KTN82_ARATH
ID KTN82_ARATH Reviewed; 1181 AA.
AC F4HTH8; A0A1P8AV57; F4HTH9; O22725;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.2 {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000303|PubMed:28978669};
DE AltName: Full=DDB1 binding WD40 hypersensitive to ABA 3 {ECO:0000303|PubMed:21421380};
DE Short=DWD hypersensitive to ABA 3 {ECO:0000303|PubMed:21421380};
GN Name=KTN80.2 {ECO:0000303|PubMed:28978669};
GN Synonyms=DWA3 {ECO:0000303|PubMed:21421380};
GN OrderedLocusNames=At1g61210 {ECO:0000312|Araport:AT1G61210};
GN ORFNames=F11P17.7 {ECO:0000312|EMBL:AAB71474.1};
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, AND INTERACTION WITH DDB1A AND DDB1B.
RC STRAIN=cv. Columbia;
RX PubMed=21421380; DOI=10.1016/j.plantsci.2010.10.008;
RA Lee J.-H., Terzaghi W., Deng X.W.;
RT "DWA3, an Arabidopsis DWD protein, acts as a negative regulator in ABA
RT signal transduction.";
RL Plant Sci. 180:352-357(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP SUBUNIT, INTERACTION WITH AAA1/KTN1, GENE 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: 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). Negative
CC regulator of abscisic acid (ABA) responses (PubMed:21421380). May
CC function as a substrate receptor for cullin-RING ubiquitin ligase 4
CC complexes (CRL4), a family of E3 ligases involved in protein
CC degradation (PubMed:21421380). {ECO:0000255|HAMAP-Rule:MF_03022,
CC ECO:0000269|PubMed:21421380, 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 (PubMed:28978669). Interacts with subunits of the CUL4-based
CC E3 ligase complex DDB1A and DDB1B (PubMed:21421380).
CC {ECO:0000269|PubMed:21421380, ECO:0000269|PubMed:28978669}.
CC -!- INTERACTION:
CC F4HTH8; Q9SEX2: AAA1; NbExp=3; IntAct=EBI-2025609, EBI-2025583;
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=3;
CC Name=1;
CC IsoId=F4HTH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HTH8-2; Sequence=VSP_060684;
CC Name=3;
CC IsoId=F4HTH8-3; Sequence=VSP_060684, VSP_060685;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in siliques, flowers,
CC leaves, stems and roots. {ECO:0000269|PubMed:28978669}.
CC -!- DISRUPTION PHENOTYPE: Hyper-induction of abscisic acid (ABA)-inducible
CC transcription factors (e.g. ABI5 and MYC2) and their downstream genes
CC in response to ABA (PubMed:21421380). Increased sensitivity to ABA and
CC salt stress leading to reduced root length and increased dehydration
CC tolerance (PubMed:21421380). The double mutant ktn80.1 ktn80.2 exhibits
CC normal growth, but the quadruple mutant ktn80.1 ktn80.2 ktn80.3 ktn80.4
CC has a severe dwarf phenotype, with small and round dark-green rosette
CC leaves as well as wide and short petioles, probably due to cell
CC elongation defects, and associated with a complex cortical microtubule
CC (MT) network with stable entanglements (PubMed:28978669). Plants
CC missing 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:21421380,
CC 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=AAB71474.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002294; AAB71474.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33803.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33804.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60526.1; -; Genomic_DNA.
DR PIR; A96638; A96638.
DR RefSeq; NP_001185277.1; NM_001198348.2. [F4HTH8-2]
DR RefSeq; NP_001322807.1; NM_001333941.1. [F4HTH8-3]
DR RefSeq; NP_176316.4; NM_104802.5. [F4HTH8-1]
DR AlphaFoldDB; F4HTH8; -.
DR SMR; F4HTH8; -.
DR IntAct; F4HTH8; 1.
DR STRING; 3702.AT1G61210.1; -.
DR PaxDb; F4HTH8; -.
DR PRIDE; F4HTH8; -.
DR ProteomicsDB; 205565; -.
DR ProteomicsDB; 209683; -. [F4HTH8-1]
DR ProteomicsDB; 218395; -.
DR EnsemblPlants; AT1G61210.1; AT1G61210.1; AT1G61210. [F4HTH8-1]
DR EnsemblPlants; AT1G61210.2; AT1G61210.2; AT1G61210. [F4HTH8-2]
DR EnsemblPlants; AT1G61210.3; AT1G61210.3; AT1G61210. [F4HTH8-3]
DR GeneID; 842414; -.
DR Gramene; AT1G61210.1; AT1G61210.1; AT1G61210. [F4HTH8-1]
DR Gramene; AT1G61210.2; AT1G61210.2; AT1G61210. [F4HTH8-2]
DR Gramene; AT1G61210.3; AT1G61210.3; AT1G61210. [F4HTH8-3]
DR KEGG; ath:AT1G61210; -.
DR Araport; AT1G61210; -.
DR TAIR; locus:2008495; AT1G61210.
DR eggNOG; KOG0267; Eukaryota.
DR HOGENOM; CLU_007811_1_0_1; -.
DR InParanoid; F4HTH8; -.
DR OMA; CHDTVDM; -.
DR OrthoDB; 425951at2759; -.
DR PRO; PR:F4HTH8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HTH8; 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 GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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; 6.
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; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1181
FT /note="Katanin p80 WD40 repeat-containing subunit B1
FT homolog KTN80.2"
FT /id="PRO_0000450714"
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 361..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1008
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 361..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 353..355
FT /note="STG -> C (in isoform 2 and isoform 3)"
FT /id="VSP_060684"
FT VAR_SEQ 720..821
FT /note="Missing (in isoform 3)"
FT /id="VSP_060685"
SQ SEQUENCE 1181 AA; 129175 MW; 8117C4EA23D10605 CRC64;
MAKRGYKLQE FLAHSANVNC LSIGKKTSRL FITGGDDYKV NLWAIGKPTS LMSLCGHTSA
VDSVAFDSAE VLVLAGASSG VIKLWDVEEA KMVRAFTGHR SNCSAVEFHP FGEFLASGSS
DANLKIWDIR KKGCIQTYKG HSRGISTIRF TPDGRWVVSG GLDNVVKVWD LTAGKLLHEF
KFHEGPIRSL DFHPLEFLLA TGSADRTVKF WDLETFELIG STRPEATGVR SIKFHPDGRT
LFCGLDDSLK VYSWEPVVCH DGVDMGWSTL GDLCISEGKL LGCSYYQNSV GIWVSDISQI
EPYGIGSADK KECVEKILSA LDDQSFDRIK STPRRSSSPD YETKEIKNIY IDSTGGNSAV
AHKSGSLSTP ATSTGQAGDN KSLVVHSVVP RDSDIGKDSS DSGKESITFS KTKPGMLLRP
AYVRKTPTKF DETKKQSVAV GYLKKSGLDG EKKLDTETAF DSEMSGRNPY DADDSIIKSI
TNKFEQALLP ESPTDEAKCM LLKPPRVQRS PSTKYNEARW ATSTDSGALD SKKNGLESSR
DMDLPTGLRD DRGSNPCEED IENKSISSRS ERVLSPEKAG DELKSLESPG GSKESKSVKV
VRGVKVVSGR TRSLVERFER GEKITHSEDK AASATVVHSS NSVEEEPLTA SVQTVSMMPT
QVMPVKLDQA TNSTTVDVPV LSTRRTKSTP VRVMPVVLGR DTSMATDTPP VTSTRPDRTS
ATNLTSDVSG VTSKRQTRTS PAPVMPMILN QTTKMKSDEP SITSTWPDRT SATDLTSDVS
GVISSRQTRT SPAPVMPMKL NQKTKIKSDE PPITSTRPDR PSATNLTSDE SPVTSTRQAK
TSPAPVTPVI LNQRQTTNMK SDEPPVISTR PLRTSSARVM PVILNQASTT YDERPLSSSR
SARTSPARIM PMKLNQADNM PSYEPPVALT RSARNSPARV IPVKLNQATN VTADASHIRS
RQRFSPTQTL ATPAVFDQVT DMTLDETTKT QQSSDILTQK EEPQISGRED DGDIWEILMR
THSEVLNTLQ SRLTKLQIVR HFWERSDIKG AIAALRKLSD HSVQADVINI LTDKTEILTL
DLFSQLAPVL TGLLGSKTER PVNVSLEMLL KLVAVFGTVI QSTVSARRVV GVDLHAEERL
QICQSCSAEL QKVQKILPLL TRRGGLIARK AQELNLVLQT P
