PABP_MAGO7
ID PABP_MAGO7 Reviewed; 762 AA.
AC A4QUF0; G4N1R5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=MGG_09505;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001233; EHA52430.1; -; Genomic_DNA.
DR RefSeq; XP_003712237.1; XM_003712189.1.
DR AlphaFoldDB; A4QUF0; -.
DR SMR; A4QUF0; -.
DR STRING; 318829.MGG_09505T0; -.
DR EnsemblFungi; MGG_09505T0; MGG_09505T0; MGG_09505.
DR GeneID; 2680542; -.
DR KEGG; mgr:MGG_09505; -.
DR VEuPathDB; FungiDB:MGG_09505; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; A4QUF0; -.
DR OMA; ASPMEQK; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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..762
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295394"
FT DOMAIN 61..139
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 149..226
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 242..320
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 346..470
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 664..741
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 39..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 81934 MW; 4E1B393FB764A040 CRC64;
MAAPSNTAAV DQLTSDLANA NMNGGEKTTV NTNVGASFTG EEIDTAGPTP SSAAPHPQAS
ASLYVGELDP SVTEAMLFEL FSQIGSVASI RVCRDAVTRR SLGYAYVNYN TTADGEKALE
ELNYTLIKGR PCRIMWSQRD PALRKTGQGN VFIKNLDVAI DNKALHDTFA AFGNILSCKV
AQDENGNSKG YGFVHYETDE AASQAIKHVN GMLLNEKKVY VGHHIPKKDR QSKFDEMKAN
FTNIYVKNIN PEVTDDEFRT LFEKYGDVTS SSLARDQETG KSRGFGFVNF TSHEDASKAV
QELNEKEFHG QNLYVGRAQK KHEREEELRK SYEAARQEKA SKYQGVNLYI KNLDDEVDDE
KLRQLFSEFG PITSAKVMRD SITEPGEEGE SKEGEESEKN KENKPEEKEG DDSKPEEKEG
EDSKSKSKLG KSKGFGFVCF ANPDDATKAV AEMNQRMVNN KPLYVALAQR KDVRKNQLEQ
SIQARNQLRM QQAAAAAGMP QQYMQAPVFY GPGSQPGFMP PAGGRGMPYP QGGMPMQPGR
PGQFPAGFAA QQGGRGAMPQ GIPPMYGLPG QFPPQGPFPQ PNNPQFLAAM QQIQQSALAG
GRGGPAGRGP MQGGVPVPGM PGGAGLPGFP PNARQQGPGA GRGAAAGRAP AGAPAGARGA
GAPEGLQGQL AAVADNPGQQ KQILGEAIFP KIQAIHPELA GKITGMLLEM DNTELVALVE
NDGALRSKVD EALAVYDDYV RQQGDGEGAQ APSKEEKTEE KA
