KTN84_ARATH
ID KTN84_ARATH Reviewed; 837 AA.
AC Q8H0T9; Q9FHL5;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 3.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.4 {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000303|PubMed:28978669};
GN Name=KTN80.4 {ECO:0000303|PubMed:28978669};
GN OrderedLocusNames=At5g23430 {ECO:0000312|Araport:AT5G23430};
GN ORFNames=K19M13.6 {ECO:0000312|EMBL:BAB09559.1};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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] (ISOFORM 1).
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 DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [5]
RP GENE FAMILY.
RX PubMed=18552200; DOI=10.1105/tpc.108.058891;
RA Zhang Y., Feng S., Chen F., Chen H., Wang J., McCall C., Xiong Y.,
RA Deng X.W.;
RT "Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin
RT ligase with DDB1 and CUL4 that is involved in multiple plant developmental
RT processes.";
RL Plant Cell 20:1437-1455(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUBUNIT, INTERACTION WITH AAA1/KTN1; KTN80.1 AND KTN80.3, GENE FAMILY, AND
RP 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: May participate in a complex which severs microtubules in an
CC ATP-dependent manner (By similarity). This activity may promote rapid
CC reorganization of cellular microtubule arrays (By similarity). Confers
CC precision to microtubule (MT) severing by specific targeting of KTN1 to
CC MT cleavage sites such as crossover or branching nucleation sites
CC (PubMed:28978669). Together with other KTN80s, regulates cell
CC elongation by modulating MT organization (PubMed:28978669).
CC {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}.
CC -!- SUBUNIT: Component of KTN80-KTN1 complexes composed of a hexamer of
CC KTN1-KTN80 heterodimers that sense microtubule (MT) geometry to confer
CC precise MT severing (PubMed:28978669). Interacts directly with
CC AAA1/KTN1, and weakly with KTN80.1 and KTN80.3 (PubMed:28978669).
CC {ECO:0000269|PubMed:28978669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03022, ECO:0000269|PubMed:28978669}. Note=Present in dynamic
CC discrete particles specifically localized to microtubule (MT)
CC crossovers and branching nucleation sites.
CC {ECO:0000269|PubMed:28978669}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H0T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H0T9-2; Sequence=VSP_015092;
CC -!- TISSUE SPECIFICITY: Expressed in siliques, flowers, leaves, stems and
CC roots. {ECO:0000269|PubMed:28978669}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: The double mutant ktn80.3 ktn80.4 exhibits normal
CC growth, but the quadruple mutant ktn80.1 ktn80.2 ktn80.3 ktn80.4 has a
CC severe dwarf phenotype, with small and round dark-green rosette leaves
CC as well as wide and short petioles, probably due to cell elongation
CC defects, and associated with a complex cortical microtubule (MT)
CC network with stable entanglements (PubMed:28978669). Plants missing
CC KTN80s have a disruption of KTN1 recruitment at MT crossover or
CC branching nucleation sites, leading to an abolishment of MT severing
CC (PubMed:28978669). {ECO:0000269|PubMed:28978669}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018110; BAB09559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93166.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93167.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69335.1; -; Genomic_DNA.
DR EMBL; BT002053; AAN72064.1; -; mRNA.
DR RefSeq; NP_001318628.1; NM_001343802.1. [Q8H0T9-2]
DR RefSeq; NP_197734.2; NM_122250.2. [Q8H0T9-2]
DR RefSeq; NP_851064.1; NM_180733.2. [Q8H0T9-1]
DR AlphaFoldDB; Q8H0T9; -.
DR SMR; Q8H0T9; -.
DR BioGRID; 17684; 3.
DR IntAct; Q8H0T9; 1.
DR STRING; 3702.AT5G23430.1; -.
DR iPTMnet; Q8H0T9; -.
DR PaxDb; Q8H0T9; -.
DR PRIDE; Q8H0T9; -.
DR ProteomicsDB; 237033; -. [Q8H0T9-1]
DR EnsemblPlants; AT5G23430.1; AT5G23430.1; AT5G23430. [Q8H0T9-1]
DR EnsemblPlants; AT5G23430.2; AT5G23430.2; AT5G23430. [Q8H0T9-2]
DR EnsemblPlants; AT5G23430.3; AT5G23430.3; AT5G23430. [Q8H0T9-2]
DR GeneID; 832409; -.
DR Gramene; AT5G23430.1; AT5G23430.1; AT5G23430. [Q8H0T9-1]
DR Gramene; AT5G23430.2; AT5G23430.2; AT5G23430. [Q8H0T9-2]
DR Gramene; AT5G23430.3; AT5G23430.3; AT5G23430. [Q8H0T9-2]
DR KEGG; ath:AT5G23430; -.
DR Araport; AT5G23430; -.
DR TAIR; locus:2154438; AT5G23430.
DR eggNOG; KOG0267; Eukaryota.
DR HOGENOM; CLU_007811_0_0_1; -.
DR InParanoid; Q8H0T9; -.
DR OMA; CNTGDAD; -.
DR OrthoDB; 425951at2759; -.
DR PhylomeDB; Q8H0T9; -.
DR PRO; PR:Q8H0T9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H0T9; baseline and differential.
DR Genevisible; Q8H0T9; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0008352; C:katanin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051013; P:microtubule severing; IMP:UniProtKB.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR HAMAP; MF_03022; Katanin_p80_B1; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR028021; Katanin_C-terminal.
DR InterPro; IPR026962; KTNB1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..837
FT /note="Katanin p80 WD40 repeat-containing subunit B1
FT homolog KTN80.4"
FT /id="PRO_0000051054"
FT REPEAT 14..54
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 57..96
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 99..138
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 141..182
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 184..222
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 225..265
FT /note="WD 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 267..304
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 307..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..131
FT /note="DWD box"
FT /evidence="ECO:0000305|PubMed:18223036"
FT COMPBIAS 358..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 816
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015092"
SQ SEQUENCE 837 AA; 91434 MW; B36AF7681770B08A CRC64;
MTTKRAYKLQ EFVAHSAAVN CLKIGRKSSR VLVTGGEDHK VNLWAIGKPN AILSLYGHSS
GIDSVTFDAS EVLVAAGAAS GTIKLWDLEE AKIVRTLTGH RSNCISVDFH PFGEFFASGS
LDTNLKIWDI RKKGCIHTYK GHTRGVNVLR FTPDGRWVVS GGEDNIVKVW DLTAGKLLTE
FKSHEGQIQS LDFHPHEFLL ATGSADRTVK FWDLETFELI GSGGPETAGV RCLSFNPDGK
TVLCGLQESL KIFSWEPIRC HDGVDVGWSR LSDMNVHEGK LLGCSYNQSC VGVWVVDLSR
TEPCMAGDTA QSNGHPEKRS CSGRDPVVLN DNNSKTVLGK LSVSQNVDPL LKETKSLGRL
SVSQNSDPST KETKSIGRSS TSQNSESSMK ESKPLGRLSV SQNSDVSKES RTFSSTGSLP
GTPHRVSSTN VSKATSGVST AVSNAATSRR NFTKANPKAN PVNKAADFAP VIVPRADPRI
EQATESRAEL DIIARTMPYS LQAADSRRSP SSRNNPDLPD ASVLEMSESQ PVEPNNIPDG
GTLPGGKVGM RGATERSIND FRYKRYGRSN SRSRMGSPPR NHDENYDLVS HRSNRDPSPT
ESQKGGRFQS LVINRERRGR FSNFEGPVSN FSSGNMPAPN IRPSNMFKQR GNHMPVEQGI
DSPSEENIVE DIMGKHNQFV SSMQSRLAKL QVVRRYWERN DVKNSIGSIE KMADNAVTAD
VLGIITERNE ILTLDNCTSL LPLLTALLGS GMDQHLSVSL DLLLKLVRLY GSPIYSSLSA
PASVGVDIEA EQRIERYSRC FVELEKVKAC LPSLARRGGL VAKSVLELNL AFQEVSS
