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PABP_ASPFU
ID   PABP_ASPFU              Reviewed;         753 AA.
AC   Q4WK03;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
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; ORFNames=AFUA_1G04190;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
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DR   EMBL; AAHF01000007; EAL88129.1; -; Genomic_DNA.
DR   RefSeq; XP_750167.1; XM_745074.1.
DR   AlphaFoldDB; Q4WK03; -.
DR   SMR; Q4WK03; -.
DR   STRING; 746128.CADAFUBP00000447; -.
DR   SwissPalm; Q4WK03; -.
DR   EnsemblFungi; EAL88129; EAL88129; AFUA_1G04190.
DR   GeneID; 3507350; -.
DR   KEGG; afm:AFUA_1G04190; -.
DR   VEuPathDB; FungiDB:Afu1g04190; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   InParanoid; Q4WK03; -.
DR   OMA; ASPMEQK; -.
DR   OrthoDB; 1027234at2759; -.
DR   PHI-base; PHI:2544; -.
DR   Proteomes; UP000002530; Chromosome 1.
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; IBA:GO_Central.
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   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 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   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA transport; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..753
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295380"
FT   DOMAIN          52..130
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          140..217
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          233..310
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          336..460
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          648..725
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..417
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  81445 MW;  37743012182E6105 CRC64;
     MSAEVSTTPA ADNTVNGTPE ATNAAATSAP EVTAVESASP STTPSASQPH SASLYVGELD
     PSVTEAMLYE LFSSIGQVAS IRVCRDAVTR RSLGYAYVNY NNTADGERAL EDLNYTLIKG
     KPCRIMWSQR DPALRKTGQG NVFIKNLDAA IDNKALHDTF AAFGNILSCK VAQDEFGNSK
     GYGFVHYETA EAANNAIKHV NGMLLNDKKV FVGHHISKKD RQSKFEEMKA NFTNVYIKNI
     DQEVTDEEFR KMFEKFGEIT SATLSRDQEG KSRGFGFVNF STHDSAQAAV DEMNDKEIKG
     QKLYVGRAQK KHEREEELRK QYEAARLEKA SKYQGVNLYV KNLTDDVDDE KLRELFSPFG
     TITSAKVMRD TVTTGETSES EKEKEKESNK ENEKEGEEKT EEKPKESEEE PKKTEKKILG
     KSKGFGFVCF SSPDEASKAV TEMNQRMVNG KPLYVALAQR KDVRRSQLEA SIQARNTIRQ
     QQAAAAAGMP QPYMQPAVFY GPGQQGFIPA GQRGGMPFAP QPGMVMGIPG GRPGQYPGPF
     PGQQGGRGMG PNQQIPPNFQ GIPMGAMQGP GGIPNGMGYP QMAQVQFGRG AGGRGQVPGM
     PMGQGIRGPG YGQGRGGAPV QGGPRPQGGR GQPAAAPPAA GREEVPATGG LTAQTLSAVP
     PPQQKQMLGE ALYPKIQAQQ PELAGKITGM LLEMDNNELL GLLEDEEALR AKVDEALSVY
     DEYMKNKGEG EAPAESAKPK EDAAETATEE NKS
 
 
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