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XRN2_CAEBR
ID   XRN2_CAEBR              Reviewed;         976 AA.
AC   Q60SG7; A8XYW7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=5'-3' exoribonuclease 2 homolog;
DE            EC=3.1.13.-;
GN   Name=xrn-2 {ECO:0000312|WormBase:CBG20900};
GN   ORFNames=CBG20900 {ECO:0000312|WormBase:CBG20900};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. Plays a role in
CC       maintenance of steady-state concentration and turnover of microRNAs
CC       (miRNA) by degradation of mature miRNA. Degradation role is enhanced
CC       when in complex with paxt-1. Partially redundant to xrn-1 in miRNA
CC       guide strand degradation. Implicated in differential regulation of
CC       mRNAs such as let-7 by controlling the accumulation of mature miRNA.
CC       Positively regulates molting of the pharyngeal cuticle.
CC       {ECO:0000250|UniProtKB:Q9U299}.
CC   -!- SUBUNIT: Interacts with paxt-1 (via N-terminus); the interaction is
CC       direct and results in stabilization of xrn-2 in the complex.
CC       {ECO:0000250|UniProtKB:Q9U299}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9U299}.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; HE600928; CAP37834.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q60SG7; -.
DR   SMR; Q60SG7; -.
DR   STRING; 6238.CBG20900; -.
DR   PRIDE; Q60SG7; -.
DR   EnsemblMetazoa; CBG20900.1; CBG20900.1; WBGene00039805.
DR   WormBase; CBG20900; CBP30614; WBGene00039805; Cbr-xrn-2.
DR   eggNOG; KOG2044; Eukaryota.
DR   HOGENOM; CLU_006038_1_2_1; -.
DR   InParanoid; Q60SG7; -.
DR   OMA; CLHYYVH; -.
DR   OrthoDB; 685597at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0004534; F:5'-3' exoribonuclease 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:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0010587; P:miRNA catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IEA:EnsemblMetazoa.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0040034; P:regulation of development, heterochronic; IEA:EnsemblMetazoa.
DR   GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
DR   InterPro; IPR027073; 5_3_exoribonuclease.
DR   InterPro; IPR004859; Put_53exo.
DR   InterPro; IPR041412; Xrn1_helical.
DR   InterPro; IPR017151; Xrn2/3/4.
DR   PANTHER; PTHR12341; PTHR12341; 1.
DR   Pfam; PF17846; XRN_M; 2.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE   3: Inferred from homology;
KW   Exonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Transcription termination; Zinc; Zinc-finger.
FT   CHAIN           1..976
FT                   /note="5'-3' exoribonuclease 2 homolog"
FT                   /id="PRO_0000249915"
FT   ZN_FING         264..281
FT                   /note="CCHC-type"
FT   REGION          411..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..788
FT                   /note="Interaction with paxt-1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U299"
FT   REGION          815..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  111453 MW;  BCF42CBA1961DE28 CRC64;
     MGVPAFFRWL TKKYPATVVN ANEDRQRGVD GRRVPVDCTQ PNPNFQEFDN LYLDMNGIIH
     PCTHPEDRPA PKNEDEMFAL IFEYIDRIFS IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
     ASKEMAEKAA SIEEQRRRLI AEGIAVPQKK KDEEEAHFDS NCITPGTPFM ARLADALRYY
     IHDRVTNDPA WANIEIILSD ANVPGEGEHK IMDYIRKQRG NPAHDPNTVH CLCGADADLI
     MLGIATHEAN FNIIREEFVP NQPRACELCG QYGHELKECR GAENDTDLGD EYCKPEQREK
     NFIFLRIPVL REYLEKEMAM PNLPFQFNLE RALDDWVFLC FFVGNDFLPH LPSLEIREGA
     IDRLIKLYKE MVYEMKGYLT KDGIPELDRV EMIMRGLGKV EDEIFKRRQQ DEERFKENQK
     NKKARMQQYG RGRGGRGRGR GQPAYVPSHG ILAPMSAPMH HSGESTRQMA SDARQAAMQF
     NATNDANAQA AANLKALLNV KGEQSPAEVA AQESRKRKAE QPIIITDEDE EPKDDIRLYE
     SGWKERYYRA KFDVGSDDVD FRHRVAWAYV EGLCWVLRYY YQGCSSWDWY FPYHYAPFAS
     DFETVGEFKP DFTRPTKPFN PLEQLMSVFP AASKQHLPVE WQKLMTEDES PIIDLYPADF
     RIDLNGKKYA WQGVALLPFV DEQRLLETLK SVYPTLTDEE KYRNTRGPNR IFIGRNHKSF
     AFFQQVAESK SNDLVDLDPS LLNGVSGKIS YDSTATAPGL PFPSPVSHEE CQDLPTNCGI
     CVLYEDPEYP ANYVFPAVRL DGAKEAEKTL RPEDWNERRD GRFNPTIGFN RNAPRGGLDL
     SGQRHINHHV RGAMYDRQGG NDNYRGGYRG GYQGGYDDRR GGRGGGGYRG GYNDSRPDFG
     RNYAGREGGG PQHYHEHQPG GGHGRPHDQQ PYQDNRRGGG YHRGGRGNGP TGYQRPPYRG
     GRGRGGGGYQ GNSSWR
 
 
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