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DDX1_RAT
ID   DDX1_RAT                Reviewed;         740 AA.
AC   Q641Y8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=ATP-dependent RNA helicase DDX1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 1;
GN   Name=Ddx1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both
CC       RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang
CC       nuclease activity. Possesses ATPase activity on various RNA, but not
CC       DNA polynucleotides. May play a role in RNA clearance at DNA double-
CC       strand breaks (DSBs), thereby facilitating the template-guided repair
CC       of transcriptionally active regions of the genome. Together with RELA,
CC       acts as a coactivator to enhance NF-kappa-B-mediated transcriptional
CC       activation. Acts as a positive transcriptional regulator of cyclin
CC       CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates
CC       with chromatin at the NF-kappa-B promoter region via association with
CC       RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and
CC       polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase
CC       complex required to facilitate the enzymatic turnover of catalytic
CC       subunit RTCB: together with archease (ZBTB8OS), acts by facilitating
CC       the guanylylation of RTCB, a key intermediate step in tRNA ligation.
CC       Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic
CC       sensor of viral double-stranded RNA (dsRNA) and plays a role in the
CC       activation of a cascade of antiviral responses including the induction
CC       of pro-inflammatory cytokines via the adapter molecule TICAM1.
CC       Specifically binds (via helicase ATP-binding domain) on both short and
CC       long poly(I:C) dsRNA (By similarity). {ECO:0000250|UniProtKB:Q91VR5,
CC       ECO:0000250|UniProtKB:Q92499}.
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: Found in a multi-helicase-TICAM1 complex at least composed of
CC       DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells
CC       with or without poly(I:C) RNA ligand stimulation (By similarity).
CC       Interacts with DHX36 (By similarity). Interacts (via B30.2/SPRY domain)
CC       with DDX21 (via N-terminus); this interaction serves as bridges to
CC       TICAM1 (By similarity). Interacts with FAM98A (via N- and C-terminus)
CC       (By similarity). Interacts with PHF5A (via C-terminus) (By similarity).
CC       Interacts with MBNL1 (By similarity). Interacts with CSTF2 (By
CC       similarity). Interacts with HNRNPK (By similarity). Interacts with ATM
CC       (By similarity). Interacts with RELA (via C-terminus) (By similarity).
CC       Component of the tRNA-splicing ligase complex (By similarity).
CC       Interacts with PQBP1 (By similarity). Interacts with ERCC6 (By
CC       similarity). {ECO:0000250|UniProtKB:Q91VR5,
CC       ECO:0000250|UniProtKB:Q92499}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92499}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:Q92499}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q91VR5}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q91VR5}. Note=Localized with MBNL1, TIAL1 and
CC       YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage
CC       bodies. Forms large aggregates called DDX1 bodies. Relocalized into
CC       multiple foci (IR-induced foci or IRIF) after IR treatment, a process
CC       that depends on the presence of chromosomal DNA and/or RNA-DNA
CC       duplexes. Relocalized at sites of DNA double-strand breaks (DSBs) in an
CC       ATM-dependent manner after IR treatment. Colocalized with RELA in the
CC       nucleus upon TNF-alpha induction. Enters into the nucleus in case of
CC       active transcription while it accumulates in cytosol when transcription
CC       level is low. Colocalizes in the cytosol with DDX21, DHX36 and TICAM1.
CC       Colocalizes in the mitochondria with TICAM1 and poly(I:C) RNA ligand.
CC       The multi-helicase-TICAM1 complex may translocate to the mitochondria
CC       upon poly(I:C) stimulation (By similarity).
CC       {ECO:0000250|UniProtKB:Q91VR5, ECO:0000250|UniProtKB:Q92499}.
CC   -!- DOMAIN: The helicase domain is involved in the stimulation of RELA
CC       transcriptional activity. {ECO:0000250|UniProtKB:Q92499}.
CC   -!- PTM: Phosphorylated by ATM kinase; phosphorylation is increased in
CC       response to ionizing radiation (IR). {ECO:0000250|UniProtKB:Q92499}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC082049; AAH82049.1; -; mRNA.
DR   RefSeq; NP_445866.1; NM_053414.1.
DR   AlphaFoldDB; Q641Y8; -.
DR   SMR; Q641Y8; -.
DR   BioGRID; 249974; 3.
DR   IntAct; Q641Y8; 3.
DR   STRING; 10116.ENSRNOP00000009100; -.
DR   iPTMnet; Q641Y8; -.
DR   PhosphoSitePlus; Q641Y8; -.
DR   jPOST; Q641Y8; -.
DR   PaxDb; Q641Y8; -.
DR   PRIDE; Q641Y8; -.
DR   Ensembl; ENSRNOT00000009100; ENSRNOP00000009100; ENSRNOG00000006652.
DR   GeneID; 84474; -.
DR   KEGG; rno:84474; -.
DR   CTD; 1653; -.
DR   RGD; 619903; Ddx1.
DR   eggNOG; KOG0349; Eukaryota.
DR   GeneTree; ENSGT00940000155678; -.
DR   HOGENOM; CLU_016321_0_0_1; -.
DR   InParanoid; Q641Y8; -.
DR   OMA; EYCIRAI; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q641Y8; -.
DR   TreeFam; TF106114; -.
DR   PRO; PR:Q641Y8; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000006652; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q641Y8; RN.
DR   GO; GO:0071920; C:cleavage body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR   GO; GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:RGD.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISO:RGD.
DR   GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:RGD.
DR   GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD.
DR   GO; GO:0009615; P:response to virus; ISO:RGD.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Antiviral defense; ATP-binding; Cytoplasm;
KW   DNA-binding; Exonuclease; Helicase; Hydrolase; Immunity; Innate immunity;
KW   Isopeptide bond; Mitochondrion; mRNA processing; Nuclease;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Transcription; Transcription regulation; tRNA processing;
KW   Ubl conjugation.
FT   CHAIN           1..740
FT                   /note="ATP-dependent RNA helicase DDX1"
FT                   /id="PRO_0000054988"
FT   DOMAIN          2..428
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          70..247
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          493..681
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..525
FT                   /note="Necessary for interaction with RELA"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   REGION          1..448
FT                   /note="Interaction with dsRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VR5"
FT   REGION          1..295
FT                   /note="Necessary for interaction with HNRNPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   REGION          525..740
FT                   /note="Necessary for interaction with HNRNPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   MOTIF           370..373
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         239
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   MOD_RES         268
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   MOD_RES         281
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        281
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92499"
SQ   SEQUENCE   740 AA;  82497 MW;  D128A389944F0BF8 CRC64;
     MAAFSEMGVM PEIAQAVEEM DWLLPTDIQA ESIPLILGGG DVLMAAETGS GKTGAFSIPV
     IQIVYETLKD QQEGKKGKAT IKTGASVLNK WQMNPYDRGS AFAIGSDGLC CQSREVKEWH
     GCRATRGLLR GKHYYEVSCH DQGLCRVGWS TMQASLDLGT DKFGFGFGGT GKKSHNKQFD
     NYGEEFTMHD TIGCYLDIDK GHVKFSKNGK DLGLAFEIPA HIKNQALFPA CVLKNAELKF
     NFGEEEFKFP PKDGFVALSK APDSYVVKSQ HTGNAQVSQT KFLPNAPKAL IVEPSRELAE
     QTLNNVKQFK KYIDNPKLRE LLIIGGVAAR DQLSVLDNGV DIVVGTPGRL DDLVSTGKLN
     LSQVRFLVLD EADGLLSQGY SDFINRMHNQ IPQITSDGKR LQVIVCSATL HSFDVKKLSE
     KIMHFPTWVD LKGEDSVPDT VHHVVVPVNP KTDRLWERLG KNHIRTDDVH AKDNTRPGAN
     SPEMWSEAIK ILKGEYAVRA IKEHKMDQAI IFCRTKIDCD NLEQYFMQQG GGPDKKGHQF
     SCVCLHGDRK PHERKQNLER FKKGDVRFLI CTDVAARGID IHGVPYVINV TLPDEKQNYV
     HRIGRVGRAE RMGLAISLVA TEKEKVWYHV CSNRGKGCYN TRLKEDGGCT IWYNEMQLLS
     EIEEHLNCTI SQVEPDIKVP VDEFDGKVTY GQKRAAGGGN YKGHVDILAP TVQELAALEK
     EAQTSFLHLG YLPNQLFRTF
 
 
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