ID   PAIP2_CHICK             Reviewed;         127 AA.
AC   Q5ZJS6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
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; ORFNames=RCJMB04_16b5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- 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; AJ720358; CAG32017.1; -; mRNA.
DR   RefSeq; NP_001007833.1; NM_001007832.1.
DR   AlphaFoldDB; Q5ZJS6; -.
DR   STRING; 9031.ENSGALP00000003912; -.
DR   PaxDb; Q5ZJS6; -.
DR   Ensembl; ENSGALT00000003921; ENSGALP00000003912; ENSGALG00000002488.
DR   Ensembl; ENSGALT00000096696; ENSGALP00000072610; ENSGALG00000002488.
DR   GeneID; 416187; -.
DR   KEGG; gga:416187; -.
DR   CTD; 400961; -.
DR   VEuPathDB; HostDB:geneid_416187; -.
DR   eggNOG; ENOG502RZKX; Eukaryota.
DR   GeneTree; ENSGT00390000017284; -.
DR   HOGENOM; CLU_134152_0_0_1; -.
DR   InParanoid; Q5ZJS6; -.
DR   OMA; NSTAWST; -.
DR   OrthoDB; 1624094at2759; -.
DR   PhylomeDB; Q5ZJS6; -.
DR   PRO; PR:Q5ZJS6; -.
DR   Proteomes; UP000000539; Chromosome 13.
DR   Bgee; ENSGALG00000002488; Expressed in testis and 12 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:InterPro.
DR   GO; GO:0030371; F:translation repressor activity; ISS:AgBase.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0045947; P:negative regulation of translational initiation; ISS:AgBase.
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..127
FT                   /note="Polyadenylate-binding protein-interacting protein 2"
FT                   /id="PRO_0000252689"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   127 AA;  15043 MW;  F3502EB5B070986B CRC64;
     MKDPSRSSTS PSIISEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC
     FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDSS SLEDLVVKSN LNPNAKEFVP
     GVKYLNI