PABP5_ARATH
ID PABP5_ARATH Reviewed; 682 AA.
AC Q05196; Q9M9G9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Polyadenylate-binding protein 5;
DE Short=PABP-5;
DE Short=Poly(A)-binding protein 5;
GN Name=PAB5; OrderedLocusNames=At1g71770; ORFNames=F14O23.15;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. Columbia;
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 [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] OF 540-682.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=8776896; DOI=10.2307/3870300;
RA Belostotsky D.A., Meagher R.B.;
RT "A pollen-, ovule-, and early embryo-specific poly(A) binding protein from
RT Arabidopsis complements essential functions in yeast.";
RL Plant Cell 8:1261-1275(1996).
RN [6]
RP GENE FAMILY.
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 [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
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. {ECO:0000269|PubMed:8341686,
CC ECO:0000269|PubMed:8776896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in immature flowers but
CC also at lower levels in mature flowers and siliques. Detected in
CC tapetum, pollen, ovules and developing seeds. Also detected in primary
CC inflorescences and immature siliques. {ECO:0000269|PubMed:15650869,
CC ECO:0000269|PubMed:8341686, ECO:0000269|PubMed:8776896}.
CC -!- MISCELLANEOUS: A.thaliana contains 8 PABP genes.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32832.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF43230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BX818355; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; M97657; AAA32832.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC012654; AAF43230.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35230.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35231.1; -; Genomic_DNA.
DR EMBL; BX818355; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B96740; B96740.
DR RefSeq; NP_001185373.1; NM_001198444.1.
DR RefSeq; NP_177322.2; NM_105835.2.
DR AlphaFoldDB; Q05196; -.
DR SMR; Q05196; -.
DR BioGRID; 28727; 9.
DR IntAct; Q05196; 5.
DR STRING; 3702.AT1G71770.1; -.
DR iPTMnet; Q05196; -.
DR PaxDb; Q05196; -.
DR PRIDE; Q05196; -.
DR ProteomicsDB; 248631; -.
DR EnsemblPlants; AT1G71770.1; AT1G71770.1; AT1G71770.
DR EnsemblPlants; AT1G71770.2; AT1G71770.2; AT1G71770.
DR GeneID; 843507; -.
DR Gramene; AT1G71770.1; AT1G71770.1; AT1G71770.
DR Gramene; AT1G71770.2; AT1G71770.2; AT1G71770.
DR KEGG; ath:AT1G71770; -.
DR Araport; AT1G71770; -.
DR TAIR; locus:2013011; AT1G71770.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q05196; -.
DR OMA; HNESLKA; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; Q05196; -.
DR PRO; PR:Q05196; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q05196; baseline and differential.
DR Genevisible; Q05196; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:TAIR.
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:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IGI:TAIR.
DR GO; GO:0006413; P:translational initiation; IGI:TAIR.
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; 4.
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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Translation regulation.
FT CHAIN 1..682
FT /note="Polyadenylate-binding protein 5"
FT /id="PRO_0000081716"
FT DOMAIN 59..136
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 146..223
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 239..316
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 342..419
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 588..665
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 624
FT /note="A -> P (in Ref. 1; AAA32832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 74423 MW; 3D0AA61682B8B91D CRC64;
MAAAVASGIA PTTAMVDQVI PNQPTVAAAA PPPFPAVSQV AAVAAAAAAA EALQTHPNSS
LYVGDLDPSV NESHLLDLFN QVAPVHNLRV CRDLTHRSLG YAYVNFANPE DASRAMESLN
YAPIRDRPIR IMLSNRDPST RLSGKGNVFI KNLDASIDNK ALYETFSSFG TILSCKVAMD
VVGRSKGYGF VQFEKEETAQ AAIDKLNGML LNDKQVFVGH FVRRQDRARS ESGAVPSFTN
VYVKNLPKEI TDDELKKTFG KYGDISSAVV MKDQSGNSRS FGFVNFVSPE AAAVAVEKMN
GISLGEDVLY VGRAQKKSDR EEELRRKFEQ ERISRFEKLQ GSNLYLKNLD DSVNDEKLKE
MFSEYGNVTS CKVMMNSQGL SRGFGFVAYS NPEEALLAMK EMNGKMIGRK PLYVALAQRK
EERQAHLQSL FTQIRSPGTM SPVPSPMSGF HHHPPGGPMS GPHHPMFIGH NGQGLVPSQP
MGYGYQVQFM PGMRPGAGPP NFMMPFPLQR QTQPGPRVGF RRGANNMQQQ FQQQQMLQQN
ASRFMGGAGN RRNGMEASAP QGIIPLPLNA SANSHNAPQR SHKPTPLTIS KLASDLALAS
PDKHPRMLGD HLYPLVEQQE PANAAKVTGM LLEMDQAEIL HLLESPEALK AKVSEALDVL
RRSADPAAVS SVDDQFALSS SE
