EPABA_XENLA
ID EPABA_XENLA Reviewed; 629 AA.
AC Q98SP8; Q68F25;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Embryonic polyadenylate-binding protein A;
DE Short=Embryonic poly(A)-binding protein A;
DE Short=ePAB-A;
DE Short=ePABP-A;
DE AltName: Full=XePABP-A;
GN Name=epabp-a; Synonyms=epab {ECO:0000312|EMBL:AAK29408.1};
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:AAK29408.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 97-104; 139-153 AND
RP 168-174, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary {ECO:0000269|PubMed:11274061};
RX PubMed=11274061; DOI=10.1101/gad.872201;
RA Voeltz G.K., Ongkasuwan J., Standart N., Steitz J.A.;
RT "A novel embryonic poly(A) binding protein, ePAB, regulates mRNA
RT deadenylation in Xenopus egg extracts.";
RL Genes Dev. 15:774-788(2001).
RN [2] {ECO:0000312|EMBL:AAH80020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH80020.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SUP35, AND DEVELOPMENTAL STAGE.
RX PubMed=12489691; DOI=10.1016/s0248-4900(02)01195-4;
RA Cosson B., Couturier A., Le Guellec R., Moreau J., Chabelskaya S.,
RA Zhouravleva G., Philippe M.;
RT "Characterization of the poly(A) binding proteins expressed during
RT oogenesis and early development of Xenopus laevis.";
RL Biol. Cell 94:217-231(2002).
RN [4] {ECO:0000305}
RP INTERACTION WITH DAZL.
RX PubMed=16001084; DOI=10.1038/sj.emboj.7600738;
RA Collier B., Gorgoni B., Loveridge C., Cooke H.J., Gray N.K.;
RT "The DAZL family proteins are PABP-binding proteins that regulate
RT translation in germ cells.";
RL EMBO J. 24:2656-2666(2005).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EIF4G1; PABPC1 AND PAIP1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15713657; DOI=10.1128/mcb.25.5.2060-2071.2005;
RA Wilkie G.S., Gautier P., Lawson D., Gray N.K.;
RT "Embryonic poly(A)-binding protein stimulates translation in germ cells.";
RL Mol. Cell. Biol. 25:2060-2071(2005).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH SPDY1; PUM2 AND DAZL.
RX PubMed=16418484; DOI=10.1101/gad.1383106;
RA Padmanabhan K., Richter J.D.;
RT "Regulated Pumilio-2 binding controls RINGO/Spy mRNA translation and CPEB
RT activation.";
RL Genes Dev. 20:199-209(2006).
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 {ECO:0000269|PubMed:11274061, ECO:0000269|PubMed:12489691,
CC ECO:0000269|PubMed:15713657}.
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.
CC {ECO:0000269|PubMed:12489691, ECO:0000269|PubMed:15713657,
CC ECO:0000269|PubMed:16001084, ECO:0000269|PubMed:16418484}.
CC -!- INTERACTION:
CC Q98SP8; O73932: igf2bp3-a; NbExp=2; IntAct=EBI-7191347, EBI-619004;
CC Q98SP8; A8KBF3: piwil2; Xeno; NbExp=3; IntAct=EBI-7191347, EBI-7191401;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11274061,
CC ECO:0000269|PubMed:15713657}. Note=Associated with polysomes.
CC -!- TISSUE SPECIFICITY: Expressed in adult testis, but at a reduced level
CC compared to oocytes. {ECO:0000269|PubMed:15713657}.
CC -!- DEVELOPMENTAL STAGE: Predominant from the stage VI oocyte through to
CC the neurula stage (30 hours embryo), with levels decreasing at the
CC onset of zygotic transcription. {ECO:0000269|PubMed:11274061,
CC ECO:0000269|PubMed:12489691, ECO:0000269|PubMed:15713657}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; AF338225; AAK29408.1; -; mRNA.
DR EMBL; BC080020; AAH80020.1; -; mRNA.
DR RefSeq; NP_001082094.1; NM_001088625.1.
DR RefSeq; XP_018092825.1; XM_018237336.1.
DR AlphaFoldDB; Q98SP8; -.
DR SMR; Q98SP8; -.
DR BioGRID; 99556; 1.
DR IntAct; Q98SP8; 3.
DR MINT; Q98SP8; -.
DR MaxQB; Q98SP8; -.
DR DNASU; 398221; -.
DR GeneID; 398221; -.
DR KEGG; xla:398221; -.
DR CTD; 398221; -.
DR Xenbase; XB-GENE-5742498; pabpc1l.S.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 398221; Expressed in ovary and 8 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IPI:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0043009; P:chordate embryonic development; IEP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA: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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; mRNA processing;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..629
FT /note="Embryonic polyadenylate-binding protein A"
FT /id="PRO_0000233954"
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"
FT CONFLICT 552
FT /note="P -> L (in Ref. 1; AAK29408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 70704 MW; F9C1BBB5A3E1B3AF CRC64;
MNATGAGYPL ASLYIGDLHP DVTEAMLYEK FSPAGPIMSI RVCRDIATRR SLSYAYINFQ
QPADAERALD TMNFEVIKGR PIRIMWSQRD PGLRKSGVGN VFIKNLDESI DNKALYDTFS
AFGNILSCKV VCDEHGSRGY GFVHFETHEA ANRAIQTMNG MLLNDRKVFV GHFKSRRERE
LEYGAKVMEF TNVYIKNFGE DMDDKRLREI FSAFGNTLSV KVMMDDSGRS RGFGFVNYGN
HEEAQKAVSE MNGKEVNGRM IYVGRAQKRI ERQSELKRKF EQIKQERINR YQGVNLYVKN
LDDGIDDDRL RKEFLPYGTI TSAKVMTEGG HSKGFGFVCF SSPEEATKAV TEMNGRIVST
KPLYVALAQR KEERKAILTN QYMQRLATMR AMPGPLLGSF QQPANYFLSA MPQPPNRTFY
SPNPVAPVRP APQWASHQSR PPQYQPPTPL MRAVQPRRMS SNISTMKQAS TQVPRVAQHS
QRVANIGTQT AGARAQVNPS MMRTMPHYKY SCGVRNVQPI VSSTHLQQVM EPAVLMQGQE
PLTASLLAGA PPQEQKQMLG ERIYPVIHEM HPTLAGKITG MLLEIDNSEL LHMLESPESL
HSKVEEAVAV LQAHQAKENA QKSAQPSLI
