PABPA_DANRE
ID PABPA_DANRE Reviewed; 634 AA.
AC F1QB54; Q499B6; Q6P5M4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Polyadenylate-binding protein 1A;
DE Short=PABP-1A;
DE Short=Poly(A)-binding protein 1A;
GN Name=pabpc1a {ECO:0000312|ZFIN:ZDB-GENE-030131-3238};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH99992.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH YBX1.
RX PubMed=31399345; DOI=10.1016/j.molcel.2019.06.033;
RA Yang Y., Wang L., Han X., Yang W.L., Zhang M., Ma H.L., Sun B.F., Li A.,
RA Xia J., Chen J., Heng J., Wu B., Chen Y.S., Xu J.W., Yang X., Yao H.,
RA Sun J., Lyu C., Wang H.L., Huang Y., Sun Y.P., Zhao Y.L., Meng A., Ma J.,
RA Liu F., Yang Y.G.;
RT "RNA 5-methylcytosine facilitates the maternal-to-zygotic transition by
RT preventing maternal mRNA decay.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Binds the poly(A) tail of mRNA (By similarity). Prevents mRNA
CC deadenylation and confers poly(A) stability (By similarity). Binds to
CC N6-methyladenosine (m6A)-containing mRNAs (By similarity). Stimulates
CC the translation of mRNAs to which it is bound, acting, at least in
CC part, with dazl (By similarity). Involved in the maternal-to-zygotic
CC transition in early embryo via interaction with ybx1: interaction
CC recruits pabpc1a on C5-methylcytosine (m5C)-containing maternal mRNAs,
CC preventing their degradation (PubMed:31399345).
CC {ECO:0000250|UniProtKB:P11940, ECO:0000250|UniProtKB:P20965,
CC ECO:0000269|PubMed:31399345}.
CC -!- SUBUNIT: Interacts with ybx1; interaction recruits pabpc1a on C5-
CC methylcytosine (m5C)-containing mRNAs, preventing their degradation.
CC {ECO:0000269|PubMed:31399345}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20965}.
CC Note=Associated with polysomes. {ECO:0000250|UniProtKB:P20965}.
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. {ECO:0000250|UniProtKB:P20965}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000255|RuleBase:RU362004}.
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DR EMBL; CU855877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062832; AAH62832.1; -; mRNA.
DR EMBL; BC099992; AAH99992.1; -; mRNA.
DR RefSeq; NP_001026846.1; NM_001031676.1.
DR RefSeq; XP_005169828.1; XM_005169771.3.
DR AlphaFoldDB; F1QB54; -.
DR SMR; F1QB54; -.
DR IntAct; F1QB54; 1.
DR MINT; F1QB54; -.
DR STRING; 7955.ENSDARP00000021064; -.
DR PaxDb; F1QB54; -.
DR PRIDE; F1QB54; -.
DR Ensembl; ENSDART00000024729; ENSDARP00000021064; ENSDARG00000017219.
DR Ensembl; ENSDART00000148392; ENSDARP00000124828; ENSDARG00000017219.
DR GeneID; 606498; -.
DR KEGG; dre:606498; -.
DR CTD; 606498; -.
DR ZFIN; ZDB-GENE-030131-3238; pabpc1a.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000160311; -.
DR HOGENOM; CLU_012062_22_2_1; -.
DR InParanoid; F1QB54; -.
DR OMA; HNESLKA; -.
DR OrthoDB; 1027234at2759; -.
DR PhylomeDB; F1QB54; -.
DR TreeFam; TF300458; -.
DR Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DRE-429947; Deadenylation of mRNA.
DR Reactome; R-DRE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DRE-72649; Translation initiation complex formation.
DR Reactome; R-DRE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:F1QB54; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000017219; Expressed in early embryo and 36 other tissues.
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:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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..634
FT /note="Polyadenylate-binding protein 1A"
FT /id="PRO_0000448384"
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 541..618
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT CONFLICT 522
FT /note="H -> R (in Ref. 2; AAH99992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 70734 MW; 94F6AA6A33D747EF CRC64;
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMMTRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGR PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETHEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE
AEMGARAKEF TNVYIKNFGE DMDDEKLKEI FCKYGPALSI RVMTDDSGKS KGFGFVSFER
HEDAQRAVDE MNGKEMNGKQ VYVGRAQKKG ERQTELKRKF EQMKQDRMTR YQGVNLYVKN
LDDGLDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTS QYMQRMASVR AVPNPVLNPY QPAPPSGYFM AAIPQAQNRA
AYYPTSQLAQ LRPSPRWATQ GVRPQHFQNM PNAAVRPSAP RPQTFNPVRP ASQVPRMMTS
QRMGSQAMGP RPAAAGAATG PAQVRGVPQY KYAPGVRNPQ QHMPTQPQVP MQQPAVHVQG
QEPLTASMLA AAPPQEQKQM LGERLFPLIQ NMHPSLAGKI TGMLLEIDNS ELLHMLESPE
SLRSKVDEAV AVLQAHQAKE AAQKSVPSPA VPAV
