PABP_CANGA
ID PABP_CANGA Reviewed; 579 AA.
AC Q6FKG4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 112.
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; OrderedLocusNames=CAGL0L11792g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380958; CAG62254.1; -; Genomic_DNA.
DR RefSeq; XP_449280.1; XM_449280.1.
DR AlphaFoldDB; Q6FKG4; -.
DR SMR; Q6FKG4; -.
DR STRING; 5478.XP_449280.1; -.
DR EnsemblFungi; CAG62254; CAG62254; CAGL0L11792g.
DR GeneID; 2890944; -.
DR KEGG; cgr:CAGL0L11792g; -.
DR CGD; CAL0135516; CAGL0L11792g.
DR VEuPathDB; FungiDB:CAGL0L11792g; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q6FKG4; -.
DR OMA; HNESLKA; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:EnsemblFungi.
DR GO; GO:0008143; F:poly(A) binding; IEA:EnsemblFungi.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:EnsemblFungi.
DR GO; GO:0008428; F:ribonuclease inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblFungi.
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; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
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..579
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295385"
FT DOMAIN 35..113
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 123..200
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 216..293
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 319..396
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 487..566
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64667 MW; 81BB5C4C7D35F798 CRC64;
MADITEKTAE QLENLSLQDK QEGTNEENQS ETVSASLYVG DLDPSVSEAH LYDIFSPIGA
VSSIRVCRDA ITKTSLGYAY VNFNDHDAAK TAIEKLNFTP IKGKLCRIMW SQRDPSLRKK
GAGNIFIKNL HPDIDNKALY DTFSVFGNIL SSKVATDETG KSKGFGYVHF EEDESASEAI
DALNGMLLNG QEIYVGPHLS KKERESKFEE MKANFTNVYI KNINTETTDK EFEELVAKFG
KTDSVVLERT PEGENKGFGF VNFVNHEDAV KCVEELNNTE FKGQPLYVNR AQKKYERQQE
LKKQYEATRM EKMAKYQGIN LFIKNLDDSI DDKKLEEEFA PYGTITSAKV MTTENGKSKG
FGFVCFSTPE EATKAITEKN QQIVAGKPLY VAIAQRKDVR RSQLAQQIQA RNQMRFQQAS
AAAAAAAAAG MPGQFMPPMF YGVMPPRGVP FNGPNPQMAN MGAMPKNGMP PHQFRNGPVY
GVPPQGGFAR NGPAANQFYQ QKQRQALGEE LYKRIFSRTN DEEAAGKITG MILDLPPQEV
VPLLENDELF EQHFKEASAA YESFKQEQQQ PQGEEAQQA
