PABP_CRYNB
ID PABP_CRYNB Reviewed; 673 AA.
AC P0CP47; Q55NH7; Q5KBW2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
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; OrderedLocusNames=CNBH1100;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AAEY01000041; EAL19418.1; -; Genomic_DNA.
DR RefSeq; XP_774065.1; XM_768972.1.
DR AlphaFoldDB; P0CP47; -.
DR SMR; P0CP47; -.
DR PRIDE; P0CP47; -.
DR EnsemblFungi; AAW45527; AAW45527; CNI01160.
DR EnsemblFungi; EAL19418; EAL19418; CNBH1100.
DR GeneID; 4937630; -.
DR KEGG; cnb:CNBH1100; -.
DR VEuPathDB; FungiDB:CNBH1100; -.
DR HOGENOM; CLU_012062_22_4_1; -.
DR Proteomes; UP000001435; Chromosome 8.
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 Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 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; Repeat; RNA-binding;
KW Translation regulation; Transport.
FT CHAIN 1..673
FT /note="Polyadenylate-binding protein, cytoplasmic and
FT nuclear"
FT /id="PRO_0000410181"
FT DOMAIN 46..124
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 134..211
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..304
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 330..407
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 569..646
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 72708 MW; B41F74AD0F3F6427 CRC64;
MSAETATSPA PAAETPVAPA PATQTTPAEG APTPAAAAPG GNTVSASLYV GELDPSVTEA
MLFEIFNMIG PVASIRVCRD AVTRRSLGYA YVNYLNAADG ERALEHLNYS LIKGQSCRIM
WSQRDPALRK TGQGNIFIKN LDQSIDNKAL HDTFAAFGDI LSCKVGTDEN GKSRGFAFVH
YSTGEAADAA IKAVNGMLLN DKKVYVGHHV GKKERLSKVE ELRAQFTNVY IKNVDLEVTD
AEFEDLVKPF GPTISVALSR DEKGVSKGFG FVNYENHESA RKAVDELNEK EVNGKKLYAG
RAQTKSEREA ELKKSHEEKR LENEAKSAGV NLYVKNLDDE WDDDRLRAEF EAFGTITSSK
VMRDDSGVSR GFGFVCYSSP DEATKAVSEM NGKMIGTKPL YVALAQRKDV RRQALESQIA
QRAQQRMQYG AGFPGMQGYM GQPMYGYPPM PGYGQPMPGM PPVRGPMMGY PGAPQNMMQS
RPRFNPNGQP LPGGVPAYGM PPQVPYPGAP GYPVRPGGAR IPAAPNANGP RNGGPSPVGA
PQGLPAGSIP RGGQMPARPH EQAAPAPQAG RLDAQSLARA APAEQKQMLG EALYPLIHET
QPELAGKITG MLLEMDNAEL LHLVESQPAL QEKVDEALRV LAEWGKDEKP AADEGAEEPK
KEEEETKEEE KKE
