PABP_ASPOR
ID PABP_ASPOR Reviewed; 765 AA.
AC Q2UK72;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=AO090003000927;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007155; BAE58043.1; -; Genomic_DNA.
DR RefSeq; XP_001820045.1; XM_001819993.2.
DR RefSeq; XP_003189588.1; XM_003189540.1.
DR AlphaFoldDB; Q2UK72; -.
DR SMR; Q2UK72; -.
DR STRING; 510516.Q2UK72; -.
DR PRIDE; Q2UK72; -.
DR EnsemblFungi; BAE58043; BAE58043; AO090003000927.
DR GeneID; 5992028; -.
DR KEGG; aor:AO090003000927; -.
DR VEuPathDB; FungiDB:AO090003000927; -.
DR HOGENOM; CLU_012062_22_4_1; -.
DR OMA; ASPMEQK; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:AspGD.
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 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;
KW Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..765
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295382"
FT DOMAIN 49..127
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 137..214
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 230..307
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 333..470
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 659..736
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 83027 MW; E98DFA415EF360DD CRC64;
MSADASTTPA ADSNVTSTPE TSTTPAAPAP EVTAVESTTA PNASQPHSAS LYVGELDPSV
TEAMLYELFS SIGQVASIRV CRDAVTRRSL GYAYVNYNNT ADGERALEDL NYTLIKGKPC
RIMWSQRDPA LRKTGQGNVF IKNLDSAIDN KALHDTFAAF GNILSCKVAQ DEFGNSKGYG
FVHYETAEAA NNAIKHVNGM LLNDKKVFVG HHISKKDRQS KFEEMKANFT NVYIKNIDQD
VTEEEFRELF EKFGEITSAT LSRDQEGKSR GFGFVNFSTH ESAQAAVDEM NEKEIRTQKL
YVGRAQKKHE REEELRKQYE AARLEKASKY QGVNLYVKNL TDDVDDEKLR ELFGPYGTIT
SAKVMRDTNI ERTQTPESDK EKENKEATKE NEKESSEAEK AEKTEEKPAD SGDEKKEDKE
SKKADKKGLG KSKGFGFVCF SSPDEASKAV TEMNQRMVNG KPLYVALAQR KDVRRSQLEA
SIQARNTIRQ QQAAAAAGMP QPYMQPAVFY GPGQQGFIPG QRGGIAFPPQ PGMVMAGIPG
GRPGQYPGPF PGQQGGRGMG PNQQLPPNFQ GIPMGAMQGP VPNGMGYPQG MAQVQFGRGA
GGRGQVPGMP NMGQGMRGPG YGQGRGGVPV QQGQMRPGQG GRGQNAAQAP AGRPEEAVAG
GLTAQALSAA PPPQQKQMLG EALYPKIQAQ QPELAGKITG MLLEMENTEL LSLLEDEEAL
RAKVDEALNV YDEYMKNKGG ESEATGEAAK PKEAAKETST EENKS
