PABP2_BOVIN
ID PABP2_BOVIN Reviewed; 306 AA.
AC Q28165; A3KN38;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Polyadenylate-binding protein 2;
DE Short=PABP-2;
DE Short=Poly(A)-binding protein 2;
DE AltName: Full=Nuclear poly(A)-binding protein 1;
DE AltName: Full=Poly(A)-binding protein II;
DE Short=PABII;
DE AltName: Full=Polyadenylate-binding nuclear protein 1;
GN Name=PABPN1; Synonyms=PAB2, PABP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187, RNA-BINDING,
RP FUNCTION IN PRE-MESSENGER POLYADENYLATION, SUBUNIT, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Aorta, Liver, Muzzle epithelium, and Thymus;
RX PubMed=7479061; DOI=10.1093/nar/23.20.4034;
RA Nemeth A., Krause S., Blank D., Jenny A., Jenoe P., Lustig A., Wahle E.;
RT "Isolation of genomic and cDNA clones encoding bovine poly(A) binding
RT protein II.";
RL Nucleic Acids Res. 23:4034-4041(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-135; 140-207; 214-243 AND 248-306, MASS SPECTROMETRY,
RP METHYLATION AT ARG-238; ARG-259; ARG-263; ARG-265; ARG-267; ARG-269;
RP ARG-277; ARG-279; ARG-287; ARG-289; ARG-291; ARG-294; ARG-296 AND ARG-298,
RP AND ACETYLATION AT ALA-2.
RX PubMed=10224081; DOI=10.1074/jbc.274.19.13229;
RA Smith J.J., Ruecknagel K.P., Schierhorn A., Tang J., Nemeth A., Linder M.,
RA Herschman H.R., Wahle E.;
RT "Unusual sites of arginine methylation in poly(A)-binding protein II and in
RT vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3.";
RL J. Biol. Chem. 274:13229-13234(1999).
RN [4]
RP PROTEIN SEQUENCE OF 2-306, STRUCTURAL ANALYSIS OF POLY-ALA EXTENSION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14627730; DOI=10.1110/ps.03214703;
RA Scheuermann T., Schulz B., Blume A., Wahle E., Rudolph R., Schwarz E.;
RT "Trinucleotide expansions leading to an extended poly-L-alanine segment in
RT the poly(A) binding protein PABPN1 cause fibril formation.";
RL Protein Sci. 12:2685-2692(2003).
RN [5]
RP FUNCTION.
RX PubMed=10481015; DOI=10.1093/nar/27.19.3771;
RA Benoit B., Nemeth A., Aulner N., Kuhn U., Simonelig M., Wahle E.,
RA Bourbon H.-M.;
RT "The Drosophila poly(A)-binding protein II is ubiquitous throughout
RT Drosophila development and has the same function in mRNA polyadenylation as
RT its bovine homolog in vitro.";
RL Nucleic Acids Res. 27:3771-3778(1999).
RN [6]
RP MUTAGENESIS OF TYR-175 AND PHE-215, INTERACTION WITH TRANSPORTIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10688363; DOI=10.1017/s1355838200991908;
RA Calado A., Kutay U., Kuehn U., Wahle E., Carmo-Fonseca M.;
RT "Deciphering the cellular pathway for transport of poly(A)-binding protein
RT II.";
RL RNA 6:245-256(2000).
RN [7]
RP FUNCTION IN PAPOLA STIMULATION, RNA-BINDING, HOMOOLIGOMERIZATION, AND
RP MUTAGENESIS OF TYR-175; LYS-213 AND PHE-215.
RX PubMed=12637556; DOI=10.1074/jbc.m209886200;
RA Kuehn U., Nemeth A., Meyer S., Wahle E.;
RT "The RNA binding domains of the nuclear poly(A)-binding protein.";
RL J. Biol. Chem. 278:16916-16925(2003).
RN [8]
RP FUNCTION IN PAPOLA STIMULATION, MUTAGENESIS OF LEU-119; GLU-120; ILE-122;
RP LYS-123; ALA-124; VAL-126; MET-129; GLU-131; ALA-133; LYS-135; LEU-136 AND
RP VAL-143, AND INTERACTION WITH PAPOLA.
RX PubMed=12853485; DOI=10.1093/emboj/cdg347;
RA Kerwitz Y., Kuehn U., Lilie H., Knoth A., Scheuermann T., Friedrich H.,
RA Schwarz E., Wahle E.;
RT "Stimulation of poly(A) polymerase through a direct interaction with the
RT nuclear poly(A) binding protein allosterically regulated by RNA.";
RL EMBO J. 22:3705-3714(2003).
CC -!- FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-
CC mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream
CC cleavage product (PubMed:7479061, PubMed:10481015). Stimulates poly(A)
CC polymerase (PAPOLA) conferring processivity on the poly(A) tail
CC elongation reaction and controls also the poly(A) tail length
CC (PubMed:12637556). Increases the affinity of poly(A) polymerase for RNA
CC (PubMed:12637556, PubMed:12853485). Is also present at various stages
CC of mRNA metabolism including nucleocytoplasmic trafficking and
CC nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to
CC synergistically activate E-box-mediated transcription through MYOD1 and
CC may regulate the expression of muscle-specific genes (By similarity).
CC Binds to poly(A) and to poly(G) with high affinity (PubMed:7479061,
CC PubMed:12637556). May protect the poly(A) tail from degradation
CC (PubMed:7479061). Subunit of the trimeric poly(A) tail exosome
CC targeting (PAXT) complex, a complex that directs a subset of long and
CC polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome
CC is fundamental for the degradation of RNA in eukaryotic nuclei.
CC Substrate targeting is facilitated by its cofactor MTREX, which links
CC to RNA-binding protein adapters (By similarity).
CC {ECO:0000250|UniProtKB:Q86U42, ECO:0000269|PubMed:12637556,
CC ECO:0000269|PubMed:12853485, ECO:0000269|PubMed:7479061}.
CC -!- SUBUNIT: Monomer and homooligomer. Binds RNA as a monomer and
CC oligomerizes when bound to poly(A). Associates in a ternary complex
CC with CPSF4 and NS/NS1 and interaction with NS/NS1, blocks nuclear
CC export of host cell mRNAs. Associates in a single complex with SKIP and
CC MYOD1 and interacts with SKIP in differentiated myocytes. Interacts
CC with NUDT21/CPSF5. Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Interacts with PAPOLA, but only
CC in presence of oligo(A) RNA. Interacts with transportin. May interact
CC with SETX. Interacts (via RRM domain and C-terminal arginine-rich
CC region) with ZFP36 (via hypophosphorylated form); this interaction
CC occurs in the nucleus in a RNA-independent manner, decreases in
CC presence of single-stranded poly(A) RNA-oligomer and in a p38-
CC dependent-manner and may down-regulated RNA poly(A) polymerase activity
CC (By similarity). Component of the poly(A) tail exosome targeting (PAXT)
CC complex composed of PABPN1, ZFC3H1 and MTREX. Interacts with ZFC3H1 in
CC a RNase-insensitive manner (By similarity). Interacts with FRG1 (By
CC similarity). {ECO:0000250|UniProtKB:Q86U42,
CC ECO:0000250|UniProtKB:Q8CCS6, ECO:0000269|PubMed:10688363,
CC ECO:0000269|PubMed:12853485, ECO:0000269|PubMed:7479061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10688363}. Cytoplasm
CC {ECO:0000269|PubMed:10688363}. Nucleus speckle
CC {ECO:0000269|PubMed:10688363}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs (By similarity). Shuttles
CC between the nucleus and the cytoplasm but predominantly found in the
CC nucleus. Its nuclear import may involve the nucleocytoplasmic transport
CC receptor transportin and a RAN-GTP-sensitive import mechanism
CC (PubMed:10688363). Is exported to the cytoplasm by a carrier-mediated
CC pathway that is independent of mRNA traffic. Nucleus; nuclear speckle.
CC Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By
CC similarity). {ECO:0000250|UniProtKB:Q86U42,
CC ECO:0000269|PubMed:10688363}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The RRM domain is essential for specific adenine bases
CC recognition in the poly(A) tail but not sufficient for poly(A) binding.
CC -!- PTM: Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3.
CC It does not influence the RNA binding properties.
CC -!- MASS SPECTROMETRY: Mass=33253; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10224081};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X89969; CAA62006.1; -; mRNA.
DR EMBL; BC133558; AAI33559.1; -; mRNA.
DR PIR; S59863; S59863.
DR RefSeq; NP_776994.1; NM_174569.2.
DR AlphaFoldDB; Q28165; -.
DR SMR; Q28165; -.
DR STRING; 9913.ENSBTAP00000021887; -.
DR iPTMnet; Q28165; -.
DR PaxDb; Q28165; -.
DR PRIDE; Q28165; -.
DR Ensembl; ENSBTAT00000021887; ENSBTAP00000021887; ENSBTAG00000006884.
DR GeneID; 282298; -.
DR KEGG; bta:282298; -.
DR CTD; 8106; -.
DR VEuPathDB; HostDB:ENSBTAG00000006884; -.
DR VGNC; VGNC:53575; PABPN1.
DR eggNOG; KOG4209; Eukaryota.
DR GeneTree; ENSGT00940000154606; -.
DR InParanoid; Q28165; -.
DR OMA; READEYE; -.
DR OrthoDB; 1412946at2759; -.
DR TreeFam; TF105907; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000006884; Expressed in granulosa cell and 100 other tissues.
DR ExpressionAtlas; Q28165; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034911; PABP2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23236:SF16; PTHR23236:SF16; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10224081,
FT ECO:0000269|PubMed:14627730"
FT CHAIN 2..306
FT /note="Polyadenylate-binding protein 2"
FT /id="PRO_0000081710"
FT DOMAIN 172..249
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..145
FT /note="Interaction with SKIP"
FT /evidence="ECO:0000250"
FT REGION 119..147
FT /note="Stimulates PAPOLA"
FT REGION 155..306
FT /note="Necessary for homooligomerization"
FT /evidence="ECO:0000250"
FT REGION 286..306
FT /note="Interaction with PAPOLA"
FT /evidence="ECO:0000269|PubMed:12853485"
FT COILED 115..151
FT /evidence="ECO:0000255"
FT COMPBIAS 51..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 17
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CCS6"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 238
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 238
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 259
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 259
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 263
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 263
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86U42"
FT MOD_RES 265
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 267
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 269
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 277
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 279
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 287
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 289
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 291
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 294
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 296
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MOD_RES 298
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:10224081"
FT MUTAGEN 119
FT /note="L->A: Strong defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 120
FT /note="E->A: No defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 122
FT /note="I->Q: Strong defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 123
FT /note="K->A: No defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 124
FT /note="A->S: Slight defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 126
FT /note="V->S: No defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 129
FT /note="M->A: Slight defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 131
FT /note="E->A: Slight defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 133
FT /note="A->S: No defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 135
FT /note="K->A: No defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 136
FT /note="L->A,S: Inactivates PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 143
FT /note="V->A: Slight defects in the stimulation of PAPOLA."
FT /evidence="ECO:0000269|PubMed:12853485"
FT MUTAGEN 175
FT /note="Y->A: At least 20% decrease in poly(A) binding; no
FT change in nuclear targeting; distributed uniformly in the
FT nucleoplasm; not detected in speckles. Same phenotypic
FT effect; when associated with A-215."
FT /evidence="ECO:0000269|PubMed:10688363,
FT ECO:0000269|PubMed:12637556"
FT MUTAGEN 213
FT /note="K->Q: No changes in poly(A) affinity."
FT /evidence="ECO:0000269|PubMed:12637556"
FT MUTAGEN 215
FT /note="F->A: At least 20% decrease in poly(A); binding; no
FT change in nuclear targeting, distributed uniformly in the
FT nucleoplasm; not detected in speckles. Same phenotypic
FT effect; when associated with A-175."
FT /evidence="ECO:0000269|PubMed:10688363,
FT ECO:0000269|PubMed:12637556"
SQ SEQUENCE 306 AA; 32766 MW; 11D5E5A555458246 CRC64;
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL
LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGNQEEEE ESGLVEGDPG DGAIEDPELE
AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD
YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR
QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT
SWYSPY
