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RH42_ARATH
ID   RH42_ARATH              Reviewed;        1166 AA.
AC   Q8H0U8; A8MQH2; Q9SYP6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 42;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD-box RNA helicase RCF1;
DE   AltName: Full=REGULATOR OF CBF GENE EXPRESSION 1;
GN   Name=RH42; Synonyms=RCF1; OrderedLocusNames=At1g20920; ORFNames=F9H16.10;
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] OF 605-1166.
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17168887; DOI=10.1111/j.1467-7652.2004.00084.x;
RA   Mingam A., Toffano-Nioche C., Brunaud V., Boudet N., Kreis M., Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a family
RT   of genes.";
RL   Plant Biotechnol. J. 2:401-415(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-324, AND
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   [6]
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).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF GLU-687 AND GLY-808, SUBCELLULAR LOCATION, AND
RP   INDUCTION BY COLD.
RX   PubMed=23371945; DOI=10.1105/tpc.112.108340;
RA   Guan Q., Wu J., Zhang Y., Jiang C., Liu R., Chai C., Zhu J.;
RT   "A DEAD box RNA helicase is critical for pre-mRNA splicing, cold-responsive
RT   gene regulation, and cold tolerance in Arabidopsis.";
RL   Plant Cell 25:342-356(2013).
CC   -!- FUNCTION: Helicase required for pre-mRNA splicing, cold-responsive gene
CC       regulation and cold tolerance. {ECO:0000269|PubMed:23371945}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23371945}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8H0U8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8H0U8-2; Sequence=VSP_053521;
CC   -!- INDUCTION: Up-regulated by cold. {ECO:0000269|PubMed:23371945}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN72041.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC007369; AAD30599.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30040.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30041.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59668.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59669.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59670.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59671.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59672.1; -; Genomic_DNA.
DR   EMBL; BT002030; AAN72041.1; ALT_INIT; mRNA.
DR   PIR; H86341; H86341.
DR   RefSeq; NP_001077571.1; NM_001084102.1. [Q8H0U8-2]
DR   RefSeq; NP_001322011.1; NM_001332479.1. [Q8H0U8-1]
DR   RefSeq; NP_001322012.1; NM_001332478.1. [Q8H0U8-1]
DR   RefSeq; NP_001322013.1; NM_001332481.1. [Q8H0U8-1]
DR   RefSeq; NP_001322014.1; NM_001332480.1. [Q8H0U8-1]
DR   RefSeq; NP_001322015.1; NM_001332477.1. [Q8H0U8-1]
DR   RefSeq; NP_173516.1; NM_101945.4. [Q8H0U8-1]
DR   AlphaFoldDB; Q8H0U8; -.
DR   SMR; Q8H0U8; -.
DR   BioGRID; 23924; 2.
DR   STRING; 3702.AT1G20920.1; -.
DR   iPTMnet; Q8H0U8; -.
DR   PaxDb; Q8H0U8; -.
DR   PRIDE; Q8H0U8; -.
DR   ProteomicsDB; 236246; -. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.1; AT1G20920.1; AT1G20920. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.2; AT1G20920.2; AT1G20920. [Q8H0U8-2]
DR   EnsemblPlants; AT1G20920.3; AT1G20920.3; AT1G20920. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.4; AT1G20920.4; AT1G20920. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.5; AT1G20920.5; AT1G20920. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.6; AT1G20920.6; AT1G20920. [Q8H0U8-1]
DR   EnsemblPlants; AT1G20920.7; AT1G20920.7; AT1G20920. [Q8H0U8-1]
DR   GeneID; 838685; -.
DR   Gramene; AT1G20920.1; AT1G20920.1; AT1G20920. [Q8H0U8-1]
DR   Gramene; AT1G20920.2; AT1G20920.2; AT1G20920. [Q8H0U8-2]
DR   Gramene; AT1G20920.3; AT1G20920.3; AT1G20920. [Q8H0U8-1]
DR   Gramene; AT1G20920.4; AT1G20920.4; AT1G20920. [Q8H0U8-1]
DR   Gramene; AT1G20920.5; AT1G20920.5; AT1G20920. [Q8H0U8-1]
DR   Gramene; AT1G20920.6; AT1G20920.6; AT1G20920. [Q8H0U8-1]
DR   Gramene; AT1G20920.7; AT1G20920.7; AT1G20920. [Q8H0U8-1]
DR   KEGG; ath:AT1G20920; -.
DR   Araport; AT1G20920; -.
DR   TAIR; locus:2037416; AT1G20920.
DR   eggNOG; KOG0334; Eukaryota.
DR   InParanoid; Q8H0U8; -.
DR   OMA; CGLGVQT; -.
DR   OrthoDB; 245118at2759; -.
DR   PhylomeDB; Q8H0U8; -.
DR   PRO; PR:Q8H0U8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8H0U8; baseline and differential.
DR   Genevisible; Q8H0U8; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..1166
FT                   /note="DEAD-box ATP-dependent RNA helicase 42"
FT                   /id="PRO_0000239182"
FT   DOMAIN          560..738
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          749..910
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          14..95
FT                   /evidence="ECO:0000255"
FT   COILED          130..302
FT                   /evidence="ECO:0000255"
FT   MOTIF           529..557
FT                   /note="Q motif"
FT   MOTIF           686..689
FT                   /note="DEAD box"
FT   COMPBIAS        1..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..346
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         573..580
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   VAR_SEQ         1..338
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053521"
FT   MUTAGEN         687
FT                   /note="E->A: Loss of ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:23371945"
FT   MUTAGEN         808
FT                   /note="G->R: In rcf1-1; loss of function and reduced cold
FT                   tolerance."
FT                   /evidence="ECO:0000269|PubMed:23371945"
FT   CONFLICT        894
FT                   /note="A -> D (in Ref. 3; AAN72041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1166 AA;  133033 MW;  597BD171F02666B5 CRC64;
     MEVEKSKYRS EDLDVVEEEA DLKKSRRDRD RSNERKKDKG SEKRREKDRR KKRVKSSDSE
     DDYDRDDDEE REKRKEKERE RRRRDKDRVK RRSERRKSSD SEDDVEEEDE RDKRRVNEKE
     RGHREHERDR GKDRKRDRER EERKDKERER EKDRERRERE REEREKERVK ERERREREDG
     ERDRREREKE RGSRRNRERE RSREVGNEES DDDVKRDLKR RRKEGGERKE KEREKSVGRS
     SRHEDSPKRK SVEDNGEKKE KKTREEELED EQKKLDEEVE KRRRRVQEWQ ELKRKKEEAE
     SESKGDADGN EPKAGKAWTL EGESDDEEGH PEEKSETEMD VDEETKPEND GDAKMVDLEN
     ETAATVSESG GDGAVDEEEI DPLDAFMNTM VLPEVEKFCN GAPPPAVNDG TLDSKMNGKE
     SGDRPKKGFN KALGRIIQGE DSDSDYSEPK NDDDPSLDED DEEFMKRVKK TKAEKLSLVD
     HSKIEYEPFR KNFYIEVKDI SRMTQEEVNT YRKELELKVH GKDVPRPIKF WHQTGLTSKI
     LDTMKKLNYE KPMPIQTQAL PIIMSGRDCI GVAKTGSGKT LGFVLPMLRH IKDQPPVEAG
     DGPIGLVMAP TRELVQQIHS DIRKFSKPLG IRCVPVYGGS GVAQQISELK RGTEIVVCTP
     GRMIDILCTS SGKITNLRRV TFLVMDEADR MFDMGFEPQI TRIIQNIRPE RQTVLFSATF
     PRQVETLARK VLNKPVEIQV GGRSVVNKDI TQLVEVRPES DRFLRLLELL GEWSEKGKIL
     VFVQSQEKCD ALYRDMIKSS YPCLSLHGGK DQTDRESTIS DFKNDVCNLL IATSVAARGL
     DVKELELVVN FDAPNHYEDY VHRVGRTGRA GRKGCAVTFI SEDDAKYAPD LVKALELSEQ
     PVPDDLKALA DGFMVKVKQG IEQAHGTGYG GSGFKFNEEE EEVRKAAKKA QAKEYGFEED
     KSDSEDENDV VRKAGGGEIS QQQATFAQIA AIAAAAKAAA AAPVSAPVTA NQLLANGGGL
     AAMPGVLPVT VPTLPSEGAG RAAAMVAAMN LQHNLAKIQA DAMPEHYEAE LEINDFPQNA
     RWKVTHKETL GPISEWTGAA ITTRGQFYPT GRIPGPGERK LYLFIEGPSE KSVKHAKAEL
     KRVLEDITNQ AMSSLPGGAS GRYSVL
 
 
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