ID   PABP5_MACMU             Reviewed;         382 AA.
AC   Q7JGR2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Polyadenylate-binding protein 5;
DE            Short=PABP-5;
DE            Short=Poly(A)-binding protein 5;
GN   Name=PABPC5; Synonyms=PABP5;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11374897; DOI=10.1006/geno.2001.6530;
RA   Blanco P., Sargent C.A., Boucher C.A., Howell G., Ross M., Affara N.A.;
RT   "A novel poly(A)-binding protein gene (PABPC5) maps to an X-specific
RT   subinterval in the Xq21.3/Yp11.2 homology block of the human sex
RT   chromosomes.";
RL   Genomics 74:1-11(2001).
CC   -!- FUNCTION: Binds the poly(A) tail of mRNA. May be involved in
CC       cytoplasmic regulatory processes of mRNA metabolism. Can probably bind
CC       to cytoplasmic RNA sequences other than poly(A) in vivo (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AJ299082; CAC42819.1; -; Genomic_DNA.
DR   RefSeq; NP_001038193.1; NM_001044728.1.
DR   RefSeq; XP_014983253.1; XM_015127767.1.
DR   AlphaFoldDB; Q7JGR2; -.
DR   SMR; Q7JGR2; -.
DR   STRING; 9544.ENSMMUP00000015191; -.
DR   GeneID; 696409; -.
DR   KEGG; mcc:696409; -.
DR   CTD; 140886; -.
DR   eggNOG; KOG0123; Eukaryota.
DR   HOGENOM; CLU_012062_22_6_1; -.
DR   InParanoid; Q7JGR2; -.
DR   OMA; KCIDNRA; -.
DR   OrthoDB; 1027234at2759; -.
DR   TreeFam; TF300458; -.
DR   Proteomes; UP000006718; Unplaced.
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   CDD; cd12379; RRM2_I_PABPs; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR006515; PABP_1234.
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; PF00076; RRM_1; 4.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 3.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   TIGRFAMs; TIGR01628; PABP-1234; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..382
FT                   /note="Polyadenylate-binding protein 5"
FT                   /id="PRO_0000081707"
FT   DOMAIN          18..96
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          106..182
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          199..276
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          302..378
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   382 AA;  43317 MW;  23A52B81780C602B CRC64;
     MGSGEPNPAG KKKKYLKAAL YVGDLDPDVT EDMLYKKFRP AGPLRFTRIC RDPVTRSPLG
     YGYVNFRFPA DAEWALNTMN FDLINGKPFR LMWSQPDDRL RKSGVGNIFI KNLDKSIDNR
     ALFYLFSAFG NILSCKVVCD DNGSKGYAYV HFDSLAAANR AIWHMNGVRL NNRQVYVGRF
     KFPEERAAEV RTRDRATFTN VFVKNIGDDI DDEKLKELFC EYGPTESVKV IRDASGKSKG
     FGFVRYETHE AAQKAVLDLH GKSIDGKVLY VGRAQKKIER LAELRRRFER LRLKEKSRPP
     GVPIYIKNLD ETINDEKLKE EFSSFGSISR AKVMMEVGQG KGFGVVCFSS FEEATKAVDE
     MNGRVVGSKP LHVTLGQARR RC