PABP1_PONAB
ID PABP1_PONAB Reviewed; 636 AA.
AC Q5R8F7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Polyadenylate-binding protein 1;
DE Short=PABP-1;
DE Short=Poly(A)-binding protein 1;
GN Name=PABPC1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds the poly(A) tail of mRNA, including that of its own
CC transcript, and regulates processes of mRNA metabolism such as pre-mRNA
CC splicing and mRNA stability. Its function in translational initiation
CC regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can
CC probably bind to cytoplasmic RNA sequences other than poly(A) in vivo.
CC Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to
CC MYC stability by binding to m6A-containing MYC mRNAs. Involved in
CC translationally coupled mRNA turnover. Implicated with other RNA-
CC binding proteins in the cytoplasmic deadenylation/translational and
CC decay interplay of the FOS mRNA mediated by the major coding-region
CC determinant of instability (mCRD) domain. Involved in regulation of
CC nonsense-mediated decay (NMD) of mRNAs containing premature stop
CC codons; for the recognition of premature termination codons (PTC) and
CC initiation of NMD a competitive interaction between UPF1 and PABPC1
CC with the ribosome-bound release factors is proposed. By binding to long
CC poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and
CC hence contribute to mRNA stability. {ECO:0000250|UniProtKB:P11940}.
CC -!- SUBUNIT: May form homodimers. Component of a multisubunit
CC autoregulatory ribonucleoprotein complex (ARC), at least composed of
CC IGF2BP1, PABPC1 and CSDE1. Directly interacts with IGF2BP1. Part of a
CC complex associated with the FOS mCRD domain and consisting of HNRPD,
CC SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with PAIP1 and PAIP2 (via the
CC PABPC1-interacting motifs PAM1 and PAM2). Interacts with PAIP1 with a
CC 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. The
CC interaction with CSDE1 is direct and RNA-independent (By similarity).
CC Found in a mRNP complex with YBX2. Interacts with TENT2/GLD2 (By
CC similarity). Identified in the spliceosome C complex. Identified in a
CC mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
CC IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1.
CC The interaction with DDX3X is direct and RNA-independent. This
CC interaction increases in stressed cells and decreases during cell
CC recovery. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with NXF1/TAP (By similarity).
CC Interacts with PIWIL1 (By similarity). Interacts with AGO1, AGO2, GSPT1
CC and GSPT2. Interacts with LARP4B. Interacts (via the second and third
CC RRM domains and the C-terminus) with PAIP2B (via central acidic portion
CC and C-terminus). Forms a complex with LARP1 and SHFL. Interacts with
CC LARP4. Interacts with ZFC3H1 in a RNase-sensitive manner. Interacts
CC with TRIM71 (via NHL repeats) in an RNA-dependent manner. Interacts
CC with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase
CC function. Interacts with G3BP1 and G3BP2 (By similarity). Interacts
CC with ENDOV; the interaction is RNA-dependent and stimulates ENDOV
CC activity (By similarity). Interacts with UPF1; the interaction is RNA-
CC dependent (By similarity). Interacts with IGF2BP2 and IGF2BP3. May
CC interact with SETX. {ECO:0000250|UniProtKB:P11940,
CC ECO:0000250|UniProtKB:P29341}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11940}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P11940}. Nucleus
CC {ECO:0000250|UniProtKB:P11940}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs (By similarity). Shuttles
CC between the cytoplasm and the nucleus (By similarity). During stress
CC and in the absence of DDX3X, localizes to the nucleus (By similarity).
CC At the leading edge of migrating fibroblasts, colocalizes with DDX3X
CC (By similarity). Relocalizes to cytoplasmic stress granules upon
CC cellular stress where it colocalizes with ENDOV (By similarity).
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus (last
CC 138 amino acids) regions interact respectively with the PABPC1-
CC interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus (last
CC 138 amino acids) regions interact with the PABPC1-interacting motif-1
CC (PAM1) and -2 (PAM2) of PAIP2, respectively.
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- PTM: Phosphorylated by MAPKAPK2. {ECO:0000250|UniProtKB:P11940}.
CC -!- PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to
CC asymmetric dimethylarginine (By similarity).
CC {ECO:0000250|UniProtKB:P11940}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; CR859795; CAH91953.1; -; mRNA.
DR RefSeq; NP_001128842.1; NM_001135370.1.
DR AlphaFoldDB; Q5R8F7; -.
DR BMRB; Q5R8F7; -.
DR SMR; Q5R8F7; -.
DR STRING; 9601.ENSPPYP00000021076; -.
DR PRIDE; Q5R8F7; -.
DR GeneID; 100189758; -.
DR KEGG; pon:100189758; -.
DR eggNOG; KOG0123; Eukaryota.
DR InParanoid; Q5R8F7; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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:0008380; P:RNA splicing; 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 Acetylation; Cell projection; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..636
FT /note="Polyadenylate-binding protein 1"
FT /id="PRO_0000292662"
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 542..619
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 166..289
FT /note="CSDE1-binding"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 299
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 385
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 436
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 455
FT /note="Omega-N-methylated arginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 460
FT /note="Omega-N-methylated arginine; by CARM1"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P29341"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 493
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 493
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 493
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 506
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
FT MOD_RES 518
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P11940"
SQ SEQUENCE 636 AA; 70643 MW; 10E58CD9FC536A2A CRC64;
MNPSAPSYPM ASLYVGDLHP DATEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE
AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA
AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ
RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ
GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
