KTN81_ARATH
ID KTN81_ARATH Reviewed; 1019 AA.
AC A0A1P8AW69; Q9SXA3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.1 {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000303|PubMed:28978669};
GN Name=KTN80.1 {ECO:0000303|PubMed:28978669};
GN OrderedLocusNames=At1g11160 {ECO:0000312|Araport:AT1G11160};
GN ORFNames=T28P6.17 {ECO:0000312|EMBL:AAD49999.1};
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=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 [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 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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUBUNIT, INTERACTION WITH AAA1/KTN1; KTN80.3 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 KTN80.3, 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 at low levels in siliques, flowers,
CC leaves, stems and roots. {ECO:0000269|PubMed:28978669}.
CC -!- DISRUPTION PHENOTYPE: The double mutant ktn80.1 ktn80.2 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=AAD49999.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007259; AAD49999.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM60883.1; -; Genomic_DNA.
DR PIR; E86245; E86245.
DR RefSeq; NP_001323134.1; NM_001331961.1.
DR AlphaFoldDB; A0A1P8AW69; -.
DR SMR; A0A1P8AW69; -.
DR ProteomicsDB; 206259; -.
DR EnsemblPlants; AT1G11160.2; AT1G11160.2; AT1G11160.
DR GeneID; 837657; -.
DR Gramene; AT1G11160.2; AT1G11160.2; AT1G11160.
DR KEGG; ath:AT1G11160; -.
DR Araport; AT1G11160; -.
DR PRO; PR:A0A1P8AW69; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8AW69; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0008352; C:katanin complex; IEA:InterPro.
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: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; 3.
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..1019
FT /note="Katanin p80 WD40 repeat-containing subunit B1
FT homolog KTN80.1"
FT /id="PRO_0000450713"
FT REPEAT 13..53
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 56..95
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 98..137
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 140..181
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 183..221
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 224..264
FT /note="WD 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03022"
FT REPEAT 266..303
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 388..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..130
FT /note="DWD box"
FT /evidence="ECO:0000305|PubMed:18223036"
FT COMPBIAS 551..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 112385 MW; 575DC59CB862C757 CRC64;
MAKRGYKLQE FVAHSGNVNC LSIGKKTSRL LLTGGDDYKV NLWSIGKTTS PMSLCGHTSP
VDSVAFNSEE VLVLAGASSG VIKLWDLEES KMVRAFTGHR SNCSAVEFHP FGEFLASGSS
DTNLRVWDTR KKGCIQTYKG HTRGISTIEF SPDGRWVVSG GLDNVVKVWD LTAGKLLHEF
KCHEGPIRSL DFHPLEFLLA TGSADRTVKF WDLETFELIG TTRPEATGVR AIAFHPDGQT
LFCGLDDGLK VYSWEPVICR DGVDMGWSTL GDFCINEGKF IGCSYYRNSV GIWVSDISEL
EPYGAVSEDK NECMVKRFSV LNDQSERMGS GPRGSVSPDY ETREIKNIYV DCGNLNVAQN
PGSLKATLPL ESGKVATMVS EKQNAAYFGP AGDKYSSTSR DSDSGEESSY SERESIPFSR
TKSGMLLRPA HVRKTLAKFE ESKQSAVVQS ATRKKSGLAV EEEPQTQNAF LSEQNASKPF
DAEDSIIKGI TNKFEKALSS EPPTDEANRM FLKPPRIHRS SNSKYNDTRR AMSADPATFG
KGGMENSGDV EDIPSKTERV LSREKPGDEQ KNTEYPSGSR ELNPVKIVEG VNVVSGRTRS
LVEKFERGEK TTHTEGASTT IEQNNNAVQE DPRKTSRQTG ETPVISTRRA RSTPARVMPI
VLNRDSNVTS DEPPLTQPAR TSSFPVMPVI LNQASNVTYD EPSVALTQES RTSHARILPV
TFNQATNITS EEASVTLRRQ RRNSAARVRP VLLSQATSHE CPVTSVRPLR TSPARVMPTK
LNQSVNMTSD TSHIASMHRV SPTQMLATPT VIDQVADMTL DETHATQIQP ACDNMPQKEE
PNISDREDDS DITENLMLTH NEFLSTLQSR LTKLQIVRHF WERSDVKGAI GALRKLTDQS
VQADVISILT EKIEILTLDM FSQLVPVLTS LLGSRTERPV NVSLDMLLKL VAVFGTVIRS
TVSAPRIVGV DLHANERLEI CQICSAGLHK IQRILPVLAR RGGLITRKAQ ELNLVLQEP
