PABPA_XENLA
ID PABPA_XENLA Reviewed; 633 AA.
AC P20965; Q7ZZV9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Polyadenylate-binding protein 1-A;
DE Short=PABP-1-A;
DE Short=Poly(A)-binding protein 1-A;
DE Short=xPABP1-A;
DE AltName: Full=Cytoplasmic poly(A)-binding protein 1-A;
GN Name=pabpc1-a; Synonyms=pabp, pabp1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=2761544; DOI=10.1128/mcb.9.6.2756-2760.1989;
RA Zelus B.D., Giebelhaus D.H., Eib D.W., Kenner K.A., Moon R.T.;
RT "Expression of the poly(A)-binding protein during development of Xenopus
RT laevis.";
RL Mol. Cell. Biol. 9:2756-2760(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=2209558; DOI=10.1002/j.1460-2075.1990.tb07582.x;
RA Nietfeld W., Mentzel H., Pieler T.;
RT "The Xenopus laevis poly(A) binding protein is composed of multiple
RT functionally independent RNA binding domains.";
RL EMBO J. 9:3699-3705(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1280105; DOI=10.1042/bj2870761;
RA Stambuk R.A., Moon R.T.;
RT "Purification and characterization of recombinant Xenopus poly(A)(+)-
RT binding protein expressed in a baculovirus system.";
RL Biochem. J. 287:761-766(1992).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8631310; DOI=10.1002/j.1460-2075.1996.tb00424.x;
RA Wormington M., Searfoss A.M., Hurney C.A.;
RT "Overexpression of poly(A) binding protein prevents maturation-specific
RT deadenylation and translational inactivation in Xenopus oocytes.";
RL EMBO J. 15:900-909(1996).
RN [6]
RP INTERACTION WITH EIF4G1.
RX PubMed=10996799; DOI=10.1016/s0960-9822(00)00701-6;
RA Wakiyama M., Imataka H., Sonenberg N.;
RT "Interaction of eIF4G with poly(A)-binding protein stimulates translation
RT and is critical for Xenopus oocyte maturation.";
RL Curr. Biol. 10:1147-1150(2000).
RN [7]
RP INTERACTION WITH EIF4G1 AND PAIP1.
RX PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
RA Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
RT "Multiple portions of poly(A)-binding protein stimulate translation in
RT vivo.";
RL EMBO J. 19:4723-4733(2000).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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 [9]
RP FUNCTION, INTERACTION WITH SUP35, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP 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 [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH EPABP.
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).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA. Prevents mRNA deadenylation
CC and confers poly(A) stability. Binds to N6-methyladenosine (m6A)-
CC containing mRNAs (By similarity). Stimulates the translation of mRNAs
CC to which it is bound, acting, at least in part, with dazl.
CC {ECO:0000250|UniProtKB:P11940, ECO:0000269|PubMed:11274061,
CC ECO:0000269|PubMed:12489691, ECO:0000269|PubMed:1280105,
CC ECO:0000269|PubMed:15713657, ECO:0000269|PubMed:2209558,
CC ECO:0000269|PubMed:8631310}.
CC -!- SUBUNIT: The C-terminus self-associates, interacts with dazl and
CC interacts with the C-terminus of epabp independently of RNA. RRM 1 and
CC RRM 2 interact with both eif4g1 and paip1, and the C-terminus also
CC interacts with paip1. Interaction with eif4g1 is necessary for
CC translation of mRNAs required for oocyte maturation. Interacts with the
CC translation termination factor sup35/erf3.
CC {ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:10996799,
CC ECO:0000269|PubMed:12489691, ECO:0000269|PubMed:15713657,
CC ECO:0000269|PubMed:16001084}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8631310}.
CC Note=Associated with polysomes.
CC -!- TISSUE SPECIFICITY: Detected in the adult brain, testis, lung, stomach
CC and heart. Expressed in the epithelial and fiber cells of the lens, and
CC in the epithelial and endothelial cells of the cornea. In the retina,
CC present in the inner but not outer segment of the photoreceptor.
CC {ECO:0000269|PubMed:12489691, ECO:0000269|PubMed:2761544}.
CC -!- DEVELOPMENTAL STAGE: Appears to be present at a low level during early
CC oogenesis, with levels decreasing before oocyte maturation. Levels
CC dramatically increase during embryonic development (at protein level).
CC {ECO:0000269|PubMed:11274061, ECO:0000269|PubMed:12489691,
CC ECO:0000269|PubMed:1280105, ECO:0000269|PubMed:2761544}.
CC -!- DOMAIN: RRM4, together with the C- and N-terminal regions, is
CC sufficient for RNA-binding. RRM 1 has no RNA-binding activity itself,
CC but improves discrimination between poly(A) and poly(U) in combination
CC with the other repeats.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:12489691 finds protein expression from early oogenesis
CC but earlier publications (PubMed:2761544, PubMed:1280105 and
CC PubMed:11274061) suggest that the protein is not present before at
CC least the blastula stage of embryos. {ECO:0000305}.
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DR EMBL; M27072; AAA60936.1; -; mRNA.
DR EMBL; X57483; CAA40721.1; -; Genomic_DNA.
DR EMBL; BC052100; AAH52100.1; -; mRNA.
DR PIR; A32323; DNXLPA.
DR RefSeq; NP_001080204.1; NM_001086735.1.
DR AlphaFoldDB; P20965; -.
DR BMRB; P20965; -.
DR SMR; P20965; -.
DR PRIDE; P20965; -.
DR DNASU; 379896; -.
DR GeneID; 379896; -.
DR CTD; 379896; -.
DR Xenbase; XB-GENE-963463; pabpc1.S.
DR OMA; HQRINEC; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 379896; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; 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:0031047; P:gene silencing by RNA; ISS: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:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive 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 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding; Translation regulation.
FT CHAIN 1..633
FT /note="Polyadenylate-binding protein 1-A"
FT /id="PRO_0000081701"
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 540..617
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT CONFLICT 252
FT /note="N -> Y (in Ref. 1; AAA60936)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="K -> N (in Ref. 1; AAA60936)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="R -> S (in Ref. 2; CAA40721)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="S -> L (in Ref. 1; AAA60936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 70468 MW; 82DC11A6631EDBF1 CRC64;
MNPSAPSYPM ASLYVGDLHQ DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGR PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIDKMNG MLLNDRKVFV GRFKSRKERE
AELGARAKEF TNVYIKNFGD DMNDERLKEM FGKYGPALSV KVMTDDNGKS KGFGFVSFER
HEDAQKAVDE MNGKDMNGKS MFVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
LDDGIDDERL RKEFLPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTN QYMQRMASVR VPNPVINPYQ PPPSSYFMAA IPPAQNRAAY
YPPGQIAQLR PSPRWTAQGA RPHPFQNMPG AIRPTAPRPP TFSTMRPASN QVPRVMSAQR
VANTSTQTMG PRPTTAAAAA ASAVRAVPQY KYAAGVRNQQ HLNTQPQVAM QQPAVHVQGQ
EPLTASMLAA APPQEQKQML GERLFPLIQA MHPTLAGKIT GMLLEIDNSE LLHMLESPES
LRSKVDEAVA VLQAHQAKEA AQKVVNATGV PTA
