ID   DHX57_MOUSE             Reviewed;        1388 AA.
AC   Q6P5D3; Q3TS93; Q6NZK4; Q6P1B4; Q8BI63; Q8BIA2; Q8R360;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Putative ATP-dependent RNA helicase DHX57;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 57;
GN   Name=Dhx57;
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] (ISOFORMS 3; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Urinary bladder;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Spleen;
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: Probable ATP-binding RNA helicase.
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=5;
CC       Name=1;
CC         IsoId=Q6P5D3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P5D3-2; Sequence=VSP_018063;
CC       Name=3;
CC         IsoId=Q6P5D3-3; Sequence=VSP_018065, VSP_018066;
CC       Name=4;
CC         IsoId=Q6P5D3-4; Sequence=VSP_018062, VSP_018064;
CC       Name=5;
CC         IsoId=Q6P5D3-5; Sequence=VSP_018061;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK035344; BAC29042.1; -; mRNA.
DR   EMBL; AK053628; BAC35451.1; -; mRNA.
DR   EMBL; AK162192; BAE36782.1; -; mRNA.
DR   EMBL; BC026474; AAH26474.1; -; mRNA.
DR   EMBL; BC062952; AAH62952.1; -; mRNA.
DR   EMBL; BC065169; AAH65169.1; -; mRNA.
DR   EMBL; BC066091; AAH66091.1; -; mRNA.
DR   CCDS; CCDS28990.1; -. [Q6P5D3-2]
DR   CCDS; CCDS50188.1; -. [Q6P5D3-1]
DR   RefSeq; NP_001157231.1; NM_001163759.1. [Q6P5D3-1]
DR   RefSeq; NP_945180.2; NM_198942.2. [Q6P5D3-2]
DR   RefSeq; XP_006523510.1; XM_006523447.1.
DR   RefSeq; XP_006523511.1; XM_006523448.1.
DR   RefSeq; XP_017172691.1; XM_017317202.1.
DR   AlphaFoldDB; Q6P5D3; -.
DR   SMR; Q6P5D3; -.
DR   BioGRID; 223127; 6.
DR   IntAct; Q6P5D3; 1.
DR   MINT; Q6P5D3; -.
DR   STRING; 10090.ENSMUSP00000083742; -.
DR   iPTMnet; Q6P5D3; -.
DR   PhosphoSitePlus; Q6P5D3; -.
DR   EPD; Q6P5D3; -.
DR   MaxQB; Q6P5D3; -.
DR   PaxDb; 10090-ENSMUSP00000083742; -.
DR   PeptideAtlas; Q6P5D3; -.
DR   ProteomicsDB; 279767; -. [Q6P5D3-1]
DR   ProteomicsDB; 279768; -. [Q6P5D3-2]
DR   ProteomicsDB; 279769; -. [Q6P5D3-3]
DR   ProteomicsDB; 279770; -. [Q6P5D3-4]
DR   ProteomicsDB; 279771; -. [Q6P5D3-5]
DR   Pumba; Q6P5D3; -.
DR   Antibodypedia; 29537; 77 antibodies from 17 providers.
DR   DNASU; 106794; -.
DR   Ensembl; ENSMUST00000038166.9; ENSMUSP00000041069.8; ENSMUSG00000035051.16. [Q6P5D3-2]
DR   Ensembl; ENSMUST00000086555.11; ENSMUSP00000083742.4; ENSMUSG00000035051.16. [Q6P5D3-1]
DR   GeneID; 106794; -.
DR   KEGG; mmu:106794; -.
DR   UCSC; uc008dqx.2; mouse. [Q6P5D3-5]
DR   UCSC; uc008dqy.2; mouse. [Q6P5D3-4]
DR   UCSC; uc008dqz.2; mouse. [Q6P5D3-2]
DR   UCSC; uc008dra.2; mouse. [Q6P5D3-1]
DR   UCSC; uc008drb.1; mouse. [Q6P5D3-3]
DR   AGR; MGI:2147067; -.
DR   CTD; 90957; -.
DR   MGI; MGI:2147067; Dhx57.
DR   VEuPathDB; HostDB:ENSMUSG00000035051; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   GeneTree; ENSGT00940000156883; -.
DR   HOGENOM; CLU_001832_4_1_1; -.
DR   InParanoid; Q6P5D3; -.
DR   OMA; PERVYVQ; -.
DR   OrthoDB; 1095660at2759; -.
DR   PhylomeDB; Q6P5D3; -.
DR   TreeFam; TF324744; -.
DR   BioGRID-ORCS; 106794; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Dhx57; mouse.
DR   PRO; PR:Q6P5D3; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q6P5D3; Protein.
DR   Bgee; ENSMUSG00000035051; Expressed in saccule of membranous labyrinth and 245 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17985; DEXHc_DHX57; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   CDD; cd14317; UBA_DHX57; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR042615; DHX57_UBA.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF256; ATP-DEPENDENT RNA HELICASE DHX57-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   Genevisible; Q6P5D3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1388
FT                   /note="Putative ATP-dependent RNA helicase DHX57"
FT                   /id="PRO_0000233152"
FT   DOMAIN          175..220
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          555..722
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          832..1012
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         299..326
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           669..672
FT                   /note="DEVH box"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         568..575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P158"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P158"
FT   MOD_RES         475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P158"
FT   VAR_SEQ         1..1160
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018061"
FT   VAR_SEQ         1..1000
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018062"
FT   VAR_SEQ         77..129
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018063"
FT   VAR_SEQ         1001..1006
FT                   /note="LEQLCL -> MILFFF (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018064"
FT   VAR_SEQ         1008..1025
FT                   /note="IKILEMFSTHNLQSVFSR -> LCPSGPPSACLGPAPPPI (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018065"
FT   VAR_SEQ         1026..1388
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018066"
FT   CONFLICT        488
FT                   /note="A -> T (in Ref. 2; AAH66091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="S -> P (in Ref. 2; AAH62952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        725
FT                   /note="A -> T (in Ref. 2; AAH66091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1137
FT                   /note="T -> A (in Ref. 1; BAC29042)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1388 AA;  155762 MW;  D3E57C648E53A805 CRC64;
     MSSSVRRKGK PGKGDGKGSS RGGRGGKGHM NKSHGGGGGG GGSCGGGGGG SRKASNRIWD
     DGDDFCVFTE PKRPSRPCDS NKSKGETRPK WKPKAKVPLQ TLHMTSENQE KVKALLRDLQ
     EQGADAGSER GTSGEEEDSE PQCGEEQGWP AGQEPIFLPD CSPWEYIGPE EVEPPVPECA
     VSPLAVQKLS RYGFHTEHCQ LALRICDGDL GAALEHLLRQ CFSETFGERM ALSEAAVYVS
     LNECVEQRQE ETLALKSICG EKFIERIQNR VWTIGLELDY LTNKFCKSKQ KESSKNVRDT
     SPETCKFYLK GNCKFGSKCK FKHEVPPHQM IGRAERNVND PHLDADDDTT FMYELQIRFS
     KDHKYPYQAP LVAFYSTNEN LPLACRLHIS EFLYGKALEF AKTSEPVVYS LITLLEEESE
     IVKLLTHTQH KYSVPPVNVP PVPSETRISK PAYRKPVVPS NTFLSNQMLE GERLSELEED
     ADEDEGPASI IVENESYVNL KKRSYKRYDR PAKSLFAENS KICRQFQMKQ ASRQFHAILQ
     ERQLLPAWEE RETILKLLSK HQVVVISGMT GCGKTTQIPQ FILDNSLNGP PERVANIICT
     QPRRISAISV AERVAKERAE RVGLTVGYQI RLESVKSSAT RLLYCTTGVL LRRLEGDATL
     QGVTHIIVDE VHERTEESDF LLLVLKDIVM QRATLQVILM SATLDAGLFS KYFSYCPVIT
     IPGRAFPVDQ FFLEDALAVT RYVLQDGSPY MRSMKQIAKE KLKARHNRTA QEEVEEDLRL
     SLHLQDEEES VKDTIPDQQL DFKQLLIRYK GVSKSVIKTM SVMDFEKVNL ELIEALLEWI
     VDGKHAYPPG AVLVFLPGLA EIKMLYEQLQ SNSLFNNRRS HRCVIHPLHS SLSSEEQQAV
     FVKPPMGVTK IIISTNIAET SITIDDVVYV IDSGKMKEKR YDAGKGMESL EDTFVSQANA
     LQRKGRAGRV ASGVCFHLFT SHHYNHQLLK QQLPEIQRVP LEQLCLRIKI LEMFSTHNLQ
     SVFSRLIEPP HIDSLRASKV RLRDLGALTP DEKLTPLGYH LASLPVDVRI GKLMLLGSIF
     RCLDPALTIA ASLAFKSPFV SPWDKKEEAN QKKLEFAFAN SDYLALLCAY KGWQLSTKES
     ARASYNYCRQ NFLSGRTLQE MASLKRQFTE LLSDIGFVKE GLRAKEIEKR AQGGDGVLDA
     TGEEANTNAE NPKLISAVLC AALYPNVVQV KTPEGKFQKT SSGVVRLQPK SAELKFVTKN
     DGYVHIHPSS VNYQVRHFDS PYLLYHEKIK TSRVFIRDCS MVSVYPLVLF GGGQVNVQLQ
     RGAFVVSLDD GWIRFVAASH QVAELVKELR CELDQLLQDK IKNPSMDLCS CPRGSRIISM
     IVKLITTQ
//