CAF1_SCHPO
ID CAF1_SCHPO Reviewed; 335 AA.
AC O74856;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Poly(A) ribonuclease pop2;
DE EC=3.1.13.4;
DE AltName: Full=CCR4-associated factor 1;
GN Name=caf1; Synonyms=pop2; ORFNames=SPCC18.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; THR-304 AND SER-306, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-274 IN COMPLEX WITH MAGNESIUM
RP IONS, FUNCTION IN MRNA DEADENYLATION, AND MUTAGENESIS OF ASP-53.
RX PubMed=17452359; DOI=10.1093/nar/gkm178;
RA Jonstrup A.T., Andersen K.R., Van L.B., Brodersen D.E.;
RT "The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit
RT unveils the configuration of an active enzyme.";
RL Nucleic Acids Res. 35:3153-3164(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-274 IN COMPLEX WITH ZINC AND
RP MANGANESE IONS, FUNCTION IN MRNA DEADENYLATION, AND COFACTOR.
RX PubMed=19307292; DOI=10.1261/rna.1489409;
RA Andersen K.R., Jonstrup A.T., Van L.B., Brodersen D.E.;
RT "The activity and selectivity of fission yeast Pop2p are affected by a high
RT affinity for Zn2+ and Mn2+ in the active site.";
RL RNA 15:850-861(2009).
CC -!- FUNCTION: Acts as the catalytic component of the CCR4-NOT core complex,
CC which in the nucleus seems to be a general transcription factor, and in
CC the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In
CC vivo and in vitro, caf1 has 3'-exoribonuclease activity with a
CC preference for poly(A) RNAs. {ECO:0000269|PubMed:17452359,
CC ECO:0000269|PubMed:19307292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19307292};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:19307292};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19307292};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19307292};
CC Note=Binds 1 Zn(2+) ion per subunit. At lower physiological Zn(2+)
CC concentrations, Mg(2+) replaces Zn(2+). The nature of the bound ion
CC affects the speed of the RNA degradation reaction and, to a limited
CC extent, base selectivity. {ECO:0000269|PubMed:19307292};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21420.2; -; Genomic_DNA.
DR PIR; T41149; T41149.
DR RefSeq; NP_588385.2; NM_001023376.2.
DR PDB; 2P51; X-ray; 1.40 A; A=4-335.
DR PDB; 3G0Z; X-ray; 2.00 A; A=4-335.
DR PDB; 3G10; X-ray; 2.60 A; A=4-335.
DR PDBsum; 2P51; -.
DR PDBsum; 3G0Z; -.
DR PDBsum; 3G10; -.
DR AlphaFoldDB; O74856; -.
DR SMR; O74856; -.
DR BioGRID; 275614; 94.
DR STRING; 4896.SPCC18.06c.1; -.
DR iPTMnet; O74856; -.
DR MaxQB; O74856; -.
DR PaxDb; O74856; -.
DR PRIDE; O74856; -.
DR EnsemblFungi; SPCC18.06c.1; SPCC18.06c.1:pep; SPCC18.06c.
DR GeneID; 2539041; -.
DR KEGG; spo:SPCC18.06c; -.
DR PomBase; SPCC18.06c; caf1.
DR VEuPathDB; FungiDB:SPCC18.06c; -.
DR eggNOG; KOG0304; Eukaryota.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; O74856; -.
DR OMA; DTKWISF; -.
DR BRENDA; 3.1.13.4; 5613.
DR EvolutionaryTrace; O74856; -.
DR PRO; PR:O74856; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:PomBase.
DR GO; GO:0030015; C:CCR4-NOT core complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; EXP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; ISS:PomBase.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:PomBase.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
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 3D-structure; Activator; Cytoplasm; Exonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..335
FT /note="Poly(A) ribonuclease pop2"
FT /id="PRO_0000362142"
FT REGION 292..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19307292"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19307292"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19307292"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 53
FT /note="D->A: No nuclease activity."
FT /evidence="ECO:0000269|PubMed:17452359"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2P51"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2P51"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2P51"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:2P51"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:2P51"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:2P51"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2P51"
SQ SEQUENCE 335 AA; 37533 MW; CDC2E9460D9465E8 CRC64;
MTAMNSNFSY PALGVDGISS QISPIRDVWS TNLQQEMNLI MSLIERYPVV SMDTEFPGVV
ARPLGVFKSS DDYHYQTLRA NVDSLKIIQI GLALSDEEGN APVEACTWQF NFTFNLQDDM
YAPESIELLT KSGIDFKKHQ EVGIEPADFA ELLIGSGLVL QEEVTWITFH SGYDFAYLLK
AMTQIPLPAE YEEFYKILCI YFPKNYDIKY IMKSVLNNSK GLQDIADDLQ IHRIGPQHQA
GSDALLTARI FFEIRSRYFD GSIDSRMLNQ LYGLGSTGSV LWHNNSSTPQ IQFRDLPGAH
PSPTPSNAGI PTTLTNTSSA PNFANSTFRF PPRVV
