ID PABP_USTMA Reviewed; 651 AA.
AC Q4P8R9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-APR-2013, entry version 51.
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=UM03494;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen
RT Ustilago maydis.";
RL Nature 444:97-101(2006).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an
CC important mediator of the multiple roles of the poly(A) tail in
CC mRNA biogenesis, stability and translation. In the nucleus,
CC involved in both mRNA cleavage and polyadenylation. Is also
CC required for efficient mRNA export to the cytoplasm. Acts in
CC concert with a poly(A)-specific nuclease (PAN) to affect poly(A)
CC tail shortening, which may occur concomitantly with either
CC nucleocytoplasmic mRNA transport or translational initiation. In
CC the cytoplasm, stimulates translation initiation and regulates
CC mRNA decay through translation termination-coupled poly(A)
CC shortening, probably mediated by PAN (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
CC family.
CC -!- SIMILARITY: Contains 1 PABC domain.
CC -!- SIMILARITY: Contains 4 RRM (RNA recognition motif) domains.
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DR EMBL; AACP01000117; EAK84632.1; -; Genomic_DNA.
DR RefSeq; XP_759641.1; XM_754548.1.
DR HSSP; P11940; 1CVJ.
DR ProteinModelPortal; Q4P8R9; -.
DR SMR; Q4P8R9; 48-215, 557-638.
DR MINT; MINT-7230141; -.
DR STRING; 5270.UM03494.1; -.
DR EnsemblFungi; UM03494T0; UM03494P0; UM03494.
DR GeneID; 3631594; -.
DR KEGG; uma:UM03494.1; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000217922; -.
DR KO; K13126; -.
DR OMA; MYGQMPP; -.
DR OrthoDB; EOG4QJVWJ; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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 Gene3D; 1.10.1900.10; -; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF63570; PABP_HYD; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; mRNA processing; mRNA transport;
KW Nucleus; Reference proteome; Repeat; RNA-binding;
KW Translation regulation; Transport.
FT CHAIN 1 651 Polyadenylate-binding protein,
FT cytoplasmic and nuclear.
FT /FTId=PRO_0000295400.
FT DOMAIN 47 125 RRM 1.
FT DOMAIN 135 211 RRM 2.
FT DOMAIN 227 304 RRM 3.
FT DOMAIN 330 407 RRM 4.
FT DOMAIN 555 632 PABC.
FT COMPBIAS 10 17 Poly-Ala.
FT COMPBIAS 439 555 Pro-rich.
SQ SEQUENCE 651 AA; 70488 MW; D33154CAAB235D83 CRC64;
MSSTESPVPA AAAPAEAVPA STPAPAAEQP AVGNGEQRNN ADAANNTSLY VGELDPSVTE
AMLFEIFSMI GTVASIRVCR DAVTRRSLGY AYVNFLNAAD GERAMEQLNY SLIRNRPCRI
MWSQRDPALR RTGQGNIFIK NLDAGIDNKA LHDTFAAFGN ILSCKVATNE TGSLGYGFVH
YETAEAAEAA IKHVNGMLLN DKKVYVGHHI PRKERQAKIE ETRANFTNVY AKNVDPEVTD
DEFEKLFTKF GKITSCVLQR DEDGKSKGFG FVNFEDHNEA QKAVDELHDS DFKGQKLFVA
RAQKKSEREE ELRRSYEAAK NEKLAKFQGV NLYLKNIPES YDDERLREEF APFGAITSCK
IMRAPSGVSR GFGFVCYSAP EEANKAVSEM NGKMLDNRPL YVALAQRKDV RRQQLEAQIM
QRNQLRLQQQ AAAQGMGYPG PGMYYPQPGA FPGQPGGMVP RPRYAPAGMM PQGMPMAPYG
QPGQFPAGMM PQGYRPARPP RGAPNAAGGP APPAGARPPT GVNGAPRPAG QPVPGQPMPR
GPAARPAGRP EADQPGALTA AALAKASPEE QKQMLGEAIY PKVAASQPEL AGKLTGMILE
LPVTELLHLL EESEALDAKV NEALEVLKEY QQNDSAGAEA EANAEAPKTE A
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