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Polyadenylate-binding protein 5 (PABP-5) (Poly(A)-binding protein 5)

 PABP5_ARATH             Reviewed;         682 AA.
Q05196; Q9M9G9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
25-OCT-2017, entry version 136.
RecName: Full=Polyadenylate-binding protein 5;
Short=PABP-5;
Short=Poly(A)-binding protein 5;
Name=PAB5; OrderedLocusNames=At1g71770; ORFNames=F14O23.15;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=8341686; DOI=10.1073/pnas.90.14.6686;
Belostotsky D.A., Meagher R.B.;
"Differential organ-specific expression of three poly(A)-binding-
protein genes from Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 90:6686-6690(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-682.
STRAIN=cv. Columbia;
PubMed=14993207; DOI=10.1101/gr.1515604;
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G.,
Caboche M., Weissenbach J., Salanoubat M.;
"Whole genome sequence comparisons and 'full-length' cDNA sequences: a
combined approach to evaluate and improve Arabidopsis genome
annotation.";
Genome Res. 14:406-413(2004).
[5]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=8776896; DOI=10.1105/tpc.8.8.1261;
Belostotsky D.A., Meagher R.B.;
"A pollen-, ovule-, and early embryo-specific poly(A) binding protein
from Arabidopsis complements essential functions in yeast.";
Plant Cell 8:1261-1275(1996).
[6]
GENE FAMILY.
PubMed=12586718;
Belostotsky D.A.;
"Unexpected complexity of poly(A)-binding protein gene families in
flowering plants: three conserved lineages that are at least 200
million years old and possible auto- and cross-regulation.";
Genetics 163:311-319(2003).
[7]
TISSUE SPECIFICITY.
PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
"Four distinct classes of proteins as interaction partners of the PABC
domain of Arabidopsis thaliana Poly(A)-binding proteins.";
Mol. Genet. Genomics 272:651-665(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
-!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an
important mediator of the multiple roles of the poly(A) tail in
mRNA biogenesis, stability and translation.
{ECO:0000269|PubMed:8341686, ECO:0000269|PubMed:8776896}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed predominantly in immature flowers
but also at lower levels in mature flowers and siliques. Detected
in tapetum, pollen, ovules and developing seeds. Also detected in
primary inflorescences and immature siliques.
{ECO:0000269|PubMed:15650869, ECO:0000269|PubMed:8341686,
ECO:0000269|PubMed:8776896}.
-!- MISCELLANEOUS: A.thaliana contains 8 PABP genes.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA32832.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF43230.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BX818355; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; M97657; AAA32832.1; ALT_INIT; Genomic_DNA.
EMBL; AC012654; AAF43230.1; ALT_INIT; Genomic_DNA.
EMBL; CP002684; AEE35230.1; -; Genomic_DNA.
EMBL; CP002684; AEE35231.1; -; Genomic_DNA.
EMBL; BX818355; -; NOT_ANNOTATED_CDS; mRNA.
PIR; B96740; B96740.
RefSeq; NP_001185373.1; NM_001198444.1.
RefSeq; NP_177322.2; NM_105835.2.
UniGene; At.50027; -.
UniGene; At.52482; -.
ProteinModelPortal; Q05196; -.
SMR; Q05196; -.
BioGrid; 28727; 6.
IntAct; Q05196; 5.
STRING; 3702.AT1G71770.1; -.
iPTMnet; Q05196; -.
PaxDb; Q05196; -.
PRIDE; Q05196; -.
EnsemblPlants; AT1G71770.1; AT1G71770.1; AT1G71770.
EnsemblPlants; AT1G71770.2; AT1G71770.2; AT1G71770.
GeneID; 843507; -.
Gramene; AT1G71770.1; AT1G71770.1; AT1G71770.
Gramene; AT1G71770.2; AT1G71770.2; AT1G71770.
KEGG; ath:AT1G71770; -.
Araport; AT1G71770; -.
TAIR; locus:2013011; AT1G71770.
eggNOG; KOG0123; Eukaryota.
eggNOG; ENOG410XR5X; LUCA.
HOGENOM; HOG000217922; -.
InParanoid; Q05196; -.
KO; K13126; -.
OMA; PLRIMWS; -.
OrthoDB; EOG093606N5; -.
PhylomeDB; Q05196; -.
Reactome; R-ATH-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-ATH-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-ATH-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:Q05196; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q05196; baseline and differential.
Genevisible; Q05196; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0008143; F:poly(A) binding; IDA:TAIR.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IGI:TAIR.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0006413; P:translational initiation; IGI:TAIR.
InterPro; IPR036053; PABP-dom.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 4.
SUPFAM; SSF54928; SSF54928; 2.
SUPFAM; SSF63570; SSF63570; 2.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Translation regulation.
CHAIN 1 682 Polyadenylate-binding protein 5.
/FTId=PRO_0000081716.
DOMAIN 59 136 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 146 223 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 239 316 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 342 419 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 588 665 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
COMPBIAS 2 52 Ala-rich.
COMPBIAS 528 535 Poly-Gln.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:18433157}.
CONFLICT 624 624 A -> P (in Ref. 1; AAA32832).
{ECO:0000305}.
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


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