PABP_SCHPO
ID PABP_SCHPO Reviewed; 653 AA.
AC P31209; P87135;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear;
DE Short=PABP;
DE Short=Poly(A)-binding protein;
DE AltName: Full=Polyadenylate tail-binding protein;
GN Name=pab1; Synonyms=pabp; ORFNames=SPAC57A7.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-628.
RX PubMed=1675426; DOI=10.1128/mcb.11.7.3419-3424.1991;
RA Burd C.G., Matunis E.L., Dreyfuss G.;
RT "The multiple RNA-binding domains of the mRNA poly(A)-binding protein have
RT different RNA-binding activities.";
RL Mol. Cell. Biol. 11:3419-3424(1991).
RN [3]
RP INTERACTION WITH CID13.
RX PubMed=12062100; DOI=10.1016/s0092-8674(02)00753-5;
RA Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III,
RA Russell P.;
RT "Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide
RT reductase mRNA.";
RL Cell 109:563-573(2002).
RN [4]
RP FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
RX PubMed=12112233; DOI=10.1002/yea.876;
RA Thakurta A.G., Ho Yoon J., Dhar R.;
RT "Schizosaccharomyces pombe spPABP, a homologue of Saccharomyces cerevisiae
RT Pab1p, is a non-essential, shuttling protein that facilitates mRNA
RT export.";
RL Yeast 19:803-810(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(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. In the nucleus, involved in both mRNA
CC cleavage and polyadenylation. Is also required for efficient mRNA
CC export to the cytoplasm. Acts in concert with a poly(A)-specific
CC nuclease (PAN) to affect poly(A) tail shortening, which may occur
CC concomitantly with either nucleocytoplasmic mRNA transport or
CC translational initiation. In the cytoplasm, stimulates translation
CC initiation and regulates mRNA decay through translation termination-
CC coupled poly(A) shortening, probably mediated by PAN (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12112233}.
CC -!- SUBUNIT: Interacts with cid13. {ECO:0000269|PubMed:12062100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35320.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB08762.1; -; Genomic_DNA.
DR EMBL; M64603; AAA35320.1; ALT_FRAME; mRNA.
DR PIR; T38950; DNZPPA.
DR RefSeq; NP_593377.1; NM_001018809.2.
DR AlphaFoldDB; P31209; -.
DR SMR; P31209; -.
DR BioGRID; 278007; 25.
DR IntAct; P31209; 1.
DR STRING; 4896.SPAC57A7.04c.1; -.
DR iPTMnet; P31209; -.
DR MaxQB; P31209; -.
DR PaxDb; P31209; -.
DR PRIDE; P31209; -.
DR EnsemblFungi; SPAC57A7.04c.1; SPAC57A7.04c.1:pep; SPAC57A7.04c.
DR GeneID; 2541505; -.
DR KEGG; spo:SPAC57A7.04c; -.
DR PomBase; SPAC57A7.04c; -.
DR VEuPathDB; FungiDB:SPAC57A7.04c; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; P31209; -.
DR OMA; ASPMEQK; -.
DR PhylomeDB; P31209; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P31209; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
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:PomBase.
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:0031124; P:mRNA 3'-end processing; ISO:PomBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
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; mRNA processing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..653
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000081718"
FT DOMAIN 80..158
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 168..245
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 261..338
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 364..441
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 569..646
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 1..34
FT /note="MPSTDLKKQADAAVESDVNTNNEAVESSTKEESS -> MSLENSSTLSLCSN
FT NTTHFW (in Ref. 2; AAA35320)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="R -> A (in Ref. 2; AAA35320)"
FT /evidence="ECO:0000305"
SQ 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
