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   24-JAN-2024, entry version 141.
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; 8.
DR   ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
DR   IntAct; Q8VE62; 1.
DR   STRING; 10090.ENSMUSP00000026520; -.
DR   iPTMnet; Q8VE62; -.
DR   PhosphoSitePlus; Q8VE62; -.
DR   SwissPalm; Q8VE62; -.
DR   EPD; Q8VE62; -.
DR   MaxQB; Q8VE62; -.
DR   PaxDb; 10090-ENSMUSP00000026520; -.
DR   PeptideAtlas; Q8VE62; -.
DR   ProteomicsDB; 294375; -.
DR   Pumba; Q8VE62; -.
DR   Antibodypedia; 10789; 235 antibodies from 27 providers.
DR   DNASU; 218693; -.
DR   Ensembl; ENSMUST00000026520.14; ENSMUSP00000026520.8; ENSMUSG00000025451.16.
DR   GeneID; 218693; -.
DR   KEGG; mmu:218693; -.
DR   UCSC; uc007rzc.2; mouse.
DR   AGR; MGI:2384993; -.
DR   CTD; 10605; -.
DR   MGI; MGI:2384993; Paip1.
DR   VEuPathDB; HostDB:ENSMUSG00000025451; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   GeneTree; ENSGT00940000153432; -.
DR   InParanoid; Q8VE62; -.
DR   OrthoDB; 92033at2759; -.
DR   PhylomeDB; Q8VE62; -.
DR   TreeFam; TF325625; -.
DR   Reactome; R-MMU-429947; Deadenylation of mRNA.
DR   BioGRID-ORCS; 218693; 6 hits in 77 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 249 other cell types or tissues.
DR   ExpressionAtlas; Q8VE62; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0044794; P:positive regulation by host of viral process; 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   GO; GO:0019081; P:viral translation; ISO:MGI.
DR   Gene3D; 1.25.40.180; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR23254; EIF4G DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR23254:SF15; POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF07145; PAM2; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; Q8VE62; MM.
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
//