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PARNL_ARATH
ID   PARNL_ARATH             Reviewed;         618 AA.
AC   Q8W4C3; Q9LSV7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Poly(A)-specific ribonuclease PARN-like;
DE            EC=3.1.13.4;
DE   AltName: Full=Polyadenylate-specific ribonuclease-like protein;
GN   OrderedLocusNames=At3g25430; ORFNames=MWL2.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of
CC       mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic
CC       degradation of the poly(A) tail is often the first step in the decay of
CC       eukaryotic mRNAs (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:O95453};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01314.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g25430 and At3g25440.; Evidence={ECO:0000305};
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DR   EMBL; AB025639; BAB01314.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77010.1; -; Genomic_DNA.
DR   EMBL; AY062664; AAL32742.1; -; mRNA.
DR   EMBL; BT008385; AAP37744.1; -; mRNA.
DR   RefSeq; NP_189170.1; NM_113439.3.
DR   AlphaFoldDB; Q8W4C3; -.
DR   SMR; Q8W4C3; -.
DR   STRING; 3702.AT3G25430.1; -.
DR   PaxDb; Q8W4C3; -.
DR   ProteomicsDB; 236357; -.
DR   EnsemblPlants; AT3G25430.1; AT3G25430.1; AT3G25430.
DR   GeneID; 822127; -.
DR   Gramene; AT3G25430.1; AT3G25430.1; AT3G25430.
DR   KEGG; ath:AT3G25430; -.
DR   Araport; AT3G25430; -.
DR   TAIR; locus:2094533; AT3G25430.
DR   eggNOG; KOG1990; Eukaryota.
DR   HOGENOM; CLU_020384_1_0_1; -.
DR   InParanoid; Q8W4C3; -.
DR   OMA; SRVKHWK; -.
DR   OrthoDB; 1402758at2759; -.
DR   PhylomeDB; Q8W4C3; -.
DR   PRO; PR:Q8W4C3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8W4C3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0043169; F:cation binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:1905392; P:plant organ morphogenesis; IMP:TAIR.
DR   Gene3D; 3.30.420.10; -; 2.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF04857; CAF1; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW   Nuclease; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..618
FT                   /note="Poly(A)-specific ribonuclease PARN-like"
FT                   /id="PRO_0000371550"
FT   REGION          588..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         56
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         332
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
FT   BINDING         418
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:O95453"
SQ   SEQUENCE   618 AA;  68807 MW;  1363FD2AA57F5082 CRC64;
     MQRRFLSSIS ATAGNTKTLN QGRWSVKQVK KSNFHVTLDE IRTSIDSSDF IALSLQNTGS
     YAAAWHRVSA IDTPQTSYLK AKYAAERYQI LQFALCPFSL QGSKLTVHPY NFHLFPRDEL
     KCGMPSYSFS CQASRLTAMA REGFDFNICI YEGISYLSRA QESASKFLSE NPILADSVTV
     SSSPATVADT VFVGRIRSRV KNWRQSCIDS GSKTGDDDLV SSLRRLVLGS EQYGSRLCLT
     IDVCSERQVQ LILEMLTEFS DDVVPLLVAS KSRGTQAVRT VFMSSKEDKD LFKRELKDLE
     KEENRRVRGF REVVDFISSS QKPVVSQNYL SDFTSIHAKF LGPLPSNVDD FSSSLSSAFP
     NVVDLSQFMK EISPLSNISN LPAAMSSLNR FFAPVDVEVA NQGCPVKLDE GHQSHGQNAV
     MISQLFAKLC TIQKSDLSTI QSNEDFQALA SDEHANSVTS CSKNAGDENV KVWSKNSRRV
     SSENLVFIWG LGKKMTAAKL KNVLQKSHPV FAREFDVKYI DRSSAILVFW ESGPSETFLS
     AVNNEEQLDG SLREMVAEGL RGAGYETYKR ACRLGFWEAD LAESLDKALE SSDTDPDSDT
     KPSEIDWSNE LAINFDEL
 
 
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