ID F4JZ19_ARATH Unreviewed; 246 AA.
AC F4JZ19;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Wound-responsive family protein {ECO:0000313|EMBL:AED98147.1};
GN OrderedLocusNames=At5g66050 {ECO:0000313|Araport:AT5G66050,
GN ECO:0000313|EMBL:AED98147.1};
GN ORFNames=K2A18.12 {ECO:0000313|EMBL:AED98147.1}, K2A18_12
GN {ECO:0000313|EMBL:AED98147.1};
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 {ECO:0000313|EMBL:AED98147.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AED98147.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC -!- FUNCTION: Bifunctional nuclease with both RNase and DNase activities.
CC Involved in basal defense response. Participates in abscisic acid-
CC derived callose deposition following infection by a necrotrophic
CC pathogen. {ECO:0000256|ARBA:ARBA00025428}.
CC -!- SIMILARITY: Belongs to the bifunctional nuclease family.
CC {ECO:0000256|ARBA:ARBA00009095}.
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DR EMBL; CP002688; AED98147.1; -; Genomic_DNA.
DR RefSeq; NP_974999.1; NM_203270.1.
DR AlphaFoldDB; F4JZ19; -.
DR SMR; F4JZ19; -.
DR ProteomicsDB; 211796; -.
DR EnsemblPlants; AT5G66050.2; AT5G66050.2; AT5G66050.
DR GeneID; 836735; -.
DR Gramene; AT5G66050.2; AT5G66050.2; AT5G66050.
DR Araport; AT5G66050; -.
DR TAIR; AT5G66050; -.
DR HOGENOM; CLU_050306_2_0_1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZ19; baseline and differential.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.690.10; Bifunctional nuclease domain; 1.
DR InterPro; IPR036104; BFN_sf.
DR InterPro; IPR003729; Bi_nuclease_dom.
DR PANTHER; PTHR15160:SF1; VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR; 1.
DR PANTHER; PTHR15160; VON HIPPEL-LINDAU PROTEIN; 1.
DR Pfam; PF02577; BFN_dom; 1.
DR SUPFAM; SSF103256; Hypothetical protein TM0160; 1.
DR PROSITE; PS51658; BFN; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4JZ19};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 31..168
FT /note="BFN"
FT /evidence="ECO:0000259|PROSITE:PS51658"
SQ SEQUENCE 246 AA; 27480 MW; 1D327131370A845C CRC64;
MHYKMRRHGF RQDSMWQTSR PLPPFSIRAS ESRVGVLPIG LGFLRQFKQP TIFLKISCDG
DYLLPVIVGD AAVEKLLDVP LQGHTEECPD QFQFVSAVVD KLGYEVKMVK LTGRIVNTYY
ASLCLGKPGD IEAICIDSRP SDAINVARAC QAPIYVNKAI VLEEAIKIGY GGRPQSAKPV
FNVILDSAPD GPDPLSEELK LVRNMDLASK EERYIDAAMW RDRLKNLQNS SSVVYNKGVE
TPESYE
//
