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Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1)

 PABP1_BOVIN             Reviewed;         636 AA.
P61286; Q3T0J7;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Polyadenylate-binding protein 1;
Short=PABP-1;
Short=Poly(A)-binding protein 1;
Name=PABPC1; Synonyms=PABP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Holstein; TISSUE=Mammary gland;
AGRICOLA=IND23230985;
Kim J.H., Jeon D.H., Choi Y.J., Baik M.G.;
"Cloning and expression of bovine polyadenylate binding protein 1 cDNA
in mammary tissues.";
Asian-Australas. J. Anim. Sci. 14:771-776(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Binds the poly(A) tail of mRNA, including that of its
own transcript. May be involved in cytoplasmic regulatory
processes of mRNA metabolism such as pre-mRNA splicing. Its
function in translational initiation regulation can either be
enhanced by PAIP1 or repressed by PAIP2. Can probably bind to
cytoplasmic RNA sequences other than poly(A) in vivo. Involved in
translationally coupled mRNA turnover. Implicated with other RNA-
binding proteins in the cytoplasmic deadenylation/translational
and decay interplay of the FOS mRNA mediated by the major coding-
region determinant of instability (mCRD) domain. Involved in
regulation of nonsense-mediated decay (NMD) of mRNAs containing
premature stop codons; for the recognition of premature
termination codons (PTC) and initiation of NMD a competitive
interaction between UPF1 and PABPC1 with the ribosome-bound
release factors is proposed (By similarity). By binding to long
poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11
and hence contribute to mRNA stability (By similarity).
{ECO:0000250|UniProtKB:P11940}.
-!- SUBUNIT: Component of a multi subunit autoregulatory
ribonucleoprotein complex (ARC) with IGF2BP1, PABPC1 and CSDE1.
Directly interacts with IGF2BP1. Part of a complex associated with
the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and
CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1)
and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1
stoichiometry and with PAIP2 with a 1:2 stoichiometry. The
interaction with CSDE1 is direct and RNA-independent. Found in a
mRNP complex with YBX2. Interacts with TENT2/GLD2. Identified in
the spliceosome C complex. Identified in a mRNP complex, at least
composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Interacts with NFX1 and PIWIL1. Interacts with AGO1, AGO2,
GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. May interact
with SETX (By similarity). Interacts (via the second and third RRM
domains and the C-terminus) with PAIP2B (via central acidic
portion and C-terminus). Interacts with LARP1. Interacts with
RYDEN. Found in a complex with RYDEN and LARP1. Interacts with
LARP4 (By similarity). Interacts with ZFC3H1 in a RNase-sensitive
manner (By similarity). Interacts with TRIM71 (via NHL repeats) in
an RNA-dependent manner (By similarity). Interacts with TENT5C;
the interaction has no effect on TENT5C poly(A) polymerase
function (By similarity). {ECO:0000250|UniProtKB:P11940,
ECO:0000250|UniProtKB:P29341}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11940}.
Nucleus {ECO:0000250|UniProtKB:P11940}. Note=Localized in
cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles
between the cytoplasm and the nucleus (By similarity).
{ECO:0000250|UniProtKB:P11940}.
-!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus
(last 138 amino acids) regions interact with the PABPC1-
interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
{ECO:0000250|UniProtKB:P11940}.
-!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus
(last 138 amino acids) regions interact with the PABPC1-
interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.
{ECO:0000250|UniProtKB:P11940}.
-!- PTM: Phosphorylated by MAPKAPK2. {ECO:0000250|UniProtKB:P11940}.
-!- PTM: Methylated by CARM1. Arg-493 is dimethylated, probably to
asymmetric dimethylarginine (By similarity).
{ECO:0000250|UniProtKB:P11940}.
-!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ401269; CAB96752.1; -; mRNA.
EMBL; BC102365; AAI02366.1; -; mRNA.
RefSeq; NP_776993.1; NM_174568.2.
UniGene; Bt.53579; -.
ProteinModelPortal; P61286; -.
SMR; P61286; -.
IntAct; P61286; 1.
STRING; 9913.ENSBTAP00000056644; -.
PaxDb; P61286; -.
PeptideAtlas; P61286; -.
PRIDE; P61286; -.
Ensembl; ENSBTAT00000064237; ENSBTAP00000056644; ENSBTAG00000046358.
GeneID; 282296; -.
KEGG; bta:282296; -.
CTD; 26986; -.
VGNC; VGNC:53870; PABPC1.
eggNOG; KOG0123; Eukaryota.
eggNOG; ENOG410XR5X; LUCA.
GeneTree; ENSGT00760000118913; -.
HOVERGEN; HBG002295; -.
InParanoid; P61286; -.
KO; K13126; -.
OMA; RAAYYPA; -.
OrthoDB; EOG091G03ZE; -.
TreeFam; TF300458; -.
Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-BTA-429947; Deadenylation of mRNA.
Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
Proteomes; UP000009136; Chromosome 14.
Bgee; ENSBTAG00000046358; Expressed in 9 organ(s), highest expression level in testis.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
Gene3D; 3.30.70.330; -; 4.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR036053; PABP-dom.
InterPro; IPR006515; PABP_1234.
InterPro; IPR002004; PABP_HYD.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF00658; PABP; 1.
Pfam; PF00076; RRM_1; 4.
SMART; SM00517; PolyA; 1.
SMART; SM00360; RRM; 4.
SMART; SM00361; RRM_1; 3.
SUPFAM; SSF54928; SSF54928; 2.
SUPFAM; SSF63570; SSF63570; 1.
TIGRFAMs; TIGR01628; PABP-1234; 1.
PROSITE; PS51309; PABC; 1.
PROSITE; PS50102; RRM; 4.
2: Evidence at transcript level;
Acetylation; Complete proteome; Cytoplasm; Methylation;
mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus;
Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
CHAIN 1 636 Polyadenylate-binding protein 1.
/FTId=PRO_0000081697.
DOMAIN 11 89 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 99 175 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 191 268 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 294 370 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 542 619 PABC. {ECO:0000255|PROSITE-
ProRule:PRU00641}.
REGION 166 289 CSDE1-binding. {ECO:0000250}.
COMPBIAS 495 501 Poly-Ala.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 299 299 N6-methyllysine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 319 319 Phosphothreonine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 385 385 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 419 419 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 432 432 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 436 436 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 455 455 Omega-N-methylated arginine; by CARM1.
{ECO:0000250}.
MOD_RES 460 460 Omega-N-methylated arginine; by CARM1.
{ECO:0000250}.
MOD_RES 475 475 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P29341}.
MOD_RES 481 481 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 493 493 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 493 493 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 493 493 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 506 506 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 512 512 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11940}.
MOD_RES 518 518 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11940}.
SEQUENCE 636 AA; 70671 MW; 2EB1B02A346132EE CRC64;
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK 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


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