ID PUM2_MOUSE Reviewed; 1066 AA. AC Q80U58; Q80UZ9; Q91YW4; Q925A0; Q9ERC7; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 02-FEB-2004, sequence version 2. DT 16-APR-2014, entry version 99. DE RecName: Full=Pumilio homolog 2; GN Name=Pum2; Synonyms=Kiaa0235; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6; RX PubMed=11780640; RA White E.K., Moore-Jarrett T., Ruley H.E.; RT "PUM2, a novel murine puf protein, and its consensus RNA-binding RT site."; RL RNA 7:1855-1866(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=12667987; DOI=10.1016/S1079-9796(03)00003-2; RA Spassov D.S., Jurecic R.; RT "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA- RT binding proteins, show differential expression in fetal and adult RT hematopoietic stem cells and progenitors."; RL Blood Cells Mol. Dis. 30:55-69(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH NANOS3, AND TISSUE SPECIFICITY. RX PubMed=18089289; DOI=10.1016/j.ydbio.2007.11.011; RA Lolicato F., Marino R., Paronetto M.P., Pellegrini M., Dolci S., RA Geremia R., Grimaldi P.; RT "Potential role of Nanos3 in maintaining the undifferentiated RT spermatogonia population."; RL Dev. Biol. 313:725-738(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=19861488; DOI=10.1530/REP-09-0373; RA Yamaji M., Tanaka T., Shigeta M., Chuma S., Saga Y., Saitou M.; RT "Functional reconstruction of NANOS3 expression in the germ cell RT lineage by a novel transgenic reporter reveals distinct subcellular RT localizations of NANOS3."; RL Reproduction 139:381-393(2010). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 706-1056. RX PubMed=19540345; DOI=10.1016/j.jsb.2009.06.007; RA Jenkins H.T., Baker-Wilding R., Edwards T.A.; RT "Structure and RNA binding of the mouse Pumilio-2 Puf domain."; RL J. Struct. Biol. 167:271-276(2009). CC -!- FUNCTION: Sequence-specific RNA-binding protein that negatively CC regulates translation and mRNA stability by binding the 3'-UTR of CC mRNA targets. Binds to an RNA consensus sequence, the Pumilio CC Response Element (PRE), 5'-UGUANAUA-3', that is related to the CC Nanos Response Element (NRE). Capable of deadenylation-dependent CC and -independent modes of repression. May be required to support CC proliferation and self-renewal of stem cells (By similarity). CC -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ, CC DAZL and NANOS1 via its pumilio repeats. Interacts with SNAPIN. CC Recruits the CCR4-POP2-NOT deadenylase leading to translational CC inhibition and mRNA degradation (By similarity). Interacts with CC NANOS3. Interacts with DDX20 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Cytoplasmic granule. CC Cytoplasm, perinuclear region (By similarity). Note=The CC cytoplasmic granules are stress granules which are a dense CC aggregation in the cytosol composed of proteins and RNAs that CC appear when the cell is under stress. Colocalizes with NANOS1 and CC SNAPIN in the perinuclear region of germ cells (By similarity). CC Colocalizes with NANOS3 in the stress granules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q80U58-1; Sequence=Displayed; CC Name=2; CC IsoId=Q80U58-2; Sequence=VSP_009322, VSP_009323; CC Name=3; CC IsoId=Q80U58-3; Sequence=VSP_009321, VSP_009322, VSP_009323; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in embryonic stem CC cells, heart, kidney, lung, skin, intestine, spleen and thymus. CC Expressed at intermediate level in brain and liver. Weakly or not CC expressed in muscles and stomach. Expressed at various stages of CC myeloid and lymphoid cell development. In the testis expressed in CC the spermatogoni, spermatocytes, spermatids and Sertoli cells. CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by CC packing together to form a right-handed superhelix that CC approximates a half doughnut. RNA-binding occurs on the concave CC side of the surface (PubMed:19540345). CC -!- SIMILARITY: Contains 1 PUM-HD domain. CC -!- SIMILARITY: Contains 8 pumilio repeats. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65507.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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; AY027917; AAK21966.1; -; mRNA. DR EMBL; AF315590; AAG31805.1; -; mRNA. DR EMBL; AK122225; BAC65507.1; ALT_INIT; mRNA. DR EMBL; BC013765; AAH13765.1; -; mRNA. DR EMBL; BC041773; AAH41773.1; -; mRNA. DR RefSeq; NP_001153691.1; NM_001160219.1. DR RefSeq; NP_001153694.1; NM_001160222.1. DR RefSeq; NP_109648.2; NM_030723.2. DR RefSeq; XP_006515340.1; XM_006515277.1. DR RefSeq; XP_006515341.1; XM_006515278.1. DR RefSeq; XP_006515342.1; XM_006515279.1. DR RefSeq; XP_006515348.1; XM_006515285.1. DR UniGene; Mm.341243; -. DR PDB; 3GVO; X-ray; 1.60 A; A=706-1056. DR PDB; 3GVT; X-ray; 2.80 A; A/B=706-1056. DR PDBsum; 3GVO; -. DR PDBsum; 3GVT; -. DR ProteinModelPortal; Q80U58; -. DR SMR; Q80U58; 706-1049. DR BioGrid; 219850; 2. DR IntAct; Q80U58; 3. DR PhosphoSite; Q80U58; -. DR PaxDb; Q80U58; -. DR PRIDE; Q80U58; -. DR Ensembl; ENSMUST00000163569; ENSMUSP00000131074; ENSMUSG00000020594. [Q80U58-1] DR Ensembl; ENSMUST00000168361; ENSMUSP00000128292; ENSMUSG00000020594. [Q80U58-1] DR Ensembl; ENSMUST00000169089; ENSMUSP00000132122; ENSMUSG00000020594. [Q80U58-2] DR Ensembl; ENSMUST00000178015; ENSMUSP00000137020; ENSMUSG00000020594. [Q80U58-2] DR GeneID; 80913; -. DR KEGG; mmu:80913; -. DR UCSC; uc007mzw.2; mouse. [Q80U58-3] DR UCSC; uc007mzy.2; mouse. [Q80U58-1] DR UCSC; uc007naa.2; mouse. [Q80U58-2] DR CTD; 23369; -. DR MGI; MGI:1931751; Pum2. DR eggNOG; COG5099; -. DR GeneTree; ENSGT00390000017241; -. DR HOGENOM; HOG000238461; -. DR HOVERGEN; HBG049462; -. DR InParanoid; Q80U58; -. DR KO; K17943; -. DR OMA; LFDYSSQ; -. DR OrthoDB; EOG7T7GT5; -. DR PhylomeDB; Q80U58; -. DR TreeFam; TF318160; -. DR ChiTaRS; PUM2; mouse. DR EvolutionaryTrace; Q80U58; -. DR NextBio; 350290; -. DR PRO; PR:Q80U58; -. DR ArrayExpress; Q80U58; -. DR Bgee; Q80U58; -. DR CleanEx; MM_PUM2; -. DR Genevestigator; Q80U58; -. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0034063; P:stress granule assembly; IDA:MGI. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR001313; Pumilio_RNA-bd_rpt. DR Pfam; PF00806; PUF; 8. DR SMART; SM00025; Pumilio; 8. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS50302; PUM; 8. DR PROSITE; PS50303; PUM_HD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; KW Translation regulation. FT CHAIN 1 1066 Pumilio homolog 2. FT /FTId=PRO_0000075920. FT DOMAIN 706 1048 PUM-HD. FT REPEAT 726 761 Pumilio 1. FT REPEAT 762 797 Pumilio 2. FT REPEAT 798 835 Pumilio 3. FT REPEAT 836 871 Pumilio 4. FT REPEAT 872 907 Pumilio 5. FT REPEAT 908 943 Pumilio 6. FT REPEAT 944 979 Pumilio 7. FT REPEAT 980 1022 Pumilio 8. FT REGION 1 260 Interaction with SNAPIN (By similarity). FT COMPBIAS 277 486 Ala-rich. FT COMPBIAS 358 404 Gln-rich. FT COMPBIAS 520 687 Ser-rich. FT MOD_RES 82 82 Phosphoserine (By similarity). FT MOD_RES 136 136 Phosphoserine. FT MOD_RES 177 177 Phosphoserine (By similarity). FT MOD_RES 181 181 Phosphoserine (By similarity). FT MOD_RES 183 183 Phosphothreonine (By similarity). FT MOD_RES 587 587 Phosphoserine (By similarity). FT VAR_SEQ 1 56 Missing (in isoform 3). FT /FTId=VSP_009321. FT VAR_SEQ 574 652 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_009322. FT VAR_SEQ 829 830 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_009323. FT CONFLICT 461 461 M -> I (in Ref. 3; BAC65507). FT CONFLICT 547 547 G -> A (in Ref. 2; AAG31805). FT CONFLICT 553 553 F -> C (in Ref. 2; AAG31805). FT CONFLICT 559 560 LG -> VR (in Ref. 2; AAG31805). FT CONFLICT 570 570 F -> C (in Ref. 2; AAG31805). FT CONFLICT 592 592 S -> A (in Ref. 2; AAG31805). FT CONFLICT 628 628 S -> G (in Ref. 2; AAG31805). FT HELIX 709 715 FT HELIX 724 727 FT TURN 728 730 FT HELIX 731 735 FT HELIX 738 748 FT HELIX 753 763 FT HELIX 764 766 FT HELIX 767 771 FT HELIX 776 786 FT HELIX 789 799 FT HELIX 803 807 FT HELIX 812 822 FT HELIX 825 828 FT HELIX 831 834 FT HELIX 835 837 FT HELIX 841 846 FT HELIX 850 860 FT HELIX 863 865 FT HELIX 867 872 FT TURN 873 876 FT HELIX 877 881 FT HELIX 886 896 FT HELIX 899 910 FT HELIX 913 917 FT HELIX 922 932 FT HELIX 935 943 FT TURN 944 947 FT HELIX 949 953 FT HELIX 958 968 FT HELIX 971 982 FT HELIX 991 997 FT HELIX 1001 1011 FT HELIX 1014 1024 FT HELIX 1025 1027 FT HELIX 1028 1031 FT TURN 1035 1037 FT HELIX 1038 1047 SQ SEQUENCE 1066 AA; 114314 MW; 027AC00FA91B055E CRC64; MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GTSHHSMSQP IMVQRRSGQS FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGTFGTRD AETDGPEKGD QKGKASPFEE DQNRDLKQDD EDSKINGRGL PNGMDADCKD FNRTPGSRQA SPTEVVERLG PSTNPPEGLG PLPNPTANKP LVEEFSNPET QNLDAMDQVG LDSLQFDYPG NQVPMDSSGA TVGLFDYNSQ QQLFQRTSAL TVQQLTAAQQ QQYALAAAQQ PHIAGVFSAG LAPAAFVPNP YIISAAPPGT DPYTAAGLAA AATLAGPAVV PPQYYGVPWG VYPANLFQQQ AAAAASNTAN QQAASQAQPG QQQVLRPGAG QRPITPSQGQ QGQQAESLAA AANPTLAFGQ SLAAGMPGYQ VLAPTAYYDQ TGALVVGPGA RTGLGAPVRL MAPTPVLISS TAAQAAAAAA AAGGTANSLT GSTNGLFRPI GTQPPQQQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS HGPGQPGSAS LGFGSGSSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQIVF NEILQAAYQL MTDVFGNYVI QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML //