PABP3_ARATH
ID PABP3_ARATH Reviewed; 660 AA.
AC O64380; O80546; Q9FYS4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Polyadenylate-binding protein 3;
DE Short=PABP-3;
DE Short=Poly(A)-binding protein 3;
GN Name=PAB3; OrderedLocusNames=At1g22760; ORFNames=T22J18.7;
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], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11516954; DOI=10.1016/s0960-9822(01)00371-2;
RA Chekanova J.A., Shaw R.J., Belostotsky D.A.;
RT "Analysis of an essential requirement for the poly(A) binding protein
RT function using cross-species complementation.";
RL Curr. Biol. 11:1207-1214(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9369203; DOI=10.1016/s0014-5793(97)01190-3;
RA Terryn N., Neyt P., de Clercq R., de Keyser A., van den Daele H.,
RA Ardiles W., Dehais P., Rouze P., Gielen J., Villarroel R., van Montagu M.;
RT "Sequence analysis of a 24-kb contiguous genomic region at the Arabidopsis
RT thaliana PFL locus on chromosome 1.";
RL FEBS Lett. 416:156-160(1997).
RN [3]
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 [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;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=8341686; DOI=10.1073/pnas.90.14.6686;
RA Belostotsky D.A., Meagher R.B.;
RT "Differential organ-specific expression of three poly(A)-binding-protein
RT genes from Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6686-6690(1993).
RN [7]
RP FUNCTION.
RX PubMed=10930416; DOI=10.1074/jbc.m005493200;
RA Chekanova J.A., Shaw R.J., Wills M.A., Belostotsky D.A.;
RT "Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana
RT rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6
RT mutant and is found in an exosome-sized complex in plant and yeast cells.";
RL J. Biol. Chem. 275:33158-33166(2000).
RN [8]
RP GENE FAMILY, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12586718; DOI=10.1093/genetics/163.1.311;
RA Belostotsky D.A.;
RT "Unexpected complexity of poly(A)-binding protein gene families in
RT flowering plants: three conserved lineages that are at least 200 million
RT years old and possible auto- and cross-regulation.";
RL Genetics 163:311-319(2003).
RN [9]
RP FUNCTION.
RX PubMed=14624004; DOI=10.1261/rna.5128903;
RA Chekanova J.A., Belostotsky D.A.;
RT "Evidence that poly(A) binding protein has an evolutionarily conserved
RT function in facilitating mRNA biogenesis and export.";
RL RNA 9:1476-1490(2003).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
RA Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
RT "Four distinct classes of proteins as interaction partners of the PABC
RT domain of Arabidopsis thaliana Poly(A)-binding proteins.";
RL Mol. Genet. Genomics 272:651-665(2005).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important
CC mediator of the multiple roles of the poly(A) tail in mRNA biogenesis,
CC stability and translation. In the cytoplasm, affects both translation
CC and mRNA decay. Inhibits the polyadenylated RNA degradation by the
CC Rrp41p 3'-->5' exonuclease in vitro. Binds with the 5'UTRs of PAB2,
CC PAB3 and with a lower affinity with the 5'UTR of PAB5.
CC {ECO:0000269|PubMed:10930416, ECO:0000269|PubMed:11516954,
CC ECO:0000269|PubMed:12586718, ECO:0000269|PubMed:14624004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in immature flowers.
CC Detected in tapetum and pollen. Strongly expressed in immatures
CC siliques. {ECO:0000269|PubMed:12586718, ECO:0000269|PubMed:15650869,
CC ECO:0000269|PubMed:8341686}.
CC -!- MISCELLANEOUS: A.thaliana contains 8 PABP genes.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; AF293840; AAG02117.1; -; mRNA.
DR EMBL; Y12227; CAA72907.1; -; Genomic_DNA.
DR EMBL; AC003979; AAC25510.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30284.1; -; Genomic_DNA.
DR EMBL; AY054490; AAK96681.1; -; mRNA.
DR PIR; T00768; T00768.
DR RefSeq; NP_173690.1; NM_102123.4.
DR AlphaFoldDB; O64380; -.
DR SMR; O64380; -.
DR BioGRID; 24121; 8.
DR STRING; 3702.AT1G22760.1; -.
DR PaxDb; O64380; -.
DR PRIDE; O64380; -.
DR ProteomicsDB; 236320; -.
DR EnsemblPlants; AT1G22760.1; AT1G22760.1; AT1G22760.
DR GeneID; 838882; -.
DR Gramene; AT1G22760.1; AT1G22760.1; AT1G22760.
DR KEGG; ath:AT1G22760; -.
DR Araport; AT1G22760; -.
DR TAIR; locus:2199700; AT1G22760.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; O64380; -.
DR OMA; CRDQNRR; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; O64380; -.
DR PRO; PR:O64380; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64380; baseline and differential.
DR Genevisible; O64380; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IGI:TAIR.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nonsense-mediated mRNA decay; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..660
FT /note="Polyadenylate-binding protein 3"
FT /id="PRO_0000081715"
FT DOMAIN 49..126
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 136..213
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 229..306
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 332..409
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 571..648
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT CONFLICT 418..422
FT /note="Missing (in Ref. 3; AAC25510)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="P -> S (in Ref. 1; AAG02117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 72873 MW; D4B14E8E4DBE502F CRC64;
MAAAVATGVA PATMVDQVPS PTAQTSVQVP VSIPLPSPVV VADQTHPNSS LYAGDLDPKV
TEAHLFDLFK HVANVVSVRV CRDQNRRSLG YAYINFSNPN DAYRAMEALN YTPLFDRPIR
IMLSNRDPST RLSGKGNIFI KNLDASIDNK ALFETFSSFG TILSCKVAMD VTGRSKGYGF
VQFEKEESAQ AAIDKLNGML MNDKQVFVGH FIRRQERARD ENTPTPRFTN VYVKNLPKEI
GEDELRKTFG KFGVISSAVV MRDQSGNSRC FGFVNFECTE AAASAVEKMN GISLGDDVLY
VGRAQKKSER EEELRRKFEQ ERINRFEKSQ GANLYLKNLD DSVDDEKLKE MFSEYGNVTS
SKVMLNPQGM SRGFGFVAYS NPEEALRALS EMNGKMIGRK PLYIALAQRK EDRRAHLQAL
FSQIRAPGPM SGFHHPPGGP MPGPPQHMYV GQNGASMVPS QPIGYGFQPQ FMPGMRPGSG
PGNFIVPYPL QRQPQTGPRM GFRRGATNVQ QHIQQQQLMH RNPSPGMRYM NGASNGRNGM
DSSVPQGILP PIIPLPIDAS SISHQKAPLL PISKLTSSLA SASPADRTRM LGEQLYPLVE
RHEPLHVAKV TGMLLEMDQA EILHLMESPE ALKSKVSEAL DVLRLSVDPT DHDLGFSTTD
