CPS3B_ARATH
ID CPS3B_ARATH Reviewed; 613 AA.
AC Q8GUU3; Q56XW2; Q9ZUA1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 3-II;
DE EC=3.1.27.-;
DE AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit II;
DE Short=AtCPSF73-II;
DE Short=CPSF 73 kDa subunit II;
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 26;
GN Name=CPSF73-II; Synonyms=EDA26, FEG; OrderedLocusNames=At2g01730;
GN ORFNames=T8O11.10;
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], TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14693369; DOI=10.1016/j.gene.2003.09.025;
RA Xu R., Ye X., Quinn Li Q.;
RT "AtCPSF73-II gene encoding an Arabidopsis homolog of CPSF 73 kDa subunit is
RT critical for early embryo development.";
RL Gene 324:35-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CPSF100, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16897494; DOI=10.1007/s11103-006-0051-6;
RA Xu R., Zhao H., Dinkins R.D., Cheng X., Carberry G., Li Q.Q.;
RT "The 73 kD subunit of the cleavage and polyadenylation specificity factor
RT (CPSF) complex affects reproductive development in Arabidopsis.";
RL Plant Mol. Biol. 61:799-815(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF30.
RX PubMed=19573236; DOI=10.1186/1471-2121-10-51;
RA Rao S., Dinkins R.D., Hunt A.G.;
RT "Distinctive interactions of the Arabidopsis homolog of the 30 kD subunit
RT of the cleavage and polyadenylation specificity factor (AtCPSF30) with
RT other polyadenylation factor subunits.";
RL BMC Cell Biol. 10:51-51(2009).
RN [7]
RP COMPONENT OF CPSF COMPLEX.
RX PubMed=19748916; DOI=10.1104/pp.109.142729;
RA Zhao H., Xing D., Li Q.Q.;
RT "Unique features of plant cleavage and polyadenylation specificity factor
RT revealed by proteomic studies.";
RL Plant Physiol. 151:1546-1556(2009).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that play a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. May function as mRNA 3'-end-processing endonuclease
CC and also be involved in the histone 3'-end pre-mRNA processing.
CC {ECO:0000305|PubMed:19748916}.
CC -!- SUBUNIT: Component of the CPSF complex, at least composed of CPSF160,
CC CPSF100, CPSF73-I, CPSF73-II, CPSF30, FY and FIPS5. Interacts with
CC CPSF30, CPSF100, CPSF160 and FY. {ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:19573236}.
CC -!- INTERACTION:
CC Q8GUU3; Q9LKF9: CPSF100; NbExp=3; IntAct=EBI-1775477, EBI-1775444;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:19573236}.
CC -!- TISSUE SPECIFICITY: Highly expressed in senescence leaves, petals,
CC stamens, pollen and late stages of siliques with seeds. Also detected
CC in roots, stems, leaves and seedlings. {ECO:0000269|PubMed:14693369,
CC ECO:0000269|PubMed:16897494}.
CC -!- DOMAIN: The HXHXDH motif is essential for the endoribonuclease activity
CC of the CPSF complex. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:14693369}.
CC -!- MISCELLANEOUS: CPSF73-I and CPSF73-II are not functionally redundant,
CC but both are essential in plant development.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. INTS11 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD12712.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY168923; AAN87883.1; -; mRNA.
DR EMBL; AC006069; AAD12712.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05489.1; -; Genomic_DNA.
DR EMBL; AK221561; BAD94982.1; -; mRNA.
DR PIR; D84428; D84428.
DR RefSeq; NP_178282.2; NM_126234.3.
DR AlphaFoldDB; Q8GUU3; -.
DR SMR; Q8GUU3; -.
DR BioGRID; 105; 5.
DR IntAct; Q8GUU3; 4.
DR STRING; 3702.AT2G01730.1; -.
DR iPTMnet; Q8GUU3; -.
DR PaxDb; Q8GUU3; -.
DR PRIDE; Q8GUU3; -.
DR ProteomicsDB; 224518; -.
DR EnsemblPlants; AT2G01730.1; AT2G01730.1; AT2G01730.
DR GeneID; 814702; -.
DR Gramene; AT2G01730.1; AT2G01730.1; AT2G01730.
DR KEGG; ath:AT2G01730; -.
DR Araport; AT2G01730; -.
DR TAIR; locus:2065368; AT2G01730.
DR eggNOG; KOG1136; Eukaryota.
DR HOGENOM; CLU_009673_3_1_1; -.
DR InParanoid; Q8GUU3; -.
DR OMA; YLDGMIW; -.
DR OrthoDB; 218195at2759; -.
DR PRO; PR:Q8GUU3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GUU3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:TAIR.
DR GO; GO:0016180; P:snRNA processing; IBA:GO_Central.
DR CDD; cd16291; INTS11-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR041897; INTS11-like_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; mRNA processing; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..613
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 3-II"
FT /id="PRO_0000391781"
FT MOTIF 67..72
FT /note="HXHXDH motif"
FT CONFLICT 323
FT /note="T -> I (in Ref. 1; AAN87883)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="F -> L (in Ref. 1; AAN87883)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="P -> L (in Ref. 1; AAN87883)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="Y -> H (in Ref. 1; AAN87883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 68037 MW; 092F96BD861FA098 CRC64;
MAIDCLVLGA GQEIGKSCVV VTINGKKIMF DCGMHMGCDD HNRYPNFSLI SKSGDFDNAI
SCIIITHFHM DHVGALPYFT EVCGYNGPIY MSYPTKALSP LMLEDYRRVM VDRRGEEELF
TTTHIANCMK KVIAIDLKQT IQVDEDLQIR AYYAGHVLGA VMVYAKMGDA AIVYTGDYNM
TTDRHLGAAK IDRLQLDLLI SESTYATTIR GSKYPREREF LQAVHKCVAG GGKALIPSFA
LGRAQELCML LDDYWERMNI KVPIYFSSGL TIQANMYYKM LISWTSQNVK EKHNTHNPFD
FKNVKDFDRS LIHAPGPCVL FATPGMLCAG FSLEVFKHWA PSPLNLVALP GYSVAGTVGH
KLMAGKPTTV DLYNGTKVDV RCKVHQVAFS PHTDAKGIMD LTKFLSPKNV VLVHGEKPSM
MILKEKITSE LDIPCFVPAN GETVSFASTT YIKANASDMF LKSCSNPNFK FSNSTQLRVT
DHRTADGVLV IEKSKKAKIV HQDEISEVLH EKNHVVSLAH CCPVKVKGES EDDDVDLIKQ
LSAKILKTVS GAQIHESENC LQVASFKGSL CLKDKCMHRS SSSSSEAVFL CCNWSIADLE
LGWEIINAIK LNH
