(data stored in ACNUC9543 zone)

SWISSPROT: ESP3_ARATH

ID   ESP3_ARATH              Reviewed;        1044 AA.
AC   Q8VY00; Q9LQK8;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 135.
DE   RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH1 {ECO:0000305};
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH RNA helicase homolog PRP2 {ECO:0000303|PubMed:17008405};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2733 {ECO:0000303|PubMed:15266054};
DE   AltName: Full=Protein ENHANCED SILENCING PHENOTYPE 3 {ECO:0000303|PubMed:17008405};
GN   Name=ESP3 {ECO:0000303|PubMed:17008405};
GN   Synonyms=EMB2733 {ECO:0000303|PubMed:15266054};
GN   OrderedLocusNames=At1g32490 {ECO:0000312|Araport:AT1G32490};
GN   ORFNames=F5D14.27 {ECO:0000312|EMBL:AAF81347.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15266054; DOI=10.1104/pp.104.045179;
RA   Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R.,
RA   Hutchens S., Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT   "Identification of genes required for embryo development in
RT   Arabidopsis.";
RL   Plant Physiol. 135:1206-1220(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16807317; DOI=10.1093/nar/gkl429;
RA   de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,
RA   Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
RT   "Phosphoproteomics reveals extensive in vivo phosphorylation of
RT   Arabidopsis proteins involved in RNA metabolism.";
RL   Nucleic Acids Res. 34:3267-3278(2006).
RN   [6]
RP   DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=17008405; DOI=10.1073/pnas.0606536103;
RA   Herr A.J., Molnar A., Jones A., Baulcombe D.C.;
RT   "Defective RNA processing enhances RNA silencing and influences
RT   flowering of Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14994-15001(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: Involved in pre-mRNA splicing.
CC       {ECO:0000269|PubMed:17008405}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=Q8VY00-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:17008405}.
CC   -!- DISRUPTION PHENOTYPE: Embryo defective (PubMed:15266054). Reduced
CC       stature, early flowering and altered leaf morphology
CC       (PubMed:17008405). {ECO:0000269|PubMed:15266054,
CC       ECO:0000269|PubMed:17008405}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. PRP2 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF81347.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC       URL="http://seedgenes.org/MutantList";
CC   -!- WEB RESOURCE: Name=Splicing Related Gene Database;
CC       URL="http://www.plantgdb.org/SRGD/index.php";
DR   EMBL; AC007767; AAF81347.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31492.1; -; Genomic_DNA.
DR   EMBL; AY074318; AAL67014.1; -; mRNA.
DR   EMBL; AY133872; AAM91806.1; -; mRNA.
DR   PIR; C86450; C86450.
DR   RefSeq; NP_174527.2; NM_102984.5. [Q8VY00-1]
DR   SMR; Q8VY00; -.
DR   IntAct; Q8VY00; 1.
DR   STRING; 3702.AT1G32490.1; -.
DR   iPTMnet; Q8VY00; -.
DR   PaxDb; Q8VY00; -.
DR   PRIDE; Q8VY00; -.
DR   EnsemblPlants; AT1G32490.1; AT1G32490.1; AT1G32490. [Q8VY00-1]
DR   GeneID; 840143; -.
DR   Gramene; AT1G32490.1; AT1G32490.1; AT1G32490. [Q8VY00-1]
DR   KEGG; ath:AT1G32490; -.
DR   Araport; AT1G32490; -.
DR   TAIR; locus:2033723; AT1G32490.
DR   eggNOG; KOG0923; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   HOGENOM; HOG000175261; -.
DR   InParanoid; Q8VY00; -.
DR   KO; K12813; -.
DR   OrthoDB; 354219at2759; -.
DR   PhylomeDB; Q8VY00; -.
DR   PRO; PR:Q8VY00; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8VY00; baseline and differential.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034459; F:ATP-dependent 3'-5' RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0035194; P:posttranscriptional gene silencing by RNA; IMP:TAIR.
DR   GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8VY00.
DR   SWISS-2DPAGE; Q8VY00.
KW   Alternative splicing; ATP-binding; Complete proteome; Helicase;
KW   Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Spliceosome.
FT   CHAIN         1   1044       Pre-mRNA-splicing factor ATP-dependent
FT                                RNA helicase DEAH1.
FT                                /FTId=PRO_0000434940.
FT   DOMAIN      414    577       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      600    775       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     427    434       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       524    527       DEAH box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOD_RES     135    135       Phosphoserine.
FT                                {ECO:0000244|PubMed:16807317}.
FT   MOD_RES     138    138       Phosphoserine.
FT                                {ECO:0000244|PubMed:16807317}.
SQ   SEQUENCE   1044 AA;  118832 MW;  187B02E796AF0E18 CRC64;
     MASNDLKTWV SDKLMMLLGY SQAAVVNYLI AMAKKTKSPT ELVGELVDYG FSSSGDTRSF
     AEEIFARVPR KTAGVNLYQK HEAEAAMLVR KQKTYALLDA DDDEDEVVVE KKSSVSESRK
     SDKGKKRFRK KSGQSDESDG EVAVREDSRH VRRKVSEEDD GSESEEERVR DQKEREELEQ
     HLKDRDTART RKLTEQTLSK KEKEEAVRRA NALEKDDLYS LRKVSRQEYL KKREQKKLDE
     LRDEIEDEQY LFGGEKLTET ELREFRYKKE LYDLVKKRTQ DEDNVEEYRI PDAYDQEGGV
     DQEKRFSVAV QRYRDLDSTE KMNPFAEQEA WEDHQIGKAT LKFGAKNKQA SDDYQFVFED
     QINFIKESVM AGENYEDAMD AKQKSQDLAE KTALEELQEV RRSLPIYTYR DQLLKAVEEH
     QVLVIVGDTG SGKTTQIPQY LHEAGYTKRG KVGCTQPRRV AAMSVAARVA QEMGVKLGHE
     VGYSIRFEDC TSDKTVLKYM TDGMLLRELL GEPDLASYSV VIVDEAHERT LSTDILFGLV
     KDIARFRPDL KLLISSATMD AEKFSDYFDT APIFSFPGRR YPVEINYTSA PEADYMDAAI
     VTILTIHVRE PLGDILVFFT GQEEIETAEE ILKHRIRGLG TKIRELIICP IYANLPSELQ
     AKIFEPTPEG ARKVVLATNI AETSLTIDGI KYVVDPGFSK MKSYNPRTGM ESLLITPISK
     ASATQRAGRA GRTSPGKCYR LYTAFNYNND LEENTVPEVQ RTNLASVVLA LKSLGIHDLI
     NFDFMDPPPA EALVKSLELL FALGALNKLG ELTKAGRRMA EFPLDPMLSK MIVVSDKYKC
     SDEIISIAAM LSIGGSIFYR PKDKQVHADN ARMNFHTGNV GDHIALLKVY SSWKETNFST
     QWCYENYIQV RSMKRARDIR DQLEGLLERV EIDISSNLNE LDSVRKSIVA GFFPHTAKLQ
     KNGSYRTVKH PQTVHIHPNS GLSQVLPRWV VYHELVLTSK EYMRQVTELK PEWLIELAPH
     YYQLKDVEDA ASKKMPKGAG KAAM
//

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