(data stored in ACNUC7421 zone)

SWISSPROT: PABP_ASPNC

ID   PABP_ASPNC              Reviewed;         731 AA.
AC   A2Q848;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 70.
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; ORFNames=An01g03050;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC       {ECO:0000305}.
DR   EMBL; AM269955; CAK43671.1; -; Genomic_DNA.
DR   SMR; A2Q848; -.
DR   PaxDb; A2Q848; -.
DR   PRIDE; A2Q848; -.
DR   EnsemblFungi; CAK43671; CAK43671; An01g03050.
DR   HOGENOM; HOG000217922; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
DR   GO; GO:0008143; F:poly(A) binding; IEA:EnsemblFungi.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:1901918; P:negative regulation of exoribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR   GO; GO:1901919; P:positive regulation of exoribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 3.
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; IPR000504; RRM_dom.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   SUPFAM; SSF63570; SSF63570; 1.
DR   TIGRFAMs; TIGR01628; PABP-1234; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   3: Inferred from homology;
DR   PRODOM; A2Q848.
DR   SWISS-2DPAGE; A2Q848.
KW   Cytoplasm; mRNA processing; mRNA transport; Nucleus; Repeat; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN           1..731
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295381"
FT   DOMAIN          54..132
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          142..219
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          235..312
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          338..472
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          658..731
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   COMPBIAS        495..499
FT                   /note="Poly-Ala"
FT   COMPBIAS        513..660
FT                   /note="Gly-rich"
SQ   SEQUENCE   731 AA;  78884 MW;  914288ADFC6C4B2E CRC64;
     MSADVSTTPA AENVNGAAEA SPAPAAAAPS ATTPEVTAVE NSTPAPAANQ PHSASLYVGE
     LDPSVTEAML YELFSSIGQV ASIRVCRDAV TRRSLGYAYV NYNNTADGER ALEDLNYTLI
     KGKPCRIMWS QRDPALRKTG QGNVFIKNLD SAIDNKALHD TFAAFGNILS CKVAQDEFGN
     SKGYGFVHYE TAEAANNAIK HVNGMLLNDK KVFVGHHISK KDRQSKFEEM KANFTNVYIK
     NLDSEIDDDE FRKMFEKFGE ITSATLSRDQ EGKSRGFGFV NFSTHESAQA AVEEMNDKEI
     RSQKLYVGRA QKKHEREEEL RKQYEAARLE KASKYQGVNL YVKNLTDDID DEKLRELFGP
     YGTITSAKVM RDTNVERDQS PDSAGKEKEA DKENDKEATP EAEKAEKAEE KPSESSEEKD
     KEAKKSDKKP FGKSKGFGFV CFSSPDEASK AVTEMNQRMV NGKPLYVALA QRKDVRRSQL
     EASIQARNTI RQQQAAAAAG MPQPYMQPAV FYGPGQQGFI PGGQRGMAFP PQPGMVMGIP
     GGRPGQYPGP FPGQQGGRGM GPNQQIPPNF AQGIPMGMQG PGGIPNGMGY PQMAQVQFGR
     GAGGRGQVPG MPMGQGMRGG PGYGQGRGAP VQQGQMRPGQ GGRGQNAAAP AGPQEGAAGG
     VNAQTLGAAP PAQQKQMLGE ALYPKIQAQQ PELAGKITGM LLEMDNTELL SLTRKPCAPR
     SMRPLAFTMS T
//

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