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PABP_EMENI
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   25-MAY-2022, entry version 110.
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 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=8978035; DOI=10.1093/genetics/144.4.1463;
RA   Marhoul J.F., Adams T.H.;
RT   "Aspergillus fabM encodes an essential product that is related to poly(A)-
RT   binding proteins and activates development when 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., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., 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., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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   -!- INDUCTION: Constitutively expressed throughout the vegetative cell
CC       cycle. {ECO:0000269|PubMed:8978035}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC       {ECO:0000305}.
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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   AlphaFoldDB; Q5B630; -.
DR   SMR; Q5B630; -.
DR   STRING; 162425.CADANIAP00004687; -.
DR   EnsemblFungi; CBF74916; CBF74916; ANIA_04000.
DR   EnsemblFungi; EAA59471; EAA59471; AN4000.2.
DR   GeneID; 2873424; -.
DR   KEGG; ani:AN4000.2; -.
DR   VEuPathDB; FungiDB:AN4000; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   InParanoid; Q5B630; -.
DR   OMA; ASPMEQK; -.
DR   OrthoDB; 1027234at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; ISS:AspGD.
DR   GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 3.
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   Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..732
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295390"
FT   DOMAIN          42..120
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          130..207
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          223..300
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          326..454
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          630..707
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        401
FT                   /note="K -> E (in Ref. 1; AAB16848)"
FT                   /evidence="ECO:0000305"
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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