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NEN4_ARATH
ID   NEN4_ARATH              Reviewed;         255 AA.
AC   F4JJ23; O65668;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein NEN4 {ECO:0000303|PubMed:25081480};
DE   AltName: Full=NAC45/NAC86-dependent exonuclease-domain protein 4 {ECO:0000303|PubMed:25081480};
DE            EC=3.1.11.-;
GN   Name=NEN4 {ECO:0000303|PubMed:25081480};
GN   OrderedLocusNames=At4g39810 {ECO:0000312|Araport:AT4G39810};
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:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY NAC045 AND
RP   NAC086, AND DISRUPTION PHENOTYPE.
RX   PubMed=25081480; DOI=10.1126/science.1253736;
RA   Furuta K.M., Yadav S.R., Lehesranta S., Belevich I., Miyashima S.,
RA   Heo J.O., Vaten A., Lindgren O., De Rybel B., Van Isterdael G.,
RA   Somervuo P., Lichtenberger R., Rocha R., Thitamadee S., Taehtiharju S.,
RA   Auvinen P., Beeckman T., Jokitalo E., Helariutta Y.;
RT   "Plant development. Arabidopsis NAC45/86 direct sieve element morphogenesis
RT   culminating in enucleation.";
RL   Science 345:933-937(2014).
CC   -!- FUNCTION: Probable exonuclease required for enuclation of sieve
CC       elements. {ECO:0000269|PubMed:25081480}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q682U6};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25081480}.
CC       Note=Accumulates in the nuclei prior to enuclation.
CC       {ECO:0000269|PubMed:25081480}.
CC   -!- TISSUE SPECIFICITY: Expressed in the sieve elements and phloem pole
CC       pericycle cells. {ECO:0000269|PubMed:25081480}.
CC   -!- INDUCTION: Regulated by the transcription factors NAC045 and NAC086.
CC       {ECO:0000269|PubMed:25081480}.
CC   -!- DISRUPTION PHENOTYPE: Shorter root phenotype and impaired phloem
CC       function. {ECO:0000269|PubMed:25081480}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18767.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80644.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL022605; CAA18767.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161595; CAB80644.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE87122.1; -; Genomic_DNA.
DR   PIR; T05018; T05018.
DR   RefSeq; NP_195691.4; NM_120144.5.
DR   AlphaFoldDB; F4JJ23; -.
DR   SMR; F4JJ23; -.
DR   STRING; 3702.AT4G39810.1; -.
DR   PaxDb; F4JJ23; -.
DR   PRIDE; F4JJ23; -.
DR   EnsemblPlants; AT4G39810.1; AT4G39810.1; AT4G39810.
DR   GeneID; 830140; -.
DR   Gramene; AT4G39810.1; AT4G39810.1; AT4G39810.
DR   KEGG; ath:AT4G39810; -.
DR   Araport; AT4G39810; -.
DR   TAIR; locus:2135302; AT4G39810.
DR   eggNOG; ENOG502QPJ4; Eukaryota.
DR   HOGENOM; CLU_079769_0_0_1; -.
DR   InParanoid; F4JJ23; -.
DR   OMA; TEIVFFD; -.
DR   OrthoDB; 1365966at2759; -.
DR   PRO; PR:F4JJ23; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JJ23; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   2: Evidence at transcript level;
KW   Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..255
FT                   /note="Protein NEN4"
FT                   /id="PRO_0000430891"
FT   DOMAIN          11..174
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        161
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XB0"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XB0"
SQ   SEQUENCE   255 AA;  28508 MW;  FB53F72BB4C16905 CRC64;
     MAVQTFPNEI VFFDLETNVP NKAGQHFHIL EFGAIIVCPK KLEELESFTT LIQPKDLSVV
     SIRSSRSDGI TRAKVTNAPS FEDVAEKIHG LLNGRIWAGH NIRRFDCVRI KEAFAEIGKA
     APEPSGIIDS LGLLSDKFGK RAGNMKMASL AAYFGLGVQK HRSLDDVRMN LEVLKHCATV
     LFLESTLPNH LEGKWHTSSK IMTRSRRNYQ IAQRAMPYSK GSLEKMTQNV KNLLSKAQGN
     QTLQSLINHS HSLLR
 
 
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