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 03-AUG-2022, entry version 149.
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; 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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference
RT 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., 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 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., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in 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 Arabidopsis
RT 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 flowering
RT 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 family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
CC -!- FUNCTION: Involved in pre-mRNA splicing. {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. {ECO:0000269|PubMed:17008405}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective (PubMed:15266054). Reduced
CC stature, early flowering and altered leaf morphology (PubMed:17008405).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:17008405}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC 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";
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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 AlphaFoldDB; Q8VY00; -.
DR SMR; Q8VY00; -.
DR IntAct; Q8VY00; 1.
DR STRING; 3702.AT1G32490.1; -.
DR iPTMnet; Q8VY00; -.
DR PaxDb; Q8VY00; -.
DR PRIDE; Q8VY00; -.
DR ProteomicsDB; 220588; -. [Q8VY00-1]
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 InParanoid; Q8VY00; -.
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:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Spliceosome.
FT CHAIN 1..1044
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT DEAH1"
FT /id="PRO_0000434940"
FT DOMAIN 414..577
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 600..775
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 106..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 524..527
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 107..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807317"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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
