PABP_DEBHA
ID PABP_DEBHA Reviewed; 627 AA.
AC Q6BI95; B5RUR5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 104.
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=DEHA2G12474g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382139; CAR65959.1; -; Genomic_DNA.
DR RefSeq; XP_002770625.1; XM_002770579.1.
DR AlphaFoldDB; Q6BI95; -.
DR SMR; Q6BI95; -.
DR STRING; 4959.XP_002770625.1; -.
DR EnsemblFungi; CAR65959; CAR65959; DEHA2G12474g.
DR GeneID; 8999193; -.
DR KEGG; dha:DEHA2G12474g; -.
DR VEuPathDB; FungiDB:DEHA2G12474g; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q6BI95; -.
DR OMA; SHAEQKD; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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; 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..627
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000295389"
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..412
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 537..618
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69963 MW; 89F646D7B0EF5962 CRC64;
MSAADANQVQ ESLEKLNLDS APVASTEETE QTASGETEEA ADSAQVSDTS ASLYVGELNP
SVNEALLFEI FSPIGQVASI RVCRDAVTKK SLGYAYVNFH KFEDGEKAIE DLNYSLIEGR
PCRIMWSQRD PSLRRNGDGN IFIKNLHPAI DNKALHDTFT AFGKILSCKV ATDDMGISKC
FGFVHYETAE AAEAAIENVN GMLLNDREVY VGKHISKKDR ESKFEEMKAN FTNVYAKNID
LDFSEEEFKK LFEAYGKITS IYLEKDHEGK SKGFGFVNFE NHESAVKAVD ELNDKEINGQ
KIYVGRAQKK RERLEELKKQ YENTRLEKLS KYQGVNLFIK NLDDTIDSEK LEEEFKPFGS
ITSARVMVDE TGKSKGFGFV CFSSPEEATK AITEMNQRMI YGKPLYVALA QRKDVRRSQL
EQQIQARNQM RMQNAAATGG IPGQFIPPMF YGQQPGFFPP NGRGNGPFPG PNPQMMMPRG
QIPPPQGQWP RPGPNGQPVP VYGMPPVYGG DFNNGANGGR QQRGYYPNRN QNQKGRQQKD
LAAIIANAPA DQQKRILGEE LYPKIVSTGK AQEPEAAGKI TGMMLDLDNE EILALLEDDE
LFNTHFEDAL TAFEEYKKSS EAATAEN
