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CAF1B_ARATH
ID   CAF1B_ARATH             Reviewed;         286 AA.
AC   Q9S9P2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable CCR4-associated factor 1 homolog 2;
DE            EC=3.1.13.4;
GN   Name=CAF1-2; OrderedLocusNames=At1g15920; ORFNames=T24D18.2;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   FUNCTION.
RX   PubMed=7791755; DOI=10.1128/mcb.15.7.3487;
RA   Draper M.P., Salvadore C., Denis C.L.;
RT   "Identification of a mouse protein whose homolog in Saccharomyces
RT   cerevisiae is a component of the CCR4 transcriptional regulatory complex.";
RL   Mol. Cell. Biol. 15:3487-3495(1995).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Ubiquitous transcription factor required for a diverse set of
CC       processes. It is a component of the CCR4 complex involved in the
CC       control of gene expression (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:7791755}.
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};
CC   -!- SUBUNIT: Component of the CCR4-NOT complex, at least composed of CRR4
CC       and CAF1 proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR   EMBL; AC010924; AAF18489.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29383.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29384.1; -; Genomic_DNA.
DR   EMBL; AY080754; AAL86000.1; -; mRNA.
DR   EMBL; AY114040; AAM45088.1; -; mRNA.
DR   EMBL; AK317215; BAH19897.1; -; mRNA.
DR   PIR; F86293; F86293.
DR   RefSeq; NP_173044.1; NM_101460.3.
DR   RefSeq; NP_973838.1; NM_202109.3.
DR   AlphaFoldDB; Q9S9P2; -.
DR   SMR; Q9S9P2; -.
DR   BioGRID; 23402; 1.
DR   IntAct; Q9S9P2; 1.
DR   STRING; 3702.AT1G15920.2; -.
DR   iPTMnet; Q9S9P2; -.
DR   PaxDb; Q9S9P2; -.
DR   PRIDE; Q9S9P2; -.
DR   ProteomicsDB; 240242; -.
DR   DNASU; 838162; -.
DR   EnsemblPlants; AT1G15920.1; AT1G15920.1; AT1G15920.
DR   EnsemblPlants; AT1G15920.2; AT1G15920.2; AT1G15920.
DR   GeneID; 838162; -.
DR   Gramene; AT1G15920.1; AT1G15920.1; AT1G15920.
DR   Gramene; AT1G15920.2; AT1G15920.2; AT1G15920.
DR   KEGG; ath:AT1G15920; -.
DR   Araport; AT1G15920; -.
DR   TAIR; locus:2200532; AT1G15920.
DR   eggNOG; KOG0304; Eukaryota.
DR   HOGENOM; CLU_027974_0_1_1; -.
DR   InParanoid; Q9S9P2; -.
DR   OMA; NENLHHE; -.
DR   OrthoDB; 931256at2759; -.
DR   PhylomeDB; Q9S9P2; -.
DR   PRO; PR:Q9S9P2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S9P2; baseline and differential.
DR   Genevisible; Q9S9P2; AT.
DR   GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10797; PTHR10797; 1.
DR   Pfam; PF04857; CAF1; 2.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Exonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Nucleus; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..286
FT                   /note="Probable CCR4-associated factor 1 homolog 2"
FT                   /id="PRO_0000371552"
FT   BINDING         44
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   286 AA;  32635 MW;  040102518AE9DE39 CRC64;
     MSQAPNPEEE DDTIEIREVW NHNLEQEMAL IEQSIDDFPY VAMDTEFPGI VCKTVTANPN
     PNPYSIHYEY NYDTLKANVN MLKLIQLGLT LSDEKGNLPT CGTNKQCIWQ FNFREFNVIS
     DMFALDSIEL LRKSAIDLEK NNECGVDAKR FAELLMGSGV VLNDKIHWVT FHCGYDFGYL
     LKLLSGKELP EEISDFFDQM EKFFPVVYDI KYLMGFCTNL YGGLEKIAEL LGVKRVGISH
     QAGSDSLLTL RTFIKMKEFF FTGSLLKYSG FLFGLDNPRL LTGSKN
 
 
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