KTN83_ARATH
ID KTN83_ARATH Reviewed; 839 AA.
AC F4KB17; Q0WV51; Q9FT96;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.3 {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000303|PubMed:28978669};
GN Name=KTN80.3 {ECO:0000303|PubMed:28978669};
GN OrderedLocusNames=At5g08390 {ECO:0000312|Araport:AT5G08390};
GN ORFNames=F8L15.120 {ECO:0000312|EMBL:CAC08339.1};
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].
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;
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 [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 KTN80.4, 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). Microtubule severing may promote
CC rapid reorganization of cellular microtubule arrays (By similarity).
CC Confers precision to microtubule (MT) severing by specific targeting of
CC KTN1 to MT cleavage sites such as crossover or branching nucleation
CC sites (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 KTN80.1, and weakly with KTN80.4 (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 -!- TISSUE SPECIFICITY: Expressed in siliques, flowers, leaves, stems and
CC roots. {ECO:0000269|PubMed:28978669}.
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 -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC08339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL392174; CAC08339.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91294.1; -; Genomic_DNA.
DR EMBL; AK226925; BAE98997.1; -; mRNA.
DR RefSeq; NP_568194.2; NM_120923.3.
DR AlphaFoldDB; F4KB17; -.
DR SMR; F4KB17; -.
DR STRING; 3702.AT5G08390.1; -.
DR TCDB; 8.A.92.1.12; the g-protein AlphaBetaGama complex (gpc) family.
DR PaxDb; F4KB17; -.
DR PRIDE; F4KB17; -.
DR ProteomicsDB; 209819; -.
DR EnsemblPlants; AT5G08390.1; AT5G08390.1; AT5G08390.
DR GeneID; 830737; -.
DR Gramene; AT5G08390.1; AT5G08390.1; AT5G08390.
DR KEGG; ath:AT5G08390; -.
DR Araport; AT5G08390; -.
DR TAIR; locus:2150788; AT5G08390.
DR eggNOG; KOG0267; Eukaryota.
DR HOGENOM; CLU_007811_0_0_1; -.
DR InParanoid; F4KB17; -.
DR OMA; IMGQHDQ; -.
DR OrthoDB; 425951at2759; -.
DR PRO; PR:F4KB17; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KB17; baseline and differential.
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 Cytoplasm; Cytoskeleton; Microtubule; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..839
FT /note="Katanin p80 WD40 repeat-containing subunit B1
FT homolog KTN80.3"
FT /id="PRO_0000450715"
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 303..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..648
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 303..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 688
FT /note="R -> L (in Ref. 3; BAE98997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 91607 MW; C7D1689079ACD0DB CRC64;
MNTKRAYKLQ EFVAHSAAVN CLKIGRKSSR VLVTGGEDHK VNLWAIGKPN AILSLYGHSS
GIDSVTFDAS EGLVAAGAAS GTIKLWDLEE AKVVRTLTGH RSNCVSVNFH PFGEFFASGS
LDTNLKIWDI RKKGCIHTYK GHTRGVNVLR FTPDGRWIVS GGEDNVVKVW DLTAGKLLHE
FKSHEGKIQS LDFHPHEFLL ATGSADKTVK FWDLETFELI GSGGTETTGV RCLTFNPDGK
SVLCGLQESL KIFSWEPIRC HDGVDVGWSN LSDMNVHEGK LLGCSYNQNC VGVWVVDLSR
TEPMSGGATQ SNSHPEKTSG SGRDQAGLND NSSKVILGKL PGSQKVDPLL KETKSLGKLS
VSQNSDPLPK DTKSTGRSSV SQSSDPLVKE PKPLGRFSAT HSSDTVKESR TLSSTGSVSD
SPHRVTLTSA PKSASGISTV VPNAAASKRN FGKANPKANP PVVNKEDYFP VIVPRTEPII
EQASESRAEL DIIGRTMPYS LQSKAADSRR LSSSRNEPDL PTSSLLERSQ SQPIEPITLQ
DGNTYPSDEG GSWDTAERTN KESKCRVFGR FNSRSLVRSP PRNHDENSDL ISYNANRDSS
PTESRKGGRL HSLVLNRERR GRFSNFEGPV SSSSGGNMTA PNSRPSNMLK QRGNHVPVDQ
GITSASEEDI VADIMGQHDQ FVSSMHSRLA KLQVVRRYWE RNDIKNSISS IEKMADNAVI
ADVLLIVNER PEILTLDTCT SLLPLLTALL GSNMDSHLSV CLDLLLKLVR MYGSQIYSSL
SAPSSVGVDI EAEQRMERYS CCFVEFEKIK ACLPSLARRG NLVAKTLHEL NLTFQEVSS
