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 03-APR-2013, entry version 63.
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; Trichocomaceae; Emericella.
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 HSSP; P11940; 1CVJ.
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; MIRITYS; -.
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; -; 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; PABP_HYD; 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
//
