EPAB2_RAT
ID EPAB2_RAT Reviewed; 269 AA.
AC B0BNE4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Embryonic polyadenylate-binding protein 2;
DE Short=Embryonic poly(A)-binding protein 2;
DE Short=ePABP-2;
DE Short=ePABP2;
DE AltName: Full=Embryonic poly(A)-binding protein type II;
DE AltName: Full=Poly(A)-binding protein nuclear-like 1;
GN Name=Pabpn1l; Synonyms=Epabp2, Pabpnl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; BC158789; AAI58790.1; -; mRNA.
DR RefSeq; NP_001107251.1; NM_001113779.1.
DR AlphaFoldDB; B0BNE4; -.
DR SMR; B0BNE4; -.
DR STRING; 10116.ENSRNOP00000050572; -.
DR jPOST; B0BNE4; -.
DR PaxDb; B0BNE4; -.
DR PeptideAtlas; B0BNE4; -.
DR GeneID; 307920; -.
DR KEGG; rno:307920; -.
DR UCSC; RGD:1562761; rat.
DR CTD; 390748; -.
DR RGD; 1562761; Pabpn1l.
DR VEuPathDB; HostDB:ENSRNOG00000029558; -.
DR eggNOG; KOG4209; Eukaryota.
DR HOGENOM; CLU_012062_23_2_1; -.
DR InParanoid; B0BNE4; -.
DR OMA; MWPFLSH; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; B0BNE4; -.
DR PRO; PR:B0BNE4; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000029558; Expressed in thymus and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0008143; F:poly(A) binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0160021; P:maternal-to-zygotic transition of gene expression; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0062026; P:negative regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process; ISO:RGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..269
FT /note="Embryonic polyadenylate-binding protein 2"
FT /id="PRO_0000349173"
FT DOMAIN 139..216
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 26..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29861 MW; 556B0E20F0952CF4 CRC64;
MWPSLSNELF PPPTEVWLQT VSSDPEAQGW GAWGRTEKTS LVPSAGSDKE AEENEDSSFL
LSLLEPENLA KSPVYNQELE AIRLKLWTME HAEVLPEPPS VQRKATEEER AEARELLSPE
TIGCFFPGAP KENVEADHRS VYVGNVDYGG SAAELEAYFS PCGEIHRVTI LCDKFSGHPK
GYAYIEFASK SSVQAAVRLD ESTFRGRVIK VLPKRTNFPG ISSTDRGGLR THSSSRAAFL
QGSLQRKPRL RPHGQSRGRG RASPWFSPY