AQR_MOUSE
ID AQR_MOUSE Reviewed; 1481 AA.
AC Q8CFQ3; P97871; Q3U9N1; Q3ULE8; Q80TX8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=RNA helicase aquarius;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O60306};
DE AltName: Full=Intron-binding protein of 160 kDa {ECO:0000250|UniProtKB:O60306};
GN Name=Aqr; Synonyms=Kiaa0560;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-794, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=9626505;
RX DOI=10.1002/(sici)1097-0177(199806)212:2<304::aid-aja15>3.0.co;2-3;
RA Sam M., Wurst W., Klueppel M., Jin O., Heng H., Bernstein A.;
RT "Aquarius, a novel gene isolated by gene trapping with an RNA-dependent RNA
RT polymerase motif.";
RL Dev. Dyn. 212:304-317(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. Intron-binding spliceosomal protein required to link pre-
CC mRNA splicing and snoRNP (small nucleolar ribonucleoprotein)
CC biogenesis. Plays a key role in position-dependent assembly of intron-
CC encoded box C/D small snoRNP, splicing being required for snoRNP
CC assembly. May act by helping the folding of the snoRNA sequence. Binds
CC to intron of pre-mRNAs in a sequence-independent manner, contacting the
CC region between snoRNA and the branchpoint of introns (40 nucleotides
CC upstream of the branchpoint) during the late stages of splicing. Has
CC ATP-dependent RNA helicase activity and can unwind double-stranded RNA
CC molecules with a 3' overhang (in vitro).
CC {ECO:0000250|UniProtKB:O60306}.
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 Evidence={ECO:0000250|UniProtKB:O60306};
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the XAB2
CC complex, a multimeric protein complex composed of XAB2, PRPF19, AQR,
CC ZNF830, ISY1, and PPIE. Identified in a pentameric intron-binding (IB)
CC complex composed of AQR, XAB2, ISY1, ZNF830 and PPIE that is
CC incorporated into the spliceosome as a preassembled complex. The IB
CC complex does not contain PRPF19. Within the spliceosome, interacts with
CC SNRPA1, SF3B1, SF3B3, SF3A1 and SF3A2. {ECO:0000250|UniProtKB:O60306}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60306}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:O60306}. Note=Localizes to speckle-
CC like regions of the nucleoplasm. {ECO:0000250|UniProtKB:O60306}.
CC -!- DEVELOPMENTAL STAGE: First detected at 8.5 dpc, when neural crest cells
CC are visible at the lateral ridges of the neural plate. During
CC embryogenesis, it is expressed in mesoderm, in the neural crest (and
CC its target tissues) and in neuroepithelium.
CC {ECO:0000269|PubMed:9626505}.
CC -!- INDUCTION: By retinoic acid (RA). {ECO:0000269|PubMed:9626505}.
CC -!- DOMAIN: Contains an N-terminal domain with structural similarity to ARM
CC repeat regions; this domain functions as scaffold for protein-protein
CC interactions, but is not required for RNA binding or for ATP-dependent
CC RNA helicase activity. {ECO:0000250|UniProtKB:O60306}.
CC -!- SIMILARITY: Belongs to the CWF11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50008.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65592.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122310; BAC65592.1; ALT_INIT; mRNA.
DR EMBL; AK145547; BAE26500.1; -; mRNA.
DR EMBL; AK151716; BAE30635.1; -; mRNA.
DR EMBL; BC042479; AAH42479.1; -; mRNA.
DR EMBL; U90333; AAB50008.1; ALT_SEQ; mRNA.
DR CCDS; CCDS16565.1; -.
DR RefSeq; NP_001277717.1; NM_001290788.1.
DR RefSeq; NP_033832.2; NM_009702.3.
DR AlphaFoldDB; Q8CFQ3; -.
DR SMR; Q8CFQ3; -.
DR BioGRID; 198178; 1.
DR IntAct; Q8CFQ3; 1.
DR STRING; 10090.ENSMUSP00000047157; -.
DR iPTMnet; Q8CFQ3; -.
DR PhosphoSitePlus; Q8CFQ3; -.
DR EPD; Q8CFQ3; -.
DR MaxQB; Q8CFQ3; -.
DR PaxDb; Q8CFQ3; -.
DR PRIDE; Q8CFQ3; -.
DR ProteomicsDB; 296275; -.
DR Antibodypedia; 53026; 95 antibodies from 20 providers.
DR DNASU; 11834; -.
DR Ensembl; ENSMUST00000043160; ENSMUSP00000047157; ENSMUSG00000040383.
DR GeneID; 11834; -.
DR KEGG; mmu:11834; -.
DR UCSC; uc008lqd.4; mouse.
DR CTD; 9716; -.
DR MGI; MGI:1276102; Aqr.
DR VEuPathDB; HostDB:ENSMUSG00000040383; -.
DR eggNOG; KOG1806; Eukaryota.
DR GeneTree; ENSGT00940000156668; -.
DR InParanoid; Q8CFQ3; -.
DR OMA; YQFIDVP; -.
DR OrthoDB; 867854at2759; -.
DR PhylomeDB; Q8CFQ3; -.
DR TreeFam; TF105711; -.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 11834; 29 hits in 72 CRISPR screens.
DR ChiTaRS; Aqr; mouse.
DR PRO; PR:Q8CFQ3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CFQ3; protein.
DR Bgee; ENSMUSG00000040383; Expressed in mandibular prominence and 253 other tissues.
DR ExpressionAtlas; Q8CFQ3; baseline and differential.
DR Genevisible; Q8CFQ3; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032174; Aquarius_N.
DR InterPro; IPR026300; CWF11_fam.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF5; PTHR10887:SF5; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF16399; Aquarius_N; 1.
DR PIRSF; PIRSF038901; AQR_cwf11; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome.
FT CHAIN 1..1481
FT /note="RNA helicase aquarius"
FT /id="PRO_0000252390"
FT REGION 1..416
FT /note="Helical region with structural similarity to ARM
FT repeat domains"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT REGION 417..1481
FT /note="Required for assembly of the IB complex"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT REGION 754..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 801
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT BINDING 806
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT BINDING 826..831
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT MOD_RES 1055
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60306"
FT CONFLICT 112
FT /note="F -> L (in Ref. 3; AAH42479)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="H -> Y (in Ref. 3; AAH42479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1481 AA; 170294 MW; DD0687337803C06B CRC64;
MAAPAQPKKI VAPTVSQINA EFVTQLACKY WAPHIKKKSP FDIKVIEEIY EKEIVKSRFA
IRKIMLLEFS QYLENYLWMN YSPEVSSKAY LMSICCMVNE KFRENVPAWE TFKKKPDHFP
FFFKCILKAA LAETDGEFSL HEQTLLLLFL DHCFNSLEVD LIRSQVQQLI SLPMWMGLQP
ARLELELKKT PKLRKFWNLI KKNDEKMDPE AREQAYQERR FLSRLIQKFI SVLKSIPLSE
PVTMDKVHYC ERFIELMIDL EALLPTRRWF NTILDDSHLL VHCYLSSLVH REEDGHLFSQ
LLDMLKFYTG FEINDQTGNA LTENEMTTIH YDRITSLQRA AFAHFPELYD FALSNVAEVD
ARDSLVKFFG PLSSNTLHQV ASYLCLLPTL PKNEDTTFDK EFLLELLVSR HERRISQIQQ
LNQMPLYPTE KIIWDENIVP TEYYSGEGCL ALPKLNLQFL TLHDYLLRNF NLFRLESTYE
IRQDIEDSVS RMKPWQSEYG GVVFGGWARM AQPIVAFTVV EVAKPNIGEN WPTRVRADVT
INLNVRDHIK DEWEGLRKHD VCFLITVRPT KPYGTKFDRR RPFIEQVGLV YVRGCEIQGM
LDDKGRVIED GPEPRPNLRG ESRTFRVFLD PNQYQQDMTN TIQNGAEDVY DTFNVIMRRK
PKENNFKAVL ETIRNLMNTD CVVPDWLHDI ILGYGDPSSA HYSKMPNQIA TLDFNDTFLS
IEHLKASFPG HNVKVTVSDP ALQIPPFRIT FPVRSGKGKK RKDADGEEDD TEEAKTLIVE
PHVIPNRGPY PYNQPKRNTI QFTHTQIEAI RAGMQPGLTM VVGPPGTGKT DVAVQIISNI
YHNFPEQRTL IVTHSNQALN QLFEKIMALD IDERHLLRLG HGEEELETEK DFSRYGRVNY
VLARRIELLE EVKRLQKSLG VPGDASYTCE TAGYFFLYQV MSRWEEYMSR VKNSGTACPD
AAPDAAQVAT FFPFHEYFAN APQPIFKGRS YEEDMEIAEG CFRHIKKIFT QLEEFRASEL
LRSGLDRSKY LLVKEAKIIA MTCTHAALKR HDLVKLGFKY DNILMEEAAQ ILEIETFIPL
LLQNPQDGFS RLKRWIMIGD HHQLPPVIKN MAFQKYSNME QSLFTRFVRV GVPTVDLDAQ
GRARASLCNL YNWRYKNLGN LPHVQLLPEF STANAGLLYD FQLINVEDFQ GVGESEPNPY
FYQNLGEAEY VVALFMYMCL LGYPADKISI LTTYNGQKHL IRDIINRRCG NNPLIGRPNK
VTTVDRFQGQ QNDYILLSLV RTRAVGHLRD VRRLVVAMSR ARLGLYIFAR VSLFQNCFEL
TPAFSQLTAR PLHLHIIPTE PFPTSRKNGE RPPHEVQVIK NMPQMANFVY NMYMHLIQTT
HHYHQTFLQL PPAMVEEGEE GQSQETEMEA EEETVSAQGN LTPSPADASL SQETPAAQPD
CSSQTEDTSA PCDIATAAEP VSAAAEAATP QDAESVPTET E
