ID   PAIP2_BOVIN             Reviewed;         124 AA.
AC   Q3ZC67;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Polyadenylate-binding protein-interacting protein 2;
DE            Short=PABP-interacting protein 2;
DE            Short=PAIP-2;
DE            Short=Poly(A)-binding protein-interacting protein 2;
GN   Name=PAIP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a repressor in the regulation of translation
CC       initiation of poly(A)-containing mRNAs. Its inhibitory activity on
CC       translation is mediated via its action on PABPC1. Displaces the
CC       interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for
CC       binding to PABPC1. Its association with PABPC1 results in disruption of
CC       the cytoplasmic poly(A) RNP structure organization (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the second and third RRM domains and C-terminus
CC       regions of PABPC1 in a 2:1 stoichiometry. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) interferes with the
CC       binding of PABPC1 to poly(A) RNA and translation initiation.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:Q9BPZ3}.
CC   -!- SIMILARITY: Belongs to the PAIP2 family. {ECO:0000305}.
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DR   EMBL; BC102885; AAI02886.1; -; mRNA.
DR   RefSeq; NP_001029808.1; NM_001034636.2.
DR   AlphaFoldDB; Q3ZC67; -.
DR   BMRB; Q3ZC67; -.
DR   STRING; 9913.ENSBTAP00000010815; -.
DR   PaxDb; Q3ZC67; -.
DR   PRIDE; Q3ZC67; -.
DR   Ensembl; ENSBTAT00000010815; ENSBTAP00000010815; ENSBTAG00000008224.
DR   GeneID; 536619; -.
DR   KEGG; bta:536619; -.
DR   CTD; 51247; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008224; -.
DR   VGNC; VGNC:53573; PAIP2.
DR   eggNOG; ENOG502RZKX; Eukaryota.
DR   GeneTree; ENSGT00390000017284; -.
DR   HOGENOM; CLU_134152_0_0_1; -.
DR   InParanoid; Q3ZC67; -.
DR   OMA; NSTAWST; -.
DR   OrthoDB; 1624094at2759; -.
DR   TreeFam; TF326855; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008224; Expressed in adenohypophysis and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:InterPro.
DR   GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IEA:Ensembl.
DR   GO; GO:1900271; P:regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:Ensembl.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR040396; PAIP2-like.
DR   PANTHER; PTHR13154; PTHR13154; 1.
DR   Pfam; PF07145; PAM2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Translation regulation; Ubl conjugation.
FT   CHAIN           1..124
FT                   /note="Polyadenylate-binding protein-interacting protein 2"
FT                   /id="PRO_0000252686"
FT   REGION          22..75
FT                   /note="PABPC1-interacting motif-1 (PAM1)"
FT                   /evidence="ECO:0000250"
FT   REGION          105..120
FT                   /note="PABPC1-interacting motif-2 (PAM2)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  14700 MW;  937E5C6E22D62023 CRC64;
     MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC
     FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP
     GVKY