EPA2A_XENLA
ID EPA2A_XENLA Reviewed; 218 AA.
AC Q804A5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Embryonic polyadenylate-binding protein 2-A;
DE Short=Embryonic poly(A)-binding protein 2-A;
DE Short=XePABP2-A;
DE Short=ePABP-2A;
DE Short=ePABP2-A;
DE AltName: Full=Embryonic poly(A)-binding protein type II-A;
DE AltName: Full=PABPN2;
DE AltName: Full=p32;
GN Name=Pabpn1l-a; Synonyms=epabp2-a, pabpnl1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO33927.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:15380618};
RX PubMed=15380618; DOI=10.1016/j.biolcel.2004.04.006;
RA Cosson B., Braun F., Paillard L., Blackshear P., Beverley Osborne H.;
RT "Identification of a novel Xenopus laevis poly(A) binding protein.";
RL Biol. Cell 96:519-527(2004).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Unable to interact with the
CC cap-binding complex and is therefore unlikely to be involved in
CC translation initiation. {ECO:0000269|PubMed:15380618}.
CC -!- INTERACTION:
CC Q804A5; Q804A5: Pabpn1l-a; NbExp=3; IntAct=EBI-15731026, EBI-15731026;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15380618}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Restricted to oogenesis and early embryogenesis. During oogenesis,
CC levels increase between stage I and II and then remain constant through
CC oocyte growth to stage VI. During early embryogenesis, levels remain
CC approximately constant up to 5 days after fertilization. In older
CC embryos levels decrease, being totally absent at 15 days post-
CC fertilization (at protein level). {ECO:0000269|PubMed:15380618}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY221506; AAO33927.1; -; mRNA.
DR RefSeq; NP_001082505.1; NM_001089036.1.
DR AlphaFoldDB; Q804A5; -.
DR SMR; Q804A5; -.
DR DIP; DIP-46304N; -.
DR GeneID; 398516; -.
DR KEGG; xla:398516; -.
DR CTD; 398516; -.
DR Xenbase; XB-GENE-6256056; pabpn1l.L.
DR OrthoDB; 1412946at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 398516; Expressed in oocyte and 6 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-binding.
FT CHAIN 1..218
FT /note="Embryonic polyadenylate-binding protein 2-A"
FT /id="PRO_0000239463"
FT DOMAIN 93..170
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24247 MW; 99B2617E4DCD3F0A CRC64;
MSERVSEEPG LDKGDGAEEC ELDDPELKAI RMRVREMEEE AERLKGLSGQ DKSIGVSPRP
CMKLIHSKMT AGEYTEGPPR PLSAEEKKEI DKRSVYVGNV DYGGTAQDLE AHFSSCGSIN
RITILCDKFS GHPKGYAYIE FAERNSVDAA VTMDETVFRG RTIKVLPKRT NMPGISSTDR
GGFRGRPRGN RGNYQRGQRP RGRPFRGCGR PGPLNHPY
