PAIP1_MOUSE
ID PAIP1_MOUSE Reviewed; 400 AA.
AC Q8VE62; Q9WUC9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 1;
DE Short=PABP-interacting protein 1;
DE Short=PAIP-1;
DE Short=Poly(A)-binding protein-interacting protein 1;
GN Name=Paip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-367.
RC STRAIN=CB6F1/J; TISSUE=Oocyte;
RA Paynton B.V.;
RT "Mouse oocyte polyA binding protein-interacting protein.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a coactivator in the regulation of translation
CC initiation of poly(A)-containing mRNAs. Its stimulatory activity on
CC translation is mediated via its action on PABPC1. Competes with PAIP2
CC for binding to PABPC1. Its association with EIF4A and PABPC1 may
CC potentiate contacts between mRNA termini. May also be 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of PABPC1
CC in a 1:1 stoichiometry. Interacts with EIF4A (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates
CC translation initiation. {ECO:0000250}.
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DR EMBL; BC019726; AAH19726.1; -; mRNA.
DR EMBL; BC051042; AAH51042.1; -; mRNA.
DR EMBL; AF128835; AAD28259.1; -; mRNA.
DR CCDS; CCDS26796.1; -.
DR RefSeq; NP_663432.1; NM_145457.4.
DR AlphaFoldDB; Q8VE62; -.
DR SMR; Q8VE62; -.
DR BioGRID; 230055; 7.
DR ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR IntAct; Q8VE62; 1.
DR STRING; 10090.ENSMUSP00000026520; -.
DR iPTMnet; Q8VE62; -.
DR PhosphoSitePlus; Q8VE62; -.
DR EPD; Q8VE62; -.
DR MaxQB; Q8VE62; -.
DR PaxDb; Q8VE62; -.
DR PeptideAtlas; Q8VE62; -.
DR PRIDE; Q8VE62; -.
DR ProteomicsDB; 294375; -.
DR Antibodypedia; 10789; 202 antibodies from 27 providers.
DR DNASU; 218693; -.
DR Ensembl; ENSMUST00000026520; ENSMUSP00000026520; ENSMUSG00000025451.
DR GeneID; 218693; -.
DR KEGG; mmu:218693; -.
DR UCSC; uc007rzc.2; mouse.
DR CTD; 10605; -.
DR MGI; MGI:2384993; Paip1.
DR VEuPathDB; HostDB:ENSMUSG00000025451; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000153432; -.
DR InParanoid; Q8VE62; -.
DR PhylomeDB; Q8VE62; -.
DR TreeFam; TF325625; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR BioGRID-ORCS; 218693; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Paip1; mouse.
DR PRO; PR:Q8VE62; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VE62; protein.
DR Bgee; ENSMUSG00000025451; Expressed in animal zygote and 246 other tissues.
DR ExpressionAtlas; Q8VE62; baseline and differential.
DR Genevisible; Q8VE62; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0106002; C:mCRD-mediated mRNA stability complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008494; F:translation activator activity; ISO:MGI.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF07145; PAM2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Translation regulation.
FT CHAIN 1..400
FT /note="Polyadenylate-binding protein-interacting protein 1"
FT /id="PRO_0000058178"
FT DOMAIN 80..297
FT /note="MIF4G"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..64
FT /note="PABPC1-interacting motif-2 (PAM2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H074"
FT REGION 78..296
FT /note="PAIP1 middle domain (PAIP1M)"
FT /evidence="ECO:0000250|UniProtKB:Q9H074"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..400
FT /note="PABPC1-interacting motif-1 (PAM1)"
FT /evidence="ECO:0000250|UniProtKB:Q9H074"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 42
FT /note="A -> V (in Ref. 2; AAD28259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 45702 MW; C5B8A18F068A5E6B CRC64;
MSDSFDRAPE QTKPQRAPPS SQDKIPQQNS ESAMAKPQVV VAPVLMSKLS ANAPEFYPSG
YSSNYTESYE DGCEDYPTLS EYVQDFLNHL TEQPGSFETE IEQFAETLNG WVTTDDALQE
LVELIYQQAT SIPNFSYMGA RLCNYLSHHL TISPQSGNFR QLLLQRCRTE YEAKDQAAKG
DEVTRKRFHA FVLFLGELYL NLEIKGTNGQ VTRADILQVG LRELLNALFS NPMDDNLICA
VKLLKLTGSV LEDTWKEKGK TDMEEIIQRI ENVVLDANCS RDVKQMLLKL VELRSSNWGR
VHATSTYREA TPENDPNYFM NEPTFYTSDG VPFTAADPDY QEKYQELLER EDFFPDYEEN
GTDLSGAGDP YLDDIDDEMD PEIEEAYEKF CLESERKRKQ
