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PAIP2_RAT
ID   PAIP2_RAT               Reviewed;         124 AA.
AC   Q6AXZ0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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; BC079261; AAH79261.1; -; mRNA.
DR   RefSeq; NP_001014170.1; NM_001014148.1.
DR   RefSeq; XP_008770266.1; XM_008772044.2.
DR   RefSeq; XP_008770270.1; XM_008772048.2.
DR   RefSeq; XP_017456481.1; XM_017600992.1.
DR   RefSeq; XP_017456482.1; XM_017600993.1.
DR   RefSeq; XP_017456484.1; XM_017600995.1.
DR   AlphaFoldDB; Q6AXZ0; -.
DR   BMRB; Q6AXZ0; -.
DR   STRING; 10116.ENSRNOP00000026989; -.
DR   jPOST; Q6AXZ0; -.
DR   PaxDb; Q6AXZ0; -.
DR   PRIDE; Q6AXZ0; -.
DR   GeneID; 361309; -.
DR   KEGG; rno:361309; -.
DR   UCSC; RGD:1359176; rat.
DR   CTD; 51247; -.
DR   RGD; 1359176; Paip2.
DR   VEuPathDB; HostDB:ENSRNOG00000019934; -.
DR   eggNOG; ENOG502RZKX; Eukaryota.
DR   HOGENOM; CLU_134152_0_0_1; -.
DR   InParanoid; Q6AXZ0; -.
DR   OMA; NSTAWST; -.
DR   OrthoDB; 1624094at2759; -.
DR   PhylomeDB; Q6AXZ0; -.
DR   TreeFam; TF326855; -.
DR   PRO; PR:Q6AXZ0; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000019934; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q6AXZ0; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:InterPro.
DR   GO; GO:0030371; F:translation repressor activity; ISO:RGD.
DR   GO; GO:0007613; P:memory; ISO:RGD.
DR   GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR   GO; GO:0045947; P:negative regulation of translational initiation; ISO:RGD.
DR   GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0006417; P:regulation of translation; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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_0000252688"
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   124 AA;  14700 MW;  0D1241C3F89C85D8 CRC64;
     MKDPSRSSTS PSIINDDVII NGHSHEEDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC
     FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP
     GVKY
 
 
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