|PubMed:11283338};
DE Short=AtAAA1 {ECO:0000303|Ref.2};
DE AltName: Full=p60 katanin {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000303|PubMed:12020351};
DE Short=Atp60 {ECO:0000303|PubMed:12020351};
GN Name=AAA1 {ECO:0000303|Ref.2};
GN Synonyms=BOT1 {ECO:0000303|PubMed:11169190},
GN ERH3 {ECO:0000303|PubMed:11782406}, FRA2 {ECO:0000303|PubMed:11283338},
GN FTR {ECO:0000303|Ref.3}, KSS {ECO:0000303|PubMed:12571277},
GN KTN1 {ECO:0000303|PubMed:11283338}, LUE1 {ECO:0000303|PubMed:12571277};
GN OrderedLocusNames=At1g80350 {ECO:0000312|Araport:AT1G80350};
GN ORFNames=F5I6.10 {ECO:0000312|EMBL:AAG52435.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11283338; DOI=10.2307/3871342;
RA Burk D.H., Liu B., Zhong R., Morrison W.H., Ye Z.-H.;
RT "A katanin-like protein regulates normal cell wall biosynthesis and cell
RT elongation.";
RL Plant Cell 13:807-827(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chandler J.S., McArdler B.R., Callis C.;
RT "AtAAA1 is a member of a family of ATPases associated with diverse, often
RT ubiquitin pathway related functions.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Matsui K., Wada T., Ishiguro S., Okada K.;
RT "Characterization of the fat root mutant in Arabidopsis.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=11169190; DOI=10.1046/j.1365-313x.2001.00946.x;
RA Bichet A., Desnos T., Turner S., Grandjean O., Hofte H.;
RT "BOTERO1 is required for normal orientation of cortical microtubules and
RT anisotropic cell expansion in Arabidopsis.";
RL Plant J. 25:137-148(2001).
RN [8]
RP FUNCTION.
RX PubMed=12020351; DOI=10.1042/bj20020689;
RA Stoppin-Mellet V., Gaillard J., Vantard M.;
RT "Functional evidence for in vitro microtubule severing by the plant katanin
RT homologue.";
RL Biochem. J. 365:337-342(2002).
RN [9]
RP FUNCTION.
RX PubMed=11782406; DOI=10.1242/dev.129.1.123;
RA Webb M., Jouannic S., Foreman J., Linstead P., Dolan L.;
RT "Cell specification in the Arabidopsis root epidermis requires the activity
RT of ECTOPIC ROOT HAIR 3-a katanin-p60 protein.";
RL Development 129:123-131(2002).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KTN80.1 AND KIN14A.
RX PubMed=12571277; DOI=10.1242/jcs.00274;
RA Bouquin T., Mattsson O., Naested H., Foster R., Mundy J.;
RT "The Arabidopsis lue1 mutant defines a katanin p60 ortholog involved in
RT hormonal control of microtubule orientation during cell growth.";
RL J. Cell Sci. 116:791-801(2003).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUBUNIT, INTERACTION WITH KTN80.1; KTN80.2; KTN80.3 AND KTN80.4, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=28978669; DOI=10.15252/embj.201796823;
RA Wang C., Liu W., Wang G., Li J., Dong L., Han L., Wang Q., Tian J., Yu Y.,
RA Gao C., Kong Z.;
RT "KTN80 confers precision to microtubule severing by specific targeting of
RT katanin complexes in plant cells.";
RL EMBO J. 36:3435-3447(2017).
CC -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner.
CC Required for oligomerization of functional KTN80-KTN1 complexes that
CC catalyze microtubule severing (PubMed:28978669). This activity may
CC promote rapid reorganization of cellular microtubule arrays. May be
CC required for reorientation of cortical microtubule arrays during
CC cellular elongation. Failure to correctly orient these arrays
CC drastically compromises fiber length, cell wall thickness and
CC mechanical strength. May also be required for the spatial organization
CC of developmental cues within the root. {ECO:0000269|PubMed:11169190,
CC ECO:0000269|PubMed:11283338, ECO:0000269|PubMed:11782406,
CC ECO:0000269|PubMed:12020351, ECO:0000269|PubMed:12571277,
CC ECO:0000269|PubMed:28978669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03023};
CC -!- SUBUNIT: May homooligomerize (PubMed:12571277). Component of KTN80-KTN1
CC complexes composed of a hexamer of KTN1-KTN80 heterodimers that sense
CC microtubule (MT) geometry to confer precise MT severing
CC (PubMed:28978669). Interacts directly with KTN80.1, KTN80.2, KTN80.3
CC and KTN80.4 (PubMed:28978669). Can interact with KTN80.1
CC (PubMed:12571277). May interact with the kinesin related protein KIN14A
CC (PubMed:12571277). Interacts with microtubule polymers
CC (PubMed:12571277). {ECO:0000269|PubMed:12571277,
CC ECO:0000269|PubMed:28978669}.
CC -!- INTERACTION:
CC Q9SEX2; Q9LX99: KIN14A; NbExp=3; IntAct=EBI-2025583, EBI-2025621;
CC Q9SEX2; F4HTH8: KTN80.2; NbExp=3; IntAct=EBI-2025583, EBI-2025609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03023, ECO:0000269|PubMed:12571277,
CC ECO:0000269|PubMed:28978669}. Note=Present in dynamic discrete
CC particles specifically localized to microtubule (MT) crossovers and
CC branching nucleation sites, in a KTN80s-dependent manner.
CC {ECO:0000269|PubMed:28978669}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, including siliques,
CC flowers, leaves, stems and roots. {ECO:0000269|PubMed:11283338,
CC ECO:0000269|PubMed:28978669}.
CC -!- DISRUPTION PHENOTYPE: Severe dwarf phenotype, with small and round
CC dark-green rosette leaves as well as wide and short petioles.
CC {ECO:0000269|PubMed:28978669}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03023}.
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DR EMBL; AF358779; AAK51051.1; -; mRNA.
DR EMBL; AF359248; AAK54074.1; -; Genomic_DNA.
DR EMBL; AF048706; AAF21247.1; -; mRNA.
DR EMBL; AB044785; BAB87822.1; -; mRNA.
DR EMBL; AC018848; AAG52435.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36390.1; -; Genomic_DNA.
DR EMBL; AY059919; AAL24401.1; -; mRNA.
DR EMBL; BT000149; AAN15468.1; -; mRNA.
DR PIR; B96835; B96835.
DR RefSeq; NP_178151.1; NM_106684.5.
DR AlphaFoldDB; Q9SEX2; -.
DR SMR; Q9SEX2; -.
DR BioGRID; 29593; 3.
DR IntAct; Q9SEX2; 2.
DR STRING; 3702.AT1G80350.1; -.
DR iPTMnet; Q9SEX2; -.
DR PaxDb; Q9SEX2; -.
DR PRIDE; Q9SEX2; -.
DR ProteomicsDB; 237036; -.
DR EnsemblPlants; AT1G80350.1; AT1G80350.1; AT1G80350.
DR GeneID; 844375; -.
DR Gramene; AT1G80350.1; AT1G80350.1; AT1G80350.
DR KEGG; ath:AT1G80350; -.
DR Araport; AT1G80350; -.
DR TAIR; locus:2034230; AT1G80350.
DR eggNOG; KOG0738; Eukaryota.
DR HOGENOM; CLU_000688_21_1_1; -.
DR InParanoid; Q9SEX2; -.
DR OMA; YEKWMSE; -.
DR OrthoDB; 717356at2759; -.
DR PhylomeDB; Q9SEX2; -.
DR BRENDA; 5.6.1.1; 399.
DR PRO; PR:Q9SEX2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SEX2; baseline and differential.
DR Genevisible; Q9SEX2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0051013; P:microtubule severing; IMP:UniProtKB.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Isomerase; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..523
FT /note="Katanin p60 ATPase-containing subunit A1"
FT /id="PRO_0000084600"
FT REGION 82..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 279..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03023"
FT CONFLICT 5
FT /note="S -> N (in Ref. 3; BAB87822)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> S (in Ref. 3; BAB87822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57236 MW; 2AE8813109DC972B CRC64;
MVGSSNSLAG LQDHLKLARE YALEGSYDTS VIFFDGAIAQ INKHLNTLDD PLARTKWMNV
KKAIMEETEV VKQLDAERRA FKEAPTGRRA ASPPINTKSS FVFQPLDEYP TSSGGGPMDD
PDVWRPPTRD VTSRRPARAG QTGTRKSPQD GAWARGPTTR TGPASRGGRG GATSKSTAGA
RSSTAGKKGA ASKSNKAESM NGDAEDGKSK RGLYEGPDED LAAMLERDVL DSTPGVRWDD
VAGLSEAKRL LEEAVVLPLW MPEYFQGIRR PWKGVLMFGP PGTGKTLLAK AVATECGTTF
FNVSSATLAS KWRGESERMV RCLFDLARAY APSTIFIDEI DSLCNSRGGS GEHESSRRVK
SELLVQVDGV SNTATNEDGS RKIVMVLAAT NFPWDIDEAL RRRLEKRIYI PLPDFESRKA
LININLRTVE VASDVNIEDV ARRTEGYSGD DLTNVCRDAS MNGMRRKIAG KTRDEIKNMS
KDDISNDPVA MCDFEEAIRK VQPSVSSSDI EKHEKWLSEF GSA
