PABP_ASPCL
ID PABP_ASPCL Reviewed; 754 AA.
AC A1CRM1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=ACLA_030250;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW08292.1; -; Genomic_DNA.
DR RefSeq; XP_001269718.1; XM_001269717.1.
DR AlphaFoldDB; A1CRM1; -.
DR SMR; A1CRM1; -.
DR STRING; 5057.CADACLAP00002493; -.
DR EnsemblFungi; EAW08292; EAW08292; ACLA_030250.
DR GeneID; 4701947; -.
DR KEGG; act:ACLA_030250; -.
DR VEuPathDB; FungiDB:ACLA_030250; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR OMA; ASPMEQK; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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 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..754
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295379"
FT DOMAIN 51..129
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 139..216
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 232..309
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 335..465
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 649..726
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 81855 MW; FEF347BF8D95B7EA CRC64;
MSAEVSTTPA ADNVNGTPEA TNAAATSAPE VTAVESSSPT SPNNNNQPHS ASLYVGELDP
SVTEAMLYEL FSSIGQVASI RVCRDAVTRR SLGYAYVNYN NTADGERALE DLNYTLIKGK
PCRIMWSQRD PALRKTGQGN VFIKNLDSAI DNKALHDTFA AFGNILSCKV AQDEFGNSKG
YGFVHYETAE AANNAIKHVN GMLLNDKKVF VGHHISKKDR QSKFDEMKAN FTNIYIKNID
PDVTEEEFRK IFEQFGEITS ATLSRDPEGK SRGFGFVNYS THESAQAAVD EMHDKEVKTQ
KLYVGRAQKK HEREEELRKQ YEAARLEKAS KYQGVNLYVK NLTDDVDDEK LRELFGPYGT
ITSAKVMRDS TPAERTETPD SEKEKEVNKE NEKKEDEEKA AEEKPKESDE EKKDETKKSD
KKLLGKSKGF GFVCFSSPDE ASKAVTEMNQ RMVNGKPLYV ALAQRKDVRR SQLEASIQAR
NTIRQQQAAA AAGMPQPYMQ PAVFYGPGQQ GFIPAGQRGG MPFAPQPGMV MGIPGGRPGQ
YPGPFPGQQG GRGMGPNQQM PPNFQGIPMG AMQGPGGIPN GMGYPQAMGQ VQFGRGGGRG
QVPGMPMGQG MRGPGYQGRG GPQGGPRPQG GRGQNAAAQP AAGREEAPAG ALTAQALNAA
APPQQKQMLG EALYPKIQAQ QPELAGKITG MLLEMDNTEL LGLLEDDDAL RAKVDEALSV
YDEYMKNKGE GEAPADADKP KEAAKETATE ENKS
