位置:首页 > 蛋白库 > DDX4_MACFA
DDX4_MACFA
ID   DDX4_MACFA              Reviewed;         725 AA.
AC   Q4R5S7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX4;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q61496};
DE   AltName: Full=DEAD box protein 4;
DE   AltName: Full=Vasa homolog;
GN   Name=DDX4; ORFNames=QtsA-21246;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to
CC       repress transposable elements and preventing their mobilization, which
CC       is essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements during
CC       meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC       governs the methylation and subsequent repression of transposons.
CC       Involved in the secondary piRNAs metabolic process, the production of
CC       piRNAs in fetal male germ cells through a ping-pong amplification
CC       cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase
CC       activity enables utilization of one of the slice cleavage fragments
CC       generated by PIWIL2 and processing these pre-piRNAs into piRNAs.
CC       {ECO:0000250|UniProtKB:Q61496}.
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:Q61496};
CC   -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC       TDRD7 and DDX4. Interacts with RANBP9. Interacts with RANBP10.
CC       Interacts with PIWIL2 and MAEL. Interacts with ARNTL/BMAL1 and CLOCK.
CC       Interacts with Tex19.1 and, probably, Tex19.2.
CC       {ECO:0000250|UniProtKB:Q61496}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61496}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}.
CC       Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC       specific organelle required to repress transposon activity during
CC       meiosis. {ECO:0000250|UniProtKB:Q61496}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC       subfamily. {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; AB169466; BAE01548.1; -; mRNA.
DR   RefSeq; NP_001270270.1; NM_001283341.1.
DR   AlphaFoldDB; Q4R5S7; -.
DR   SMR; Q4R5S7; -.
DR   STRING; 9541.XP_005556970.1; -.
DR   PRIDE; Q4R5S7; -.
DR   GeneID; 101867046; -.
DR   CTD; 54514; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR   GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR   GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR   GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS: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; 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; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW   Hydrolase; Meiosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN           1..725
FT                   /note="Probable ATP-dependent RNA helicase DDX4"
FT                   /id="PRO_0000054978"
FT   DOMAIN          320..503
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          531..676
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..248
FT                   /note="Interaction with RANBP9"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQI0"
FT   REGION          702..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           289..317
FT                   /note="Q motif"
FT   MOTIF           447..450
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000250|UniProtKB:Q61496"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64060"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61496"
FT   MOD_RES         723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61496"
SQ   SEQUENCE   725 AA;  79168 MW;  5780C6A6BB44C17D CRC64;
     MGDEDWEAEI NPHMSSYVPI FEKDRYSSGE NGDNFNRTPT SSSEMDDGPS RRDHFMKSGF
     ASGRNFGNRD AGESNKRDNT STMGGFGVGK SFGNRGFSNS KFEDGDSSGF WRESSNDCED
     NPTRNRGFSK RGGYRDGNNS EASGPSRRGG RSSFRGCRGG FGLGSPNNDL DPDECMQRTG
     GLFGSRRPAL SGTGNGDTSQ SRSGSGSERG GYKGLNEEVI TGSGKNSWKS EAEGGESSDT
     QGPKVTYIPP PPPEDEDSIF AHYQTGISFD KYDTILVEVS GHDAPPAILT FEEANLCQTL
     NNNIAKAGYT KLTPVQKYSI PIILAGRDLM ACAQTGSGKT AAFLLPILAH MMHDGITASC
     FKELQEPECI IVAPTRELVN QIYLEARKFS FGTCVRAVVI YGGTQLGHSI RQIVQGCNIL
     CATPGRLMDI IGKEKIGLKQ IKYLVLDEAD RMLDMGFGPE MKKLISCPGM PSKEQRQTLM
     FSATFPEEIQ RLAAEFLKSN YLFVAVGQVG GACRDVQQTV LQVGQFSKRE KLVEILRNIG
     DERTMVFVET KKKADFIATF LCQEKISTTS IHGDREQRER EQALGDFRCG KCPVLVATSV
     AARGLDIENV QHVINFDLPS TIDEYVHRIG RTGRCGNTGR AISFFDLESD NHLAQPLVKV
     LTDAQQDVPA WLEEIAFSTY IPGFSGSTRG NVFASVDTRK GKSSLNTAGF SSSQAPNPVD
     DESWD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024