EPAB_XENTR
ID EPAB_XENTR Reviewed; 629 AA.
AC Q6DEY7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Embryonic polyadenylate-binding protein;
DE Short=Embryonic poly(A)-binding protein;
DE Short=ePABP;
GN Name=epabp {ECO:0000250|UniProtKB:Q98SP8};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH76956.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH76956.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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; BC076956; AAH76956.1; -; mRNA.
DR RefSeq; NP_001005062.1; NM_001005062.1.
DR AlphaFoldDB; Q6DEY7; -.
DR SMR; Q6DEY7; -.
DR STRING; 8364.ENSXETP00000034446; -.
DR DNASU; 448615; -.
DR Ensembl; ENSXETT00000091878; ENSXETP00000088612; ENSXETG00000022831.
DR GeneID; 448615; -.
DR KEGG; xtr:448615; -.
DR CTD; 80336; -.
DR Xenbase; XB-GENE-5742459; pabpc1l.
DR eggNOG; KOG0123; Eukaryota.
DR InParanoid; Q6DEY7; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022831; Expressed in ovary and 8 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0031370; F:eukaryotic initiation factor 4G binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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"
FT /id="PRO_0000233956"
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; 70648 MW; 9ECDBFA42254B307 CRC64;
MNATGAGYPL ASLYVGDLHP DVTEAMLYEK FSPAGPIMSI RVCRDIATRR SLGYAYINFQ
QPADAERALD TMNFEVIKGR PIRIMWSQRD PGLRKSGVGN VFIKNLDESI DNKALYDTFS
AFGNILSCKV VCDEHGSRGY GFVHFETQEA ANRAIQTMNG MLLNDRKVFV GHFKSRRERE
LEYGAKVMEF TNVYIKNFGE DMDDKRLREI FSAFGNTLSV KVMMDDTGRS RGFGFVNYGN
HEEAQKAVSE MNGKEVNGRM IYVGRAQKRI ERQGELKRKF EQIKQERINR YQGVNLYVKN
LDDGIDDDRL RKEFSPYGTI TSAKVMTEGG HSKGFGFVCF SSPEEATKAV TEMNGRIVST
KPLYVALAQR KEERKAILTN QYMQRLATMR AMPGPLLGSF QQPANYFLPA MPQPPNRTFY
SPNPVAPVRQ APQWTSHQSR PPQYQPPAPL MRAVPPRRMS SNISTMKQAS TQVPRVAPHS
QRVANIGTQT AGARAQVNPS IMRTMPHYKY SCAVRNVQPI GTNTHLQQVM EPAVLMQGQE
PLTASSLASA PPQEQKQMLG ERLYPLIHEM HPTLAGKITG MLLEIDNSEL LHMLESPESL
HSKVEEAVAV LQAHQAKENS QKSAQQSLI
