ID   PABP_CRYNJ              Reviewed;         673 AA.
AC   P0CP46; Q55NH7; Q5KBW2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=CNI01160;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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; AE017349; AAW45527.1; -; Genomic_DNA.
DR   RefSeq; XP_572834.1; XM_572834.1.
DR   AlphaFoldDB; P0CP46; -.
DR   SMR; P0CP46; -.
DR   STRING; 5207.AAW45527; -.
DR   PaxDb; P0CP46; -.
DR   PRIDE; P0CP46; -.
DR   EnsemblFungi; AAW45527; AAW45527; CNI01160.
DR   GeneID; 3259708; -.
DR   KEGG; cne:CNI01160; -.
DR   VEuPathDB; FungiDB:CNI01160; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_4_1; -.
DR   InParanoid; P0CP46; -.
DR   OMA; ASPMEQK; -.
DR   OrthoDB; 1027234at2759; -.
DR   Proteomes; UP000002149; Chromosome 9.
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   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; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..673
FT                   /note="Polyadenylate-binding protein, cytoplasmic and
FT                   nuclear"
FT                   /id="PRO_0000295388"
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