ID   EPABB_XENLA             Reviewed;         629 AA.
AC   Q6GR16;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Embryonic polyadenylate-binding protein B;
DE            Short=Embryonic poly(A)-binding protein B;
DE            Short=ePAB-B;
DE            Short=ePABP-B;
DE   AltName: Full=XePABP-B;
GN   Name=epabp-b;
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:0000312|EMBL:AAH71118.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH71118.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds and protects the poly(A) tail of mRNA with or without
CC       an AU-rich element (ARE) and prevents mRNA deadenylation. Stimulates
CC       the translation of mRNAs to which it is bound during early development
CC       (By similarity). {ECO:0000250|UniProtKB:Q98SP8}.
CC   -!- SUBUNIT: Interacts with dazl in an RNA-independent manner. The C-
CC       terminus can self-associate and also interact with the C-terminus of
CC       pabpc1, independently of RNA. RRM 1 and RRM 2 interact with both eif4g1
CC       and paip1, and the C-terminus also interacts with paip1. Prior to
CC       oocyte maturation, found in a complex with dazl and pum2 proteins and
CC       spdy1 mRNA; pum2 dissociates from the complex during maturation.
CC       Interacts with the translation termination factor sup35/erf3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q98SP8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associated with
CC       polysomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC071118; AAH71118.1; -; mRNA.
DR   RefSeq; NP_001085351.1; NM_001091882.1.
DR   AlphaFoldDB; Q6GR16; -.
DR   SMR; Q6GR16; -.
DR   BioGRID; 101940; 1.
DR   DNASU; 443777; -.
DR   GeneID; 443777; -.
DR   KEGG; xla:443777; -.
DR   CTD; 443777; -.
DR   Xenbase; XB-GENE-6251876; pabpc1l.L.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 443777; Expressed in oocyte and 14 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031370; F:eukaryotic initiation factor 4G binding; ISS:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0043009; P:chordate embryonic development; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR   GO; GO:0006412; P: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   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 4.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SMART; SM00361; RRM_1; 3.
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   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; Protein biosynthesis; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..629
FT                   /note="Embryonic polyadenylate-binding protein B"
FT                   /id="PRO_0000233955"
FT   DOMAIN          11..89
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          99..175
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          191..268
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          294..370
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          539..616
FT                   /note="PABC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
SQ   SEQUENCE   629 AA;  70589 MW;  754CBE81F0B67FAA CRC64;
     MNATRAEYPL ASLYIGDLHP DVTEAMLYEK FSPAGPIMSI RVCRDIATRR SLGYAYINFQ
     QPADAERALD TMNFEVIKGR PIRIMWSQRD PGLRKSGVGN VFIKNLDDSI DNKALYDTFS
     AFGDILSCKV VCDEYGSRGY GFVHFETQEA ANRAIQTMNG MLLNDRKVFV GHFKSRRERE
     LEYGAKVMEF TNVYIKNFGE DMDDKRLKEI FSAFGNTLSV KVMMDNSGRS RGFGFVNYGN
     HEEAQKAVTE MNGKEVNGRM VYVGRAQKRI ERQGELKRKF EQIKQERINR YQGVNLYVKN
     LDDGIDDDRL RKEFSPYGTI TSTKVMTEGG HSKGFGFVCF SSPEEATKAV TEMNGRIVST
     KPLYVALAQR KEERKAILTN QYMQRLATMR AMPGPLLGSF QQPANYFLPT MPQPSNRAFY
     SPNPVAPVRP APQWASHQSR PPQYQPPAPL MRAVPPRRMH SNISTMKQAS TQVPRVPLQS
     QRVANIGTQT AGARAQVNAS IMRAMPHYKY SCGVRNVQPI GSSAHLQQVL EPAVLMQGQE
     PLTASLLAAA PLQEQKQILG ERIYPLIHEM HPTLAGKITG MLLEIDNSEL LHMLESPESL
     HSKVEEAVAV LQAHQAKESA PKSAPQSLI