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Database: UniProt
Entry: Q5B630
LinkDB: Q5B630
Original site: Q5B630 
ID   PABP_EMENI              Reviewed;         732 AA.
AC   Q5B630; C8V5R9; Q92227;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   22-JAN-2014, entry version 68.
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; Synonyms=fabM; ORFNames=AN4000;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=8978035;
RA   Marhoul J.F., Adams T.H.;
RT   "Aspergillus fabM encodes an essential product that is related to
RT   poly(A)-binding proteins and activates development when
RT   overexpressed.";
RL   Genetics 144:1463-1470(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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   -!- INDUCTION: Constitutively expressed throughout the vegetative cell
CC       cycle.
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; U70731; AAB16848.1; -; Genomic_DNA.
DR   EMBL; AACD01000065; EAA59471.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF74916.1; -; Genomic_DNA.
DR   RefSeq; XP_661604.1; XM_656512.1.
DR   ProteinModelPortal; Q5B630; -.
DR   SMR; Q5B630; 42-211, 633-712.
DR   STRING; 162425.CADANIAP00004687; -.
DR   PRIDE; Q5B630; -.
DR   EnsemblFungi; CADANIAT00004687; CADANIAP00004687; CADANIAG00004687.
DR   GeneID; 2873424; -.
DR   KEGG; ani:AN4000.2; -.
DR   eggNOG; COG0724; -.
DR   HOGENOM; HOG000217922; -.
DR   KO; K13126; -.
DR   OMA; LHADITE; -.
DR   OrthoDB; EOG706125; -.
DR   GO; GO:0005829; C:cytosol; IDA:ASPGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008143; F:poly(A) RNA binding; ISS:ASPGD.
DR   GO; GO:0006527; P:arginine catabolic process; IMP:ASPGD.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IMP:ASPGD.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:ASPGD.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1900.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 5.
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; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF63570; SSF63570; 1.
DR   TIGRFAMs; TIGR01628; PABP-1234; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; mRNA processing; mRNA transport;
KW   Nucleus; Reference proteome; Repeat; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN         1    732       Polyadenylate-binding protein,
FT                                cytoplasmic and nuclear.
FT                                /FTId=PRO_0000295390.
FT   DOMAIN       42    120       RRM 1.
FT   DOMAIN      130    207       RRM 2.
FT   DOMAIN      223    300       RRM 3.
FT   DOMAIN      326    454       RRM 4.
FT   DOMAIN      630    707       PABC.
FT   COMPBIAS    477    481       Poly-Ala.
FT   COMPBIAS    495    625       Gly-rich.
FT   CONFLICT    401    401       K -> E (in Ref. 1; AAB16848).
SQ   SEQUENCE   732 AA;  79321 MW;  69D3FD71EA49668E CRC64;
     MSAETSTTPA PAENTNGTPD NAPAPEVTAV EAPATTSQPH SASLYVGELD PSVTEAMLYE
     LFSSIGQVAS IRVCRDAVTR RSLGYAYVNY NDTAHGERAL DELNYTLIKG KPCRIMWSQR
     DPALRKTGQG NVFIKNLDSA IDNKALHDTF AAFGNILSCK VAQDEFGVSK GYGFVHYETA
     EAANNAIKHV NGMLLNDKKV FVGHHISKKD RQSKFEEMKA NFTNIYIKNI DPEVEDEEFR
     KLFEKFGEIT SATLSRDSEG KSRGFGFVNF STHESAQAAV EEMNDKEVRS QKLYVGRAQK
     KHEREEELRK QYEAARMEKA SKYQGVNLYV KNLTDDVDDD KLRELFGPYG TITSAKVMRD
     TAPVETATPE SETKESANKE NEKAAEGEKE PAAEEKEKEE KKEAEQKPEK KPLGKSKGFG
     FVCFSSPDEA SKAVTEMNQR MVNGKPLYVA LAQRKDVRRS QLEASIQARN NIRQQQAAAA
     AGMGQAYMAP AVFYGPGQQG FIPGAQRGGM FPPQPGMMMG MPGRPGQYPG PFPGQQGGRG
     VGPNQQIPPN FQGLPMGAMQ GPGIPNGMGY PMVQGQFGGG RGRGQVPGMG GPMRGGYGGG
     RGGVPLGGQM RPGQGGRGQA VGQPGPETPV GVLTAQALSA APPQQQKQML GEALYPKIQA
     TQPELAGKIT GMLLEMDNTE LLGLLEDDEA LRAKVDEALS VYDEYMKNKS DEPAAEKPKE
     AAQEAPAEEN KA
//
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