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RH15_ORYSJ
ID   RH15_ORYSJ              Reviewed;         432 AA.
AC   Q5JK84; B7F820;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=DEAD-box ATP-dependent RNA helicase 15;
DE            EC=3.6.4.13;
DE   AltName: Full=API5-interacting protein 1 {ECO:0000303|PubMed:21467577};
GN   Name=AIP2 {ECO:0000303|PubMed:21467577};
GN   OrderedLocusNames=Os01g0550000, LOC_Os01g36920;
GN   ORFNames=B1156H12.21-1, OSJNBa0024F24.6-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   FUNCTION, SUBUNIT, INTERACTION WITH API5, AND SUBCELLULAR LOCATION.
RX   PubMed=21467577; DOI=10.1105/tpc.110.082636;
RA   Li X., Gao X., Wei Y., Deng L., Ouyang Y., Chen G., Li X., Zhang Q., Wu C.;
RT   "Rice APOPTOSIS INHIBITOR5 coupled with two DEAD-box adenosine 5'-
RT   triphosphate-dependent RNA helicases regulates tapetum degeneration.";
RL   Plant Cell 23:1416-1434(2011).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in pre-mRNA splicing.
CC       Required for the export of mRNA out of the nucleus (By similarity).
CC       Required for tapetal programmed cell death (PCD) and degeneration
CC       during anther development. Forms dimer with AIP1 and binds the promoter
CC       region of the cysteine protease CP1. Can complement the yeast RNA
CC       helicase SUB2. Plants silencing AIP1 and AIP2 are male sterile
CC       (PubMed:21467577). {ECO:0000250|UniProtKB:Q07478,
CC       ECO:0000269|PubMed:21467577}.
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   -!- SUBUNIT: Homodimer and heterodimer with AIP1 (PubMed:21467577).
CC       Interacts with API5 (PubMed:21467577). {ECO:0000269|PubMed:21467577}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21467577}.
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. DECD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AP004225; BAD88055.1; -; Genomic_DNA.
DR   EMBL; AP004258; BAD88115.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05212.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72635.1; -; Genomic_DNA.
DR   EMBL; AK122050; BAH00768.1; -; mRNA.
DR   RefSeq; XP_015621815.1; XM_015766329.1.
DR   AlphaFoldDB; Q5JK84; -.
DR   SMR; Q5JK84; -.
DR   STRING; 4530.OS01T0550000-01; -.
DR   PaxDb; Q5JK84; -.
DR   PRIDE; Q5JK84; -.
DR   EnsemblPlants; Os01t0550000-01; Os01t0550000-01; Os01g0550000.
DR   GeneID; 4326193; -.
DR   Gramene; Os01t0550000-01; Os01t0550000-01; Os01g0550000.
DR   KEGG; osa:4326193; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q5JK84; -.
DR   OMA; INFELPM; -.
DR   OrthoDB; 779000at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5JK84; baseline and differential.
DR   Genevisible; Q5JK84; OS.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IBA:GO_Central.
DR   GO; GO:0048653; P:anther development; IMP:UniProtKB.
DR   GO; GO:0009555; P:pollen development; IMP:UniProtKB.
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; 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; 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   ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..432
FT                   /note="DEAD-box ATP-dependent RNA helicase 15"
FT                   /id="PRO_0000282496"
FT   DOMAIN          82..255
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..428
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   COILED          3..28
FT                   /evidence="ECO:0000255"
FT   MOTIF           51..79
FT                   /note="Q motif"
FT   MOTIF           202..205
FT                   /note="DEAD box"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   432 AA;  48567 MW;  EE00942821DC1F2F CRC64;
     MGEAEVKDNE VYEEDLVDYE EEVENGADGG AAAANASADV VKKGYVGIHS SGFRDFLLKP
     ELLRAIQDCG FEHPSEVQHE CIPQAILGMD VICQAKSGMG KTAVFVLSSL QQIDPVAGQV
     GALVLCHTRE LAYQICHEFE RFSKYLPEVK VAVFYGGVHI KKHKDLLKND CPHIVVGTPG
     RILALAREKD LSLKNVRHFI LDECDKMLDS LDMRRDVQEI FKMTPHDKQV MMFSATLSKE
     IRPVCKKFMQ DPMEIYVDDE AKLTLHGLVQ HYIKLSEAEK NRKLNDLLDA LDFNQVVIFV
     KSVSRAAELN KLLCECNFPA ISIHSGMTQE ERLTRYKNFK EGHKRILVAT DLVGRGIDIE
     RVNIVINYDM PDSADSYLHR VGRAGRFGTK GLAITFVSSA SDSDVLNQVQ ERFEVDIKEL
     PEQIDTSTYM PS
 
 
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