PAIP1_XENLA
ID PAIP1_XENLA Reviewed; 463 AA.
AC Q7ZYB4; Q0IHK4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 1;
DE Short=PABP-interacting protein 1;
DE Short=PAIP-1;
DE Short=Paip1 protein;
DE Short=Poly(A)-binding protein-interacting protein 1;
DE AltName: Full=XlPaip1;
GN Name=paip1 {ECO:0000250|UniProtKB:Q9H074};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH43861.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH43861.1}, and Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP INTERACTION WITH EPABP.
RX PubMed=15713657; DOI=10.1128/mcb.25.5.2060-2071.2005;
RA Wilkie G.S., Gautier P., Lawson D., Gray N.K.;
RT "Embryonic poly(A)-binding protein stimulates translation in germ cells.";
RL Mol. Cell. Biol. 25:2060-2071(2005).
CC -!- FUNCTION: Acts as a coactivator in the regulation of translation
CC initiation of poly(A)-containing mRNAs. {ECO:0000250|UniProtKB:Q9H074}.
CC -!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminal regions of epabp.
CC {ECO:0000269|PubMed:15713657}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H074,
CC ECO:0000305}.
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DR EMBL; BC043861; AAH43861.1; -; mRNA.
DR EMBL; BC123119; AAI23120.1; -; mRNA.
DR RefSeq; NP_001080531.1; NM_001087062.1.
DR AlphaFoldDB; Q7ZYB4; -.
DR SMR; Q7ZYB4; -.
DR MaxQB; Q7ZYB4; -.
DR DNASU; 380223; -.
DR GeneID; 380223; -.
DR KEGG; xla:380223; -.
DR CTD; 380223; -.
DR Xenbase; XB-GENE-866621; paip1.S.
DR OrthoDB; 1384163at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 380223; Expressed in ovary and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008494; F:translation activator activity; ISS:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 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..463
FT /note="Polyadenylate-binding protein-interacting protein 1"
FT /id="PRO_0000233952"
FT DOMAIN 145..362
FT /note="MIF4G"
FT /evidence="ECO:0000255"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 51223 MW; 5ED498040677D5EE CRC64;
MSDGFERAPG VGRGRGRGRG IETAEGGKTP GFSGASGAGD EPGRAKAAGS QQQEPLRPPR
TGPPGGGGDA GAAQTSHKRT SPAAQLPAHT YTMAVSKAQP ADRGRLLSNL SANAAEFYPS
GYSVEANNCV EENGCYPVLP EGTLTEYVQD FLNHLTEQPG SFEAEVFPFS DVLNNCVTTD
ESLQELVELI YQQAISVPNF SYTGARLCNY LSNNLHINPQ NQNFRQLLLK RCQTEFEKRD
QAAKGDGAAR KQFHAFVLFL GELYLNLEIK GAKGQVTRAE ILQSGLQELL NSLFSNPVDD
NLMCAVKLLK LTGSVLEDAW KEKALSCMEE VMLRMKNVVL DANCSRDVKQ MLLKLVELRS
SNWGRVHAAS TFKEATPEND PNYFMNEPTF YTSEGVPFTA ADPDYQEKYQ ELLDREDFFR
DYDENGTDGG DSYFEDDDDN EMDPEMEEAY EKFCLESEHK KKQ