ID   PABP_NEUCR              Reviewed;         764 AA.
AC   Q7S6N6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 122.
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=pabp-1; Synonyms=pab1; ORFNames=NCU04799;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
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DR   EMBL; CM002241; EAA31189.1; -; Genomic_DNA.
DR   RefSeq; XP_960425.1; XM_955332.3.
DR   AlphaFoldDB; Q7S6N6; -.
DR   SMR; Q7S6N6; -.
DR   STRING; 5141.EFNCRP00000004477; -.
DR   EnsemblFungi; EAA31189; EAA31189; NCU04799.
DR   GeneID; 3876563; -.
DR   KEGG; ncr:NCU04799; -.
DR   VEuPathDB; FungiDB:NCU04799; -.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   InParanoid; Q7S6N6; -.
DR   OMA; ASPMEQK; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 3.
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;
KW   Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..764
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295396"
FT   DOMAIN          60..138
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          148..225
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          241..318
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          344..462
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          657..734
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   REGION          36..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  82317 MW;  44E2BD4A9169A572 CRC64;
     MAATSTAAVD QLAADLGNTS LDNKAAAPAP IDTSAVPEAQ AEGAEAAPTP TAAPHPQASA
     SLYVGELDPS VTEAMLFELF SQIGSVASIR VCRDAVTRRS LGYAYVNYNT TADGEKALEE
     LNYTLIKGRP CRIMWSQRDP ALRKTGAGNI FIKNLDAAID NKALHDTFAA FGNILSCKVA
     QDEHGNSKGY GFVHYETDEA ASQAIKHVNG MLLNEKKVYV GHHIPKKDRQ SKFEEMKANF
     TNVYVKNINN EVTDEEFREL FAKFGEVTSS SLARDQEGKS RGFGFVNFTT HEAAAQAVDE
     LNGKDFRGQD LYVGRAQKKH EREEELRKSY EAARLEKANK YQGVNLYIKN LGDDVDDDKL
     RAMFSEYGPI TSAKVMRDSL IEGSEEKDEK DKENKKEGET KEEEQNEGSE KKTEKKGDRK
     LGKSKGFGFV CFSNPDDATK AVTEMNQRMV DGKPLYVALA QRKDVRKSQL EASIQARNQL
     RMQQAAAQAG MPQQYMQAPV YYAGQQPGFM PAPGGRGVPF PQGGIVPGVQ GGRPGQYPYQ
     QGGRGGVPPQ QMPPMGYPIN QFGPGAFPPN TPQYMAAMGQ VGALGGGRGG PAGRGPQGIP
     AGIPQGLQGG PAVPGYPPAG RPQNGGGRGT PRGNANFMAA GRGASPIPGA PADLSAGSFL
     QAQLATTQDP QAQKQIIGEN LFPKIQAIQP ALAGKITGML LEMDNAELIN LFEDDNALNV
     KVQEALAVYD EYLKTQGQQP TQQPAEANGE QPKAEEQKPE EQKA