PABP_PHANO
ID PABP_PHANO Reviewed; 744 AA.
AC Q0U1G2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 25-MAY-2022, entry version 80.
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=SNOG_14351;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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}.
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DR EMBL; CH445355; EAT78222.2; -; Genomic_DNA.
DR RefSeq; XP_001804541.1; XM_001804489.1.
DR AlphaFoldDB; Q0U1G2; -.
DR SMR; Q0U1G2; -.
DR STRING; 13684.SNOT_14351; -.
DR PRIDE; Q0U1G2; -.
DR EnsemblFungi; SNOT_14351; SNOT_14351; SNOG_14351.
DR GeneID; 5981465; -.
DR KEGG; pno:SNOG_14351; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q0U1G2; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..744
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295397"
FT DOMAIN 48..126
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 136..213
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 229..306
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 332..462
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 647..724
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 81007 MW; E046C53B6663B36E CRC64;
MSEVANSTSP VQDGADANGA QINTNVPAAS GDAPTPTTAA QQAHQNSASL YVGELDPSVT
EAMLFELFSS IGQVASIRVC RDAVTRRSLG YAYVNYNSSE DGEKALEELN YTVIKGKPCR
IMWSQRDPAL RKTGQGNVFI KNLDHAIDNK ALHDTFAAFG NILSCKVAQD ELGNSKGYGF
VHYETAEAAN NAIKHVNGML LNEKKVFVGH HIPKKERMSK FEEMKANFTN IYVKNIDLDV
TDEDFRELFE KHGDITSASI ARDDQGKSRG FGFVNYIRHE AAAVAVDHLN DIEFKGQKLY
VGRAQKKHER EEELRKQYEA ARLEKQSKYQ GVNLYIKNLN DDVDDEKLRD MFTPFGTITS
AKVILRDEEK KDEEEKEVKE EKKEDEKKED EEAKEGSSSE QNGEDTKAGD KVTIKGEKKI
LGKSKGFGFV CFSNPDEATK AVTEMNQKMI EGKPLYVALA QRKDVRKNQL EATIQARNQL
RMQQQQQQQF GGIPQMFIAP GQQPMMYPPG ARGQMPFPAG MPGAQGGRGA GFPGGMPGQQ
GGRGGPNAQQ MPPMYMPPGM APGAFPPGPY MNQQYMQLAQ AAQQAMGGRG GRGGPMPGMP
GMPQAQIAGG PGIRGGQGGF PQGGRGAPGG RGQPPMPGFP QGGRPGGPGV DMSVLSAAAP
GQQKQMLGEA LYPKIHEMQP ELAGKITGML LEMDNSELIN LTADESALRA KVDEAMSVYD
EYVKNKEGDG EKEAPKEESK EEKA
