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PABP_PICGU
ID   PABP_PICGU              Reviewed;         631 AA.
AC   A5DM21;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 72.
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=PGUG_04322;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC       {ECO:0000305}.
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DR   EMBL; CH408159; EDK40224.2; -; Genomic_DNA.
DR   RefSeq; XP_001483593.1; XM_001483543.1.
DR   AlphaFoldDB; A5DM21; -.
DR   SMR; A5DM21; -.
DR   STRING; 4929.XP_001483593.1; -.
DR   PRIDE; A5DM21; -.
DR   EnsemblFungi; EDK40224; EDK40224; PGUG_04322.
DR   GeneID; 5125666; -.
DR   KEGG; pgu:PGUG_04322; -.
DR   VEuPathDB; FungiDB:PGUG_04322; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   InParanoid; A5DM21; -.
DR   OMA; ASPMEQK; -.
DR   OrthoDB; 1027234at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; 4.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 4.
DR   SUPFAM; SSF54928; SSF54928; 2.
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..631
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295398"
FT   DOMAIN          58..136
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          146..223
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          239..316
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          342..419
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          545..626
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  69928 MW;  62FEEEC5B4D6BA33 CRC64;
     MSDLQESLEK LSINEKAPQA PADDATPSNT TTLEKESSES AAAAAGEGAG EEGEEASASL
     YVGELNPSVN EALLFEIFSP IGQVSSIRVC RDAVTKKSLG YAYVNFHKHA DGSRAIEELN
     YSLVDGRPCR IMWSQRDPSL RRNGDGNIFI KNLHPAIDNK ALHDTFSAFG RILSCKVATD
     ELGQSKCFGF VHYETAEAAE AAIENVNGML LNDREVFVGK HVSKRDRESK FEEMKANFTN
     VYVKNLAPEV DNAKFEEIFK PFGPVTSVHL ETDQEGKSRG FGFVNFENHE SALNAVKEMN
     DKEIDGQKLY VGRAQKKRER LDELKRLYES TRLEKLSKYQ GVNLFVKNLD DSIDSEKLEE
     EFKPFGTITS ARVMVDDAGK SKGFGFVCFS SPEEATKAIT EMNQRMIQGK PLYVALAQRK
     DVRRSQLEQQ IQARNQMRMQ NAAAAAGMPG QFMSPMFYGQ QPGFFPPNGR GGAQGPFPPN
     PQMMMPRGGQ MPPPQGQWPR AGPNGQPVPV YGMPPVYGGE FNGPNGQRQQ RGAYPPNRNQ
     KGGRPQRDLA AIISTVPVDQ QKRILGEELY PKIVATGKAQ EPEAAGKITG MMLDLENEEI
     LALLEDDELF ENHFEDALTA FEEYKKGEQA E
 
 
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