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SUV3_RAT
ID   SUV3_RAT                Reviewed;         776 AA.
AC   Q5EBA1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYB8};
DE   AltName: Full=Suppressor of var1 3-like protein 1;
DE            Short=SUV3-like protein 1;
DE   Flags: Precursor;
GN   Name=Supv3l1;
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=Liver;
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).
CC   -!- FUNCTION: Major helicase player in mitochondrial RNA metabolism.
CC       Component of the mitochondrial degradosome (mtEXO) complex, that
CC       degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality
CC       in an ATP-dependent manner. Involved in the degradation of non-coding
CC       mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules. ATPase
CC       and ATP-dependent multisubstrate helicase, able to unwind double-
CC       stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3'
CC       direction. Plays a role in the RNA surveillance system in mitochondria;
CC       regulates the stability of mature mRNAs, the removal of aberrantly
CC       formed mRNAs and the rapid degradation of non coding processing
CC       intermediates. Also implicated in recombination and chromatin
CC       maintenance pathways. May protect cells from apoptosis. Associates with
CC       mitochondrial DNA. {ECO:0000250|UniProtKB:Q8IYB8}.
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:Q8IYB8};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8IYB8};
CC   -!- ACTIVITY REGULATION: Helicase activity toward DNA substrate is
CC       inhibited by micromolar concentrations of 5,6-dichloro-1-(beta-D-
CC       ribofuranosyl)benzotriazole (DRBT) and 4,5,6,7-tetrabromobenzotriazole
CC       (TBBT). Helicase activity toward RNA substrate is inhibited by elevated
CC       concentrations of TBBT. Inhibited by some ring-expanded nucleoside
CC       analogs. {ECO:0000250|UniProtKB:Q8IYB8}.
CC   -!- SUBUNIT: Homodimer; in free form. Component of the mitochondrial
CC       degradosome (mtEXO) complex which is a heteropentamer containing 2
CC       copies of SUPV3L1 and 3 copies of PNPT1. As part of mitochondrial
CC       degradosome complex, interacts with GRSF1 in a RNA-dependent manner;
CC       the interaction enhances the activity of the complex. Interacts with
CC       LAMTOR5/HBXIP, WRN and BLM. {ECO:0000250|UniProtKB:Q8IYB8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYB8}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:Q8IYB8}. Mitochondrion
CC       matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q8IYB8}.
CC   -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
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DR   EMBL; BC089883; AAH89883.1; -; mRNA.
DR   RefSeq; NP_001012480.1; NM_001012462.1.
DR   AlphaFoldDB; Q5EBA1; -.
DR   SMR; Q5EBA1; -.
DR   STRING; 10116.ENSRNOP00000000441; -.
DR   iPTMnet; Q5EBA1; -.
DR   PhosphoSitePlus; Q5EBA1; -.
DR   PaxDb; Q5EBA1; -.
DR   PRIDE; Q5EBA1; -.
DR   GeneID; 294385; -.
DR   KEGG; rno:294385; -.
DR   UCSC; RGD:1305565; rat.
DR   CTD; 6832; -.
DR   RGD; 1305565; Supv3l1.
DR   eggNOG; KOG0953; Eukaryota.
DR   InParanoid; Q5EBA1; -.
DR   OrthoDB; 1106167at2759; -.
DR   PhylomeDB; Q5EBA1; -.
DR   PRO; PR:Q5EBA1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0045025; C:mitochondrial degradosome; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; 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:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR   GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0035946; P:mitochondrial mRNA surveillance; ISS:UniProtKB.
DR   GO; GO:0035945; P:mitochondrial ncRNA surveillance; ISS:UniProtKB.
DR   GO; GO:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR   GO; GO:2000827; P:mitochondrial RNA surveillance; ISS:UniProtKB.
DR   GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR   CDD; cd17913; DEXQc_Suv3; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022192; SUV3_C.
DR   InterPro; IPR041082; Suv3_C_1.
DR   InterPro; IPR044774; Suv3_DEXQc.
DR   InterPro; IPR041453; Suv3_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12513; SUV3_C; 1.
DR   Pfam; PF18147; Suv3_C_1; 1.
DR   Pfam; PF18114; Suv3_N; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; Mitochondrion;
KW   Mitochondrion nucleoid; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..776
FT                   /note="ATP-dependent RNA helicase SUPV3L1, mitochondrial"
FT                   /id="PRO_0000310547"
FT   DOMAIN          194..334
FT                   /note="Helicase ATP-binding"
FT   DOMAIN          353..521
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          650..776
FT                   /note="Interaction with LAMTOR5, important for protein
FT                   stability"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT   REGION          689..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..776
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYB8"
FT   MOD_RES         722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IYB8"
SQ   SEQUENCE   776 AA;  86706 MW;  E2C263973DCC0396 CRC64;
     MSLPRCALLW ARLPAGRGAG PRAAPCSALR ALVGSFPGAS GRVPCLAASS SASGGSKAPN
     TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKILDKF YKRQEIQKLS ADYGLDARLF
     HQAFISFRNY IMQSHSLDVD IHIVLNDICF SAAHVDDLFP FFLRHAKQIF PVLECKDDLR
     QISDLRRPPN WYPEARAIQR KIIFHSGPTN SGKTYHAIQR YLSATSGVYC GPLKLLAHEI
     FEKSNAAGVP CDLVTGEERL TVEPEGKQAT HVSCTVEMCN VATPYEVAVI DEIQMIRDPA
     RGWAWTRALL GLCAEEVHLC GESAAIDLVT ELLYTTGEEV EVQKYERLTP ISVLDRALES
     LDNLRPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQARK FNDPNDPCKI
     LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGEKELEPIT TSQALQIAGR AGRFSSHFKE
     GEVTTMHRDD LALLKEILNR PVDPIQAAGL HPTAEQIEMF AYHLPETTLS NLIDIFVDFA
     QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
     EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVFDLYLW LSYRFIDMFP DSSFVRSLQK
     ELDVIIQEGV HNITKLIKIS ESHKLLNLEP SGSQSRLPGA SKSPARRTRG TKTGNKAAEP
     PSPSDKELPL ASRLVQQGLL TADMLKQLQK EWLTQRPEQG KEKVGTRRKK KDPNSD
 
 
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