RENT2_MOUSE
ID RENT2_MOUSE Reviewed; 1269 AA.
AC A2AT37;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Regulator of nonsense transcripts 2 {ECO:0000250|UniProtKB:Q9HAU5};
DE AltName: Full=Up-frameshift suppressor 2 homolog {ECO:0000250|UniProtKB:P38798};
DE Short=Upf2;
GN Name=Upf2 {ECO:0000312|MGI:MGI:2449307};
GN Synonyms=RENT2 {ECO:0000250|UniProtKB:Q9HAU5};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI38359.1};
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] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=20657840; DOI=10.1371/journal.pone.0011650;
RA Thoren L.A., Noergaard G.A., Weischenfeldt J., Waage J., Jakobsen J.S.,
RA Damgaard I., Bergstroem F.C., Blom A.M., Borup R., Bisgaard H.C.,
RA Porse B.T.;
RT "UPF2 is a critical regulator of liver development, function and
RT regeneration.";
RL PLoS ONE 5:E11650-E11650(2010).
RN [5]
RP INTERACTION WITH UPF1, INTERACTION WITH MVH, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27149095; DOI=10.1371/journal.pgen.1005857;
RA Fanourgakis G., Lesche M., Akpinar M., Dahl A., Jessberger R.;
RT "Chromatoid Body Protein TDRD6 Supports Long 3' UTR Triggered Nonsense
RT Mediated mRNA Decay.";
RL PLoS Genet. 12:E1005857-E1005857(2016).
CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing
CC premature stop codons by associating with the nuclear exon junction
CC complex (EJC). Recruited by UPF3B associated with the EJC core at the
CC cytoplasmic side of the nuclear envelope and the subsequent formation
CC of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to
CC release factors at the stalled ribosome) is believed to activate NMD.
CC In cooperation with UPF3B stimulates both ATPase and RNA helicase
CC activities of UPF1. Binds spliced mRNA. {ECO:0000250|UniProtKB:Q9HAU5}.
CC -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP)
CC complex (By similarity). Associates with the exon junction complex
CC (EJC) (By similarity). Interacts with SMG1, EST1A, UPF3A, UPF3B, EIF4A1
CC and EIF1 (By similarity). Interacts with UPF1; interaction is promoted
CC by TDRD6 (PubMed:27149095). Interacts with DDX4 (PubMed:27149095).
CC {ECO:0000250|UniProtKB:Q9HAU5, ECO:0000269|PubMed:27149095}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9HAU5}. Cytoplasm
CC {ECO:0000269|PubMed:27149095}.
CC -!- TISSUE SPECIFICITY: Localized in male germ cells.
CC {ECO:0000269|PubMed:27149095}.
CC -!- DEVELOPMENTAL STAGE: Weakly expressed in neonatal testes and expression
CC increases during the development of spermatocytes and spermatids, in
CC the late meiotic and postmeiotic stages of spermatogenesis.
CC {ECO:0000269|PubMed:27149095}.
CC -!- DISRUPTION PHENOTYPE: Knockout adult liver results in hepatosteatosis
CC and disruption of liver homeostasis. {ECO:0000269|PubMed:20657840}.
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DR EMBL; AL928735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138358; AAI38359.1; -; mRNA.
DR EMBL; BC138359; AAI38360.1; -; mRNA.
DR CCDS; CCDS38041.1; -.
DR RefSeq; NP_001074601.1; NM_001081132.1.
DR RefSeq; XP_006497548.1; XM_006497485.3.
DR AlphaFoldDB; A2AT37; -.
DR SMR; A2AT37; -.
DR IntAct; A2AT37; 1.
DR STRING; 10090.ENSMUSP00000058375; -.
DR iPTMnet; A2AT37; -.
DR PhosphoSitePlus; A2AT37; -.
DR SwissPalm; A2AT37; -.
DR EPD; A2AT37; -.
DR jPOST; A2AT37; -.
DR MaxQB; A2AT37; -.
DR PaxDb; A2AT37; -.
DR PeptideAtlas; A2AT37; -.
DR PRIDE; A2AT37; -.
DR ProteomicsDB; 343380; -.
DR Antibodypedia; 24600; 172 antibodies from 26 providers.
DR Ensembl; ENSMUST00000060092; ENSMUSP00000058375; ENSMUSG00000043241.
DR GeneID; 326622; -.
DR KEGG; mmu:326622; -.
DR UCSC; uc008igc.1; mouse.
DR CTD; 26019; -.
DR MGI; MGI:2449307; Upf2.
DR VEuPathDB; HostDB:ENSMUSG00000043241; -.
DR eggNOG; KOG2051; Eukaryota.
DR GeneTree; ENSGT00530000064318; -.
DR HOGENOM; CLU_002633_2_1_1; -.
DR InParanoid; A2AT37; -.
DR OMA; DFQHHQI; -.
DR OrthoDB; 653534at2759; -.
DR PhylomeDB; A2AT37; -.
DR TreeFam; TF300543; -.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 326622; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Upf2; mouse.
DR PRO; PR:A2AT37; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AT37; protein.
DR Bgee; ENSMUSG00000043241; Expressed in ureter smooth muscle and 247 other tissues.
DR ExpressionAtlas; A2AT37; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; ISO:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR039762; Nmd2/UPF2.
DR InterPro; IPR007193; Upf2/Nmd2_C.
DR PANTHER; PTHR12839; PTHR12839; 1.
DR Pfam; PF02854; MIF4G; 3.
DR Pfam; PF04050; Upf2; 1.
DR SMART; SM00543; MIF4G; 3.
DR SUPFAM; SSF48371; SSF48371; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1269
FT /note="Regulator of nonsense transcripts 2"
FT /id="PRO_0000448685"
FT DOMAIN 168..396
FT /note="MIF4G 1"
FT /evidence="ECO:0000255"
FT DOMAIN 571..755
FT /note="MIF4G 2"
FT /evidence="ECO:0000255"
FT DOMAIN 774..984
FT /note="MIF4G 3"
FT /evidence="ECO:0000255"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..132
FT /note="Sufficient for interaction with UPF1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..926
FT /note="Sufficient for interaction with UPF3A and UPF3B"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 755..1269
FT /note="Sufficient for interaction with EIF4A1 and EIF1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 837..857
FT /note="Binds to UPF3B"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 1017..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1269
FT /note="Sufficient for interaction with UPF1 C-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 1102..1195
FT /note="Necessary for interaction with UPF1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 1102..1126
FT /note="Interaction with UPF1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 1164..1204
FT /note="Interaction with UPF1"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
FT REGION 1218..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..133
FT /evidence="ECO:0000255"
FT COMPBIAS 487..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1075
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1085
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAU5"
SQ SEQUENCE 1269 AA; 147553 MW; E95314FDF923F01E CRC64;
MPAERKKSAS MEEKESLLNN KEKDCSERRP VSSKEKPRDD LKVTAKKEVS KVPEDKKKRL
EEDKRKKEDK ERKKKEEEKV KAEEELKKKE EEEKKKQEEE ERKKQEEQAK RQQEEAAAQL
KEKEESLQLH QEAWERHQLR KELRSKNQNA PDNRPEENFF SRLDSSLKKN TAFVKKLKTI
TEQQRDSLSH DFNGLNLSKY IAEAVASIVE AKLKLSDVNC AAHLCSLFHQ RYSDFAPSLL
QVWKKHFEAR KEEKTPNITK LRTDLRFIAE LTIVGIFTDK EGLSLIYEQL KSIINADRES
HTHVSVVISF CRHCGDDIAG LVPRKVKSAA EKFNLSFPPS EIISPEKQQP FQNLLKEYFT
SLTKHLKRDH RELQNTERQN RRILHSKGEL SEDRHKQYEE FAMSYQKLLA NSQSLADLLD
ENMPDLPQDK PTPEEHGPGI DIFTPGKPGE YDLEGGIWED EDARNFYENL IDLKAFVPAI
LFKDNEKSQN KDSNKDDSKE AKEPKDNKEA SSPDDLELEL ENLEINDDTL ELEGADEAED
LTKKLLDEQE QEDEEASTGS HLKLIVDAFL QQLPNCVNRD LIDKAAMDFC MNMNTKANRK
KLVRALFIVP RQRLDLLPFY ARLVATLHPC MSDVAEDLCS MLRGDFRFHV RKKDQINIET
KNKTVRFIGE LTKFKMFTKN DTLHCLKMLL SDFSHHHIEM ACTLLETCGR FLFRSPESHL
RTSVLLEQMM RKKQAMHLDA RYVTMVENAY YYCNPPPAEK TVRKKRPPLQ EYVRKLLYKD
LSKVTTEKVL RQMRKLPWQD QEVKDYVICC MINIWNVKYN SIHCVANLLA GLVLYQEDVG
IHVVDGVLED IRLGMEVNQP KFNQRRISSA KFLGELYNYR MVESAVIFRT LYSFTSFGVN
PDGSPSSLDP PEHLFRIRLV CTILDTCGQY FDRGSSKRKL DCFLVYFQRY VWWKKSLEVW
TKDHPFPIDI DYMISDTLEL LRPKIKLCNS LEESIRQVQD LEREFLIKLG LVNDKESKDS
MTEGENLEED EEEEEGGAET EEQSGNESEV NEPEEEEGSE EEEEGEEEEE ENTDYLTDSN
KENETDEENA EVMIKGGGLK HVPCVEDEDF IQALDKMMLE NLQQRSGESV KVHQLDVAIP
LHLKSQLRKG PPLGGGEGET ESADTMPFVM LTRKGNKQQF KILNVPMSSQ LAANHWNQQQ
AEQEERMRMK KLTLDINERQ EQEDYQEMLQ SLAQRPAPAN TNRERRPRYQ HPKGAPNADL
IFKTGGRRR
