PAIP2_MOUSE
ID PAIP2_MOUSE Reviewed; 124 AA.
AC Q9D6V8; Q3UBH5; Q9DAW7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 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=BALB/cJ, and C57BL/6J;
RC TISSUE=Bone marrow, Placenta, Stomach, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=16804161; DOI=10.1261/rna.106506;
RA Berlanga J.J., Baass A., Sonenberg N.;
RT "Regulation of poly(A) binding protein function in translation:
RT Characterization of the Paip2 homolog, Paip2B.";
RL RNA 12:1556-1568(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 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 -!- TISSUE SPECIFICITY: Expressed at high levels in testis with expression
CC also detected in heart, brain, lung, liver, kidney, pancreas and small
CC intestine (at protein level). {ECO:0000269|PubMed:16804161}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005462; BAB24053.1; -; mRNA.
DR EMBL; AK009909; BAB26578.1; -; mRNA.
DR EMBL; AK146327; BAE27082.1; -; mRNA.
DR EMBL; AK150957; BAE29989.1; -; mRNA.
DR EMBL; AK169207; BAE40979.1; -; mRNA.
DR EMBL; AK169411; BAE41157.1; -; mRNA.
DR EMBL; BC010190; AAH10190.1; -; mRNA.
DR CCDS; CCDS29143.1; -.
DR RefSeq; NP_080696.1; NM_026420.2.
DR RefSeq; XP_011245289.1; XM_011246987.2.
DR RefSeq; XP_011245290.1; XM_011246988.2.
DR RefSeq; XP_011245291.1; XM_011246989.1.
DR RefSeq; XP_011245292.1; XM_011246990.2.
DR RefSeq; XP_017173461.1; XM_017317972.1.
DR RefSeq; XP_017173462.1; XM_017317973.1.
DR AlphaFoldDB; Q9D6V8; -.
DR BMRB; Q9D6V8; -.
DR STRING; 10090.ENSMUSP00000036021; -.
DR PhosphoSitePlus; Q9D6V8; -.
DR EPD; Q9D6V8; -.
DR MaxQB; Q9D6V8; -.
DR PaxDb; Q9D6V8; -.
DR PeptideAtlas; Q9D6V8; -.
DR PRIDE; Q9D6V8; -.
DR ProteomicsDB; 287767; -.
DR Antibodypedia; 26731; 197 antibodies from 25 providers.
DR Ensembl; ENSMUST00000041314; ENSMUSP00000036021; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000235210; ENSMUSP00000157936; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000235400; ENSMUSP00000157519; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000235476; ENSMUSP00000158496; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000236020; ENSMUSP00000157742; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000236414; ENSMUSP00000158248; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000236666; ENSMUSP00000158160; ENSMUSG00000037058.
DR Ensembl; ENSMUST00000236868; ENSMUSP00000157456; ENSMUSG00000037058.
DR GeneID; 67869; -.
DR KEGG; mmu:67869; -.
DR UCSC; uc008emj.1; mouse.
DR CTD; 51247; -.
DR MGI; MGI:1915119; Paip2.
DR VEuPathDB; HostDB:ENSMUSG00000037058; -.
DR eggNOG; ENOG502RZKX; Eukaryota.
DR GeneTree; ENSGT00390000017284; -.
DR HOGENOM; CLU_134152_0_0_1; -.
DR InParanoid; Q9D6V8; -.
DR OMA; NSTAWST; -.
DR OrthoDB; 1624094at2759; -.
DR PhylomeDB; Q9D6V8; -.
DR TreeFam; TF326855; -.
DR BioGRID-ORCS; 67869; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Paip2; mouse.
DR PRO; PR:Q9D6V8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D6V8; protein.
DR Bgee; ENSMUSG00000037058; Expressed in saccule of membranous labyrinth and 254 other tissues.
DR Genevisible; Q9D6V8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISO:MGI.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0030371; F:translation repressor activity; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IMP:MGI.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISO:MGI.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0006417; P:regulation of translation; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR040396; PAIP2-like.
DR PANTHER; PTHR13154; PTHR13154; 1.
DR Pfam; PF07145; PAM2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Translation regulation; Ubl conjugation.
FT CHAIN 1..124
FT /note="Polyadenylate-binding protein-interacting protein 2"
FT /id="PRO_0000058180"
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"
FT CONFLICT 30
FT /note="P -> T (in Ref. 1; BAB24053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 14700 MW; 0D1241C3F89C85D8 CRC64;
MKDPSRSSTS PSIINDDVII NGHSHEEDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC
FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP
GVKY
