CAN1_ARATH
ID CAN1_ARATH Reviewed; 323 AA.
AC F4IZC5; Q9LWC0; Q9LYM4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Staphylococcal-like nuclease CAN1;
DE EC=3.1.31.-;
DE AltName: Full=Calcium-dependent nuclease 1;
DE Short=AtCAN1;
DE Short=Ca(2+)-dependent nuclease 1;
GN Name=CAN1; Synonyms=CAN; OrderedLocusNames=At3g56170; ORFNames=F18O21.130;
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 [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10760589; DOI=10.1016/s0167-4781(00)00007-5;
RA Isono K., Satoh K., Kobayashi H.;
RT "Molecular cloning of a cDNA encoding a novel Ca(2+)-dependent nuclease of
RT Arabidopsis that is similar to staphylococcal nuclease.";
RL Biochim. Biophys. Acta 1491:267-272(2000).
RN [2]
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 [3]
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 [4]
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).
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:10760589, ECO:0000269|PubMed:23102437}.
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:10760589,
CC ECO:0000269|PubMed:23102437}.
CC -!- INTERACTION:
CC F4IZC5; Q8H0X6: CYS6; NbExp=3; IntAct=EBI-8760221, EBI-8760191;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23102437};
CC Lipid-anchor {ECO:0000305|PubMed:23102437}.
CC -!- SIMILARITY: Belongs to the thermonuclease family. {ECO:0000255|PROSITE-
CC ProRule:PRU00272}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D84226; BAA95210.1; -; mRNA.
DR EMBL; AL163763; CAB87416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79489.1; -; Genomic_DNA.
DR PIR; T47734; T47734.
DR PIR; T52640; T52640.
DR RefSeq; NP_567036.1; NM_115475.5.
DR AlphaFoldDB; F4IZC5; -.
DR SMR; F4IZC5; -.
DR IntAct; F4IZC5; 1.
DR MINT; F4IZC5; -.
DR STRING; 3702.AT3G56170.1; -.
DR PaxDb; F4IZC5; -.
DR PRIDE; F4IZC5; -.
DR ProteomicsDB; 239189; -.
DR EnsemblPlants; AT3G56170.1; AT3G56170.1; AT3G56170.
DR GeneID; 824783; -.
DR Gramene; AT3G56170.1; AT3G56170.1; AT3G56170.
DR KEGG; ath:AT3G56170; -.
DR Araport; AT3G56170; -.
DR TAIR; locus:2078486; AT3G56170.
DR eggNOG; ENOG502QT2R; Eukaryota.
DR HOGENOM; CLU_046484_1_1_1; -.
DR InParanoid; F4IZC5; -.
DR OMA; WENEARQ; -.
DR OrthoDB; 936977at2759; -.
DR PRO; PR:F4IZC5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IZC5; baseline and differential.
DR Genevisible; F4IZC5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IDA:TAIR.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Endonuclease; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nuclease; Palmitate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..323
FT /note="Staphylococcal-like nuclease CAN1"
FT /id="PRO_0000430198"
FT DOMAIN 130..306
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 213
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 218
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 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 318
FT /note="N -> Y (in Ref. 1; BAA95210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36134 MW; 642ED584E3D050B4 CRC64;
MGNAIRLLRK CLNSHGVSAS SGGVSALSRD LLNFETTSQV PEKLGSYVVS SQKAQANWYR
KILEAWKQAK PRPKTPEEAS RLVIAALKNH QKADVEGLLS FYGLPSPHNL VEVPTEAPVS
LPKGVRFELN TLPVDTKSVA DGDTVTVYVS SKDPLVSSSL PKDVSLAAVK RAKAREKKNY
TEADALHKTI IASGYRMISF QNEEVLAKKF RIRLSGIDSP ESKMPYGKEA HDELLKMVEG
KCLKVLVYTE DRYGRCVGDI YCNGKFVQEV MLKKGLAWHY VAYDKRAELA KWENEARQKR
VGLWASSNPE KPWEWRKNKR GGN
