NCA1_ARATH
ID NCA1_ARATH Reviewed; 405 AA.
AC Q9M2V1; B9DI00;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Protein NCA1 {ECO:0000303|PubMed:24285797};
DE AltName: Full=NO CATALASE ACTIVITY 1 {ECO:0000303|PubMed:24285797};
GN Name=NCA1 {ECO:0000303|PubMed:24285797};
GN OrderedLocusNames=At3g54360 {ECO:0000312|Araport:AT3G54360};
GN ORFNames=T12E18.50 {ECO:0000312|EMBL:CAB81801.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-405.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24285797; DOI=10.1105/tpc.113.117192;
RA Hackenberg T., Juul T., Auzina A., Gwizdz S., Malolepszy A.,
RA Van Der Kelen K., Dam S., Bressendorff S., Lorentzen A., Roepstorff P.,
RA Lehmann Nielsen K., Joergensen J.E., Hofius D., Van Breusegem F.,
RA Petersen M., Andersen S.U.;
RT "Catalase and NO CATALASE ACTIVITY1 promote autophagy-dependent cell death
RT in Arabidopsis.";
RL Plant Cell 25:4616-4626(2013).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH CAT1; CAT2 AND CAT3, INDUCTION BY H(2)O(2) AND SALT,
RP DOMAIN, AND MUTAGENESIS OF CYS-111; HIS-126 AND CYS-129.
RX PubMed=25700484; DOI=10.1105/tpc.114.135095;
RA Li J., Liu J., Wang G., Cha J.Y., Li G., Chen S., Li Z., Guo J., Zhang C.,
RA Yang Y., Kim W.Y., Yun D.J., Schumaker K.S., Chen Z., Guo Y.;
RT "A chaperone function of NO CATALASE ACTIVITY1 is required to maintain
RT catalase activity and for multiple stress responses in Arabidopsis.";
RL Plant Cell 27:908-925(2015).
CC -!- FUNCTION: Has holdase chaperone activity that may fold catalase to a
CC functional structure (PubMed:25700484). Not required for the peroxisome
CC import of catalases (PubMed:25700484). Required for the activity of
CC catalases and acts mainly at the post-transcriptional level
CC (PubMed:24285797). {ECO:0000269|PubMed:24285797,
CC ECO:0000269|PubMed:25700484}.
CC -!- SUBUNIT: Interacts with the catalases CAT1, CAT2 and CAT3. This
CC interaction is not induced by alkaline stress or H(2)O(2) and NaCl
CC treatments. {ECO:0000269|PubMed:25700484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24285797,
CC ECO:0000269|PubMed:25700484}. Nucleus {ECO:0000269|PubMed:24285797}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:25700484}.
CC -!- INDUCTION: Up-regulated upon H(2)O(2) or salt treatments.
CC {ECO:0000269|PubMed:25700484}.
CC -!- DOMAIN: The RING-type zinc finger domain (1-158) is involved in the
CC increase of catalase activity and zinc ion binding is required for this
CC increase. {ECO:0000269|PubMed:25700484}.
CC -!- DOMAIN: The interaction with CAT2 is through the C-terminal TPR-
CC containing domain (159-405). {ECO:0000269|PubMed:25700484}.
CC -!- DISRUPTION PHENOTYPE: Hyponastic leaves and reduced growth
CC (PubMed:24285797). Severely reduced catalase activities
CC (PubMed:24285797). Hypersensitivity to multiple abiotic stresses
CC (PubMed:25700484). {ECO:0000269|PubMed:24285797,
CC ECO:0000269|PubMed:25700484}.
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DR EMBL; AL132971; CAB81801.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79220.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65013.1; -; Genomic_DNA.
DR EMBL; AF410273; AAK95259.1; -; mRNA.
DR EMBL; BT000620; AAN18187.1; -; mRNA.
DR EMBL; AY086065; AAM63273.1; -; mRNA.
DR EMBL; AK317708; BAH20367.1; -; mRNA.
DR PIR; T47595; T47595.
DR RefSeq; NP_001327012.1; NM_001339663.1.
DR RefSeq; NP_191004.1; NM_115296.3.
DR AlphaFoldDB; Q9M2V1; -.
DR SMR; Q9M2V1; -.
DR IntAct; Q9M2V1; 2.
DR STRING; 3702.AT3G54360.1; -.
DR iPTMnet; Q9M2V1; -.
DR PaxDb; Q9M2V1; -.
DR PRIDE; Q9M2V1; -.
DR ProteomicsDB; 251096; -.
DR EnsemblPlants; AT3G54360.1; AT3G54360.1; AT3G54360.
DR EnsemblPlants; AT3G54360.2; AT3G54360.2; AT3G54360.
DR GeneID; 824603; -.
DR Gramene; AT3G54360.1; AT3G54360.1; AT3G54360.
DR Gramene; AT3G54360.2; AT3G54360.2; AT3G54360.
DR KEGG; ath:AT3G54360; -.
DR Araport; AT3G54360; -.
DR TAIR; locus:2096179; AT3G54360.
DR eggNOG; ENOG502QW0D; Eukaryota.
DR HOGENOM; CLU_050147_0_0_1; -.
DR InParanoid; Q9M2V1; -.
DR OMA; VPPKCPF; -.
DR OrthoDB; 679837at2759; -.
DR PhylomeDB; Q9M2V1; -.
DR PRO; PR:Q9M2V1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2V1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:1902553; P:positive regulation of catalase activity; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW TPR repeat; Zinc; Zinc-finger.
FT CHAIN 1..405
FT /note="Protein NCA1"
FT /id="PRO_0000440614"
FT REPEAT 247..280
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 292..325
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT ZN_FING 108..142
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 111
FT /note="C->S: No effect on the interaction with CAT2, but no
FT increase of catalase activity."
FT /evidence="ECO:0000269|PubMed:25700484"
FT MUTAGEN 126
FT /note="H->Y: No effect on the interaction with CAT2, but no
FT increase of catalase activity."
FT /evidence="ECO:0000269|PubMed:25700484"
FT MUTAGEN 129
FT /note="C->A: No effect on the interaction with CAT2, but no
FT increase of catalase activity."
FT /evidence="ECO:0000269|PubMed:25700484"
SQ SEQUENCE 405 AA; 44530 MW; 7922FAEB50266E83 CRC64;
MTTTSVCPFS KAARPDDGST RKQGEITASG CPFSKAARPD DASARKQGET TASGCPFSKS
ARPDENGSKG CPEQEGNLNK DSTDSATVPA KCPFGYDSQT FKLGPFSCML CQALLYESSR
CVPCTHVFCK VCLTRFKDCP LCGADIESIE VDENLQKMVD QFIEGHARIK RSVVNGTEKE
EVENDNKKVI YADVSMERGS FLVQQAMRAF SAQNYESAKS RLAMCTEDIR DQLGREGNTP
ELCSQLGAVL GMLGDCSRAM GDSSSAVKHF EESVEFLMKL PLNDLEITHT LSVSLNKIGD
LKYYDEDLQA ARSYYDRALN VRRDAMKHHP NAPSQILDVA VSLAKVADID RTLQNEVAAT
DGFKEGMRLL ESLKLDSEDS ALEQRRLSVL EFLKKQVETD AETAL
