CAN2_ARATH
ID CAN2_ARATH Reviewed; 332 AA.
AC F4IH31; Q8RWK9; Q9SIY4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Staphylococcal-like nuclease CAN2;
DE EC=3.1.31.-;
DE AltName: Full=Calcium-dependent nuclease 2;
DE Short=AtCAN2;
DE Short=Ca(2+)-dependent nuclease 2;
GN Name=CAN2; OrderedLocusNames=At2g40410; ORFNames=T3G21.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 2).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=23102437; DOI=10.1186/1471-2229-12-195;
RA Lesniewicz K., Poreba E., Smolarkiewicz M., Wolff N., Stanislawski S.,
RA Wojtaszek P.;
RT "Plant plasma membrane-bound staphylococcal-like DNases as a novel class of
RT eukaryotic nucleases.";
RL BMC Plant Biol. 12:195-195(2012).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22450164; DOI=10.1016/j.pep.2012.03.007;
RA Guo K., Liu S., Takano T., Zhang X.;
RT "Molecular cloning, expression, and characterization of a Ca2+-dependent
RT nuclease of Arabidopsis thaliana.";
RL Protein Expr. Purif. 83:70-74(2012).
RN [7]
RP FUNCTION, INTERACTION WITH CYS6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=24076026; DOI=10.1016/j.febslet.2013.09.019;
RA Guo K., Bu Y., Takano T., Liu S., Zhang X.;
RT "Arabidopsis cysteine proteinase inhibitor AtCYSb interacts with a Ca(2+)-
RT dependent nuclease, AtCaN2.";
RL FEBS Lett. 587:3417-3421(2013).
CC -!- FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at
CC the 5' position of the phosphodiester bond. Possesses activity toward
CC the single-stranded DNA, double-stranded DNA and RNA. May be involved
CC in genomic DNA degradation during programmed cell death.
CC {ECO:0000269|PubMed:22450164, ECO:0000269|PubMed:23102437,
CC ECO:0000269|PubMed:24076026}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+). {ECO:0000269|PubMed:22450164,
CC ECO:0000269|PubMed:23102437}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:22450164};
CC -!- SUBUNIT: Interacts with CYS6/CYSB; this interaction inhibits nuclease
CC activity of CAN2. {ECO:0000269|PubMed:24076026}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23102437,
CC ECO:0000305|PubMed:24076026}; Lipid-anchor
CC {ECO:0000305|PubMed:23102437, ECO:0000305|PubMed:24076026}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IH31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IH31-2; Sequence=VSP_055868, VSP_055869;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and siliques.
CC {ECO:0000269|PubMed:24076026}.
CC -!- INDUCTION: By hydrogen peroxide and cold stress.
CC {ECO:0000269|PubMed:24076026}.
CC -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC ProRule:PRU00272}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25675.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007020; AAD25675.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09825.1; -; Genomic_DNA.
DR EMBL; AY093027; AAM13026.1; -; mRNA.
DR EMBL; AY128927; AAM91327.1; -; mRNA.
DR EMBL; BX820591; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B84829; B84829.
DR RefSeq; NP_973649.1; NM_201920.3. [F4IH31-1]
DR AlphaFoldDB; F4IH31; -.
DR SMR; F4IH31; -.
DR BioGRID; 3972; 1.
DR STRING; 3702.AT2G40410.2; -.
DR PaxDb; F4IH31; -.
DR PRIDE; F4IH31; -.
DR ProteomicsDB; 222779; -. [F4IH31-1]
DR EnsemblPlants; AT2G40410.2; AT2G40410.2; AT2G40410. [F4IH31-1]
DR GeneID; 818634; -.
DR Gramene; AT2G40410.2; AT2G40410.2; AT2G40410. [F4IH31-1]
DR KEGG; ath:AT2G40410; -.
DR Araport; AT2G40410; -.
DR TAIR; locus:2063058; AT2G40410.
DR eggNOG; ENOG502QT2R; Eukaryota.
DR HOGENOM; CLU_046484_1_1_1; -.
DR InParanoid; F4IH31; -.
DR OMA; LLYGHCC; -.
DR PhylomeDB; F4IH31; -.
DR PRO; PR:F4IH31; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IH31; baseline and differential.
DR Genevisible; F4IH31; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006308; P:DNA catabolic process; IDA:TAIR.
DR GO; GO:0006401; P:RNA catabolic process; IDA:TAIR.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Endonuclease; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Nuclease; Palmitate;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..332
FT /note="Staphylococcal-like nuclease CAN2"
FT /id="PRO_0000430199"
FT DOMAIN 140..316
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 12
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 226
FT /note="G -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_055868"
FT VAR_SEQ 227..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_055869"
SQ SEQUENCE 332 AA; 37298 MW; 1678CC319101ACC0 CRC64;
MGNALTFLYG KCCKPTTTDD SLGPHGVSAA TVGVSALAHD LFNFEITSQV PEGLGRYVQS
SRKAQANWYR KILEAWKQAK PPPQTAEEAS RLVTDILKRN QKADVEGLLS FYGLPLSHTL
VEVTVEAPVS LPEGILFEFQ TLPVDPKAVA DGDTITVYVS TSEPVVSSSV PREVNLAAVQ
RAKAREKRNY PKADELHQKI IDSGYRVLNI ENEEVLARKF RIRLRGIDAP ESQMPFGKEA
QEGLLKIVGR KSLKVLVYGE DQYGRCVGDL YCNGIFVQEA MLKKGLAWHY LAYDKRPVLA
KWEKEARQKR IGLWASSNPE KPWDWRKNNR RE
