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CPL4_ARATH
ID   CPL4_ARATH              Reviewed;         440 AA.
AC   Q00IB6; Q9FJL6;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=RNA polymerase II C-terminal domain phosphatase-like 4;
DE            Short=FCP-like 4;
DE            EC=3.1.3.16;
DE   AltName: Full=Carboxyl-terminal phosphatase-like 4;
DE            Short=AtCPL4;
DE            Short=CTD phosphatase-like 4;
GN   Name=CPL4; OrderedLocusNames=At5g58003; ORFNames=MTI20;
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 [MRNA], FUNCTION, INTERACTION WITH RAP74, INDUCTION BY
RP   NACL, BRCT DOMAIN, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=16905668; DOI=10.1104/pp.106.084939;
RA   Bang W., Kim S., Ueda A., Vikram M., Yun D., Bressan R.A., Hasegawa P.M.,
RA   Bahk J., Koiwa H.;
RT   "Arabidopsis carboxyl-terminal domain phosphatase-like isoforms share
RT   common catalytic and interaction domains but have distinct in planta
RT   functions.";
RL   Plant Physiol. 142:586-594(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
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   [4]
RP   GENE FAMILY.
RX   PubMed=18156295; DOI=10.1104/pp.107.111393;
RA   Kerk D., Templeton G., Moorhead G.B.G.;
RT   "Evolutionary radiation pattern of novel protein phosphatases revealed by
RT   analysis of protein data from the completely sequenced genomes of humans,
RT   green algae, and higher plants.";
RL   Plant Physiol. 146:351-367(2008).
CC   -!- FUNCTION: Processively dephosphorylates 'Ser-2' and/or 'Ser-5' of the
CC       heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC       polymerase II subunit (RPB1). This promotes the activity of RNA
CC       polymerase II (By similarity). Required for normal plant growth.
CC       {ECO:0000250, ECO:0000269|PubMed:16905668}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds Mg(2+), Co(2+) or Mn(2+). {ECO:0000250};
CC   -!- SUBUNIT: Interacts with RAP74. {ECO:0000269|PubMed:16905668}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16905668}.
CC   -!- INDUCTION: By NaCl. {ECO:0000269|PubMed:16905668}.
CC   -!- DOMAIN: The BRCT domain is required for interaction with RAP74.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08870.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At5g58000 and At5g58003.; Evidence={ECO:0000305};
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DR   EMBL; DQ503426; ABF55959.1; -; mRNA.
DR   EMBL; AB013396; BAB08870.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96984.1; -; Genomic_DNA.
DR   RefSeq; NP_001078764.1; NM_001085295.2.
DR   AlphaFoldDB; Q00IB6; -.
DR   SMR; Q00IB6; -.
DR   BioGRID; 624522; 4.
DR   STRING; 3702.AT5G58003.1; -.
DR   PaxDb; Q00IB6; -.
DR   PRIDE; Q00IB6; -.
DR   ProteomicsDB; 220487; -.
DR   EnsemblPlants; AT5G58003.1; AT5G58003.1; AT5G58003.
DR   GeneID; 5008312; -.
DR   Gramene; AT5G58003.1; AT5G58003.1; AT5G58003.
DR   KEGG; ath:AT5G58003; -.
DR   Araport; AT5G58003; -.
DR   TAIR; locus:4010714056; AT5G58003.
DR   eggNOG; KOG0323; Eukaryota.
DR   HOGENOM; CLU_023960_1_0_1; -.
DR   InParanoid; Q00IB6; -.
DR   OrthoDB; 683531at2759; -.
DR   PhylomeDB; Q00IB6; -.
DR   PRO; PR:Q00IB6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q00IB6; baseline and differential.
DR   Genevisible; Q00IB6; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR039189; Fcp1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR23081; PTHR23081; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Nucleus; Reference proteome; Repressor;
KW   RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..440
FT                   /note="RNA polymerase II C-terminal domain phosphatase-like
FT                   4"
FT                   /id="PRO_0000376086"
FT   DOMAIN          118..292
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   DOMAIN          337..429
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  50264 MW;  7712641DC888B82B CRC64;
     MSVASDSPVH SSSSSDDLAA FLDAELDSAS DASSGPSEEE EAEDDVESGL KRQKLEHLEE
     ASSSKGECEH PGSFGNMCFV CGQKLEETGV SFRYIHKEMR LNEDEISRLR DSDSRFLQRQ
     RKLYLVLDLD HTLLNTTILR DLKPEEEYLK SHTHSLQDGC NVSGGSLFLL EFMQMMTKLR
     PFVHSFLKEA SEMFVMYIYT MGDRNYARQM AKLLDPKGEY FGDRVISRDD GTVRHEKSLD
     VVLGQESAVL ILDDTENAWP KHKDNLIVIE RYHFFSSSCR QFDHRYKSLS ELKSDESEPD
     GALATVLKVL KQAHALFFEN VDEGISNRDV RLMLKQVRKE ILKGCKIVFS RVFPTKAKPE
     DHPLWKMAEE LGATCATEVD ASVTHVVAMD VGTEKARWAV REKKYVVHRG WIDAANYLWM
     KQPEENFGLE QLKKQLTEEE
 
 
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