CPSF3_ARATH
ID CPSF3_ARATH Reviewed; 693 AA.
AC Q9C952; Q8VY18;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 3-I;
DE EC=3.1.27.-;
DE AltName: Full=Cleavage and polyadenylation specificity factor 73 kDa subunit I;
DE Short=AtCPSF73-I;
DE Short=CPSF 73 kDa subunit I;
GN Name=CPSF73-I; OrderedLocusNames=At1g61010; ORFNames=T7P1.15;
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], 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 [2]
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 [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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 [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:0000303|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 CLPS3, CPSF100, CPSF160 and FY. {ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:19573236}.
CC -!- INTERACTION:
CC Q9C952; Q9LKF9: CPSF100; NbExp=4; IntAct=EBI-1775464, EBI-1775444;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16897494,
CC ECO:0000269|PubMed:19573236}.
CC -!- TISSUE SPECIFICITY: Highly expressed in carpels. Also detected in
CC seedlings, roots, stems, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:16897494}.
CC -!- DOMAIN: The HXHXDH motif is essential for the endoribonuclease activity
CC of the CPSF complex. {ECO:0000250}.
CC -!- MISCELLANEOUS: CPSF73-I and CPSF73-II are not functionally redundant,
CC but both are essential in plant development. Knockdown or
CC overexpression of CPSF73-I are lethal.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. INTS11 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY140900; AAN41458.1; -; mRNA.
DR EMBL; AC018908; AAG51638.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33766.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33767.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33768.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58845.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58846.1; -; Genomic_DNA.
DR EMBL; AY150478; AAN13003.1; -; mRNA.
DR EMBL; AY074280; AAL66977.1; -; mRNA.
DR EMBL; AK316692; BAH19419.1; -; mRNA.
DR EMBL; AK316794; BAH19511.1; -; mRNA.
DR PIR; G96635; G96635.
DR RefSeq; NP_001031215.1; NM_001036138.2.
DR RefSeq; NP_001319278.1; NM_001333924.1.
DR RefSeq; NP_001321253.1; NM_001333925.1.
DR RefSeq; NP_176297.1; NM_104782.4.
DR RefSeq; NP_849835.1; NM_179504.2.
DR AlphaFoldDB; Q9C952; -.
DR SMR; Q9C952; -.
DR BioGRID; 27617; 6.
DR DIP; DIP-40388N; -.
DR IntAct; Q9C952; 2.
DR STRING; 3702.AT1G61010.2; -.
DR iPTMnet; Q9C952; -.
DR PaxDb; Q9C952; -.
DR PRIDE; Q9C952; -.
DR ProteomicsDB; 222673; -.
DR EnsemblPlants; AT1G61010.1; AT1G61010.1; AT1G61010.
DR EnsemblPlants; AT1G61010.2; AT1G61010.2; AT1G61010.
DR EnsemblPlants; AT1G61010.3; AT1G61010.3; AT1G61010.
DR EnsemblPlants; AT1G61010.4; AT1G61010.4; AT1G61010.
DR EnsemblPlants; AT1G61010.5; AT1G61010.5; AT1G61010.
DR GeneID; 842393; -.
DR Gramene; AT1G61010.1; AT1G61010.1; AT1G61010.
DR Gramene; AT1G61010.2; AT1G61010.2; AT1G61010.
DR Gramene; AT1G61010.3; AT1G61010.3; AT1G61010.
DR Gramene; AT1G61010.4; AT1G61010.4; AT1G61010.
DR Gramene; AT1G61010.5; AT1G61010.5; AT1G61010.
DR KEGG; ath:AT1G61010; -.
DR Araport; AT1G61010; -.
DR TAIR; locus:2206076; AT1G61010.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q9C952; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR PhylomeDB; Q9C952; -.
DR PRO; PR:Q9C952; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C952; baseline and differential.
DR Genevisible; Q9C952; AT.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0016180; P:snRNA processing; IMP:TAIR.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 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..693
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 3-I"
FT /id="PRO_0000391780"
FT MOTIF 81..86
FT /note="HXHXDH motif"
FT CONFLICT 651
FT /note="G -> S (in Ref. 4; AAL66977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77365 MW; D225E47A675ACB1C CRC64;
MASSSTSLKR REQPISRDGD QLIVTPLGAG SEVGRSCVYM SFRGKNILFD CGIHPAYSGM
AALPYFDEID PSSIDVLLIT HFHIDHAASL PYFLEKTTFN GRVFMTHATK AIYKLLLTDY
VKVSKVSVED MLFDEQDINK SMDKIEVIDF HQTVEVNGIK FWCYTAGHVL GAAMFMVDIA
GVRILYTGDY SREEDRHLRA AELPQFSPDI CIIESTSGVQ LHQSRHIREK RFTDVIHSTV
AQGGRVLIPA FALGRAQELL LILDEYWANH PDLHNIPIYY ASPLAKKCMA VYQTYILSMN
DRIRNQFANS NPFVFKHISP LNSIDDFNDV GPSVVMATPG GLQSGLSRQL FDSWCSDKKN
ACIIPGYMVE GTLAKTIINE PKEVTLMNGL TAPLNMQVHY ISFSAHADYA QTSTFLKELM
PPNIILVHGE ANEMMRLKQK LLTEFPDGNT KIMTPKNCES VEMYFNSEKL AKTIGRLAEK
TPDVGDTVSG ILVKKGFTYQ IMAPDELHVF SQLSTATVTQ RITIPFVGAF GVIKHRLEKI
FESVEFSTDE ESGLPALKVH ERVTVKQESE KHISLQWSSD PISDMVSDSI VALILNISRE
VPKIVMEEED AVKSEEENGK KVEKVIYALL VSLFGDVKLG ENGKLVIRVD GNVAQLDKES
GEVESEHSGL KERVRVAFER IQSAVKPIPL SAS
