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Polyadenylate-binding protein, cytoplasmic and nuclear (PABP) (Poly(A)-binding protein) (Polyadenylate tail-binding protein)

 PABP_SCHPO              Reviewed;         653 AA.
P31209; P87135;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
28-FEB-2018, entry version 148.
RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
Short=PABP;
Short=Poly(A)-binding protein;
AltName: Full=Polyadenylate tail-binding protein;
Name=pab1; Synonyms=pabp; ORFNames=SPAC57A7.04c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-628.
PubMed=1675426; DOI=10.1128/MCB.11.7.3419;
Burd C.G., Matunis E.L., Dreyfuss G.;
"The multiple RNA-binding domains of the mRNA poly(A)-binding protein
have different RNA-binding activities.";
Mol. Cell. Biol. 11:3419-3424(1991).
[3]
INTERACTION WITH CID13.
PubMed=12062100; DOI=10.1016/S0092-8674(02)00753-5;
Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III,
Russell P.;
"Cid13 is a cytoplasmic poly(A) polymerase that regulates
ribonucleotide reductase mRNA.";
Cell 109:563-573(2002).
[4]
FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
PubMed=12112233; DOI=10.1002/yea.876;
Thakurta A.G., Ho Yoon J., Dhar R.;
"Schizosaccharomyces pombe spPABP, a homologue of Saccharomyces
cerevisiae Pab1p, is a non-essential, shuttling protein that
facilitates mRNA export.";
Yeast 19:803-810(2002).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(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. In the nucleus,
involved in both mRNA cleavage and polyadenylation. Is also
required for efficient mRNA export to the cytoplasm. Acts in
concert with a poly(A)-specific nuclease (PAN) to affect poly(A)
tail shortening, which may occur concomitantly with either
nucleocytoplasmic mRNA transport or translational initiation. In
the cytoplasm, stimulates translation initiation and regulates
mRNA decay through translation termination-coupled poly(A)
shortening, probably mediated by PAN (By similarity).
{ECO:0000250, ECO:0000269|PubMed:12112233}.
-!- SUBUNIT: Interacts with cid13. {ECO:0000269|PubMed:12062100}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35320.1; Type=Frameshift; Positions=518, 526; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; CU329670; CAB08762.1; -; Genomic_DNA.
EMBL; M64603; AAA35320.1; ALT_FRAME; mRNA.
PIR; T38950; DNZPPA.
RefSeq; NP_593377.1; NM_001018809.2.
ProteinModelPortal; P31209; -.
SMR; P31209; -.
BioGrid; 278007; 17.
IntAct; P31209; 1.
STRING; 4896.SPAC57A7.04c.1; -.
iPTMnet; P31209; -.
MaxQB; P31209; -.
PaxDb; P31209; -.
PRIDE; P31209; -.
EnsemblFungi; SPAC57A7.04c.1; SPAC57A7.04c.1:pep; SPAC57A7.04c.
GeneID; 2541505; -.
KEGG; spo:SPAC57A7.04c; -.
EuPathDB; FungiDB:SPAC57A7.04c; -.
PomBase; SPAC57A7.04c; -.
HOGENOM; HOG000217922; -.
InParanoid; P31209; -.
KO; K13126; -.
OMA; KKVYVGH; -.
OrthoDB; EOG092C3SCB; -.
PhylomeDB; P31209; -.
Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SPO-72649; Translation initiation complex formation.
Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:P31209; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
GO; GO:0008143; F:poly(A) binding; TAS:PomBase.
GO; GO:0006406; P:mRNA export from nucleus; IMP:PomBase.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
Gene3D; 3.30.70.330; -; 4.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
1: Evidence at protein level;
Complete proteome; Cytoplasm; mRNA processing; mRNA transport;
Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
Translation regulation; Transport.
CHAIN 1 653 Polyadenylate-binding protein,
cytoplasmic and nuclear.
/FTId=PRO_0000081718.
DOMAIN 80 158 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 168 245 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 261 338 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 364 441 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 569 646 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
COMPBIAS 481 569 Pro-rich.
MOD_RES 167 167 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
CONFLICT 1 34 MPSTDLKKQADAAVESDVNTNNEAVESSTKEESS -> MSL
ENSSTLSLCSNNTTHFW (in Ref. 2; AAA35320).
{ECO:0000305}.
CONFLICT 349 349 R -> A (in Ref. 2; AAA35320).
{ECO:0000305}.
SEQUENCE 653 AA; 71513 MW; 7F8F5CAD69D0CFE1 CRC64;
MPSTDLKKQA DAAVESDVNT NNEAVESSTK EESSNTPSTE TQPEKKAEEP EAAAEPSEST
STPTNASSVA TPSGTAPTSA SLYVGELDPS VTEAMLFELF NSIGPVASIR VCRDAVTRRS
LGYAYVNFHN MEDGEKALDE LNYTLIKGRP CRIMWSQRDP SLRKMGTGNV FIKNLDPAID
NKALHDTFSA FGKILSCKVA VDELGNAKGY GFVHFDSVES ANAAIEHVNG MLLNDKKVYV
GHHVSRRERQ SKVEALKANF TNVYIKNLDT EITEQEFSDL FGQFGEITSL SLVKDQNDKP
RGFGFVNYAN HECAQKAVDE LNDKEYKGKK LYVGRAQKKH EREEELRKRY EQMKLEKMNK
YQGVNLFIKN LQDEVDDERL KAEFSAFGTI TSAKIMTDEQ GKSKGFGFVC YTTPEEANKA
VTEMNQRMLA GKPLYVALAQ RKEVRRSQLE AQIQARNQFR LQQQVAAAAG IPAVQYGATG
PLIYGPGGYP IPAAVNGRGM PMVPGHNGPM PMYPGMPTQF PAGGPAPGYP GMNARGPVPA
QGRPMMMPGS VPSAGPAEAE AVPAVPGMPE RFTAADLAAV PEESRKQVLG ELLYPKVFVR
EEKLSGKITG MLLEMPNSEL LELLEDDSAL NERVNEAIGV LQEFVDQEPG FTE


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