NEMF_MOUSE
ID NEMF_MOUSE Reviewed; 1064 AA.
AC Q8CCP0; Q3TAS9; Q3UF46; Q66JX6; Q8C9R6; Q8CA65; Q8JZT9; Q8R072; Q9CW30;
AC Q9CYB8; Q9D4A9;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ribosome quality control complex subunit NEMF {ECO:0000305};
DE AltName: Full=Nuclear export mediator factor {ECO:0000312|MGI:MGI:1918305};
DE AltName: Full=Serologically defined colon cancer antigen 1 homolog;
GN Name=Nemf {ECO:0000312|MGI:MGI:1918305}; Synonyms=Sdccag1;
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] (ISOFORMS 1; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-438 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Embryo, Olfactory bulb, Spinal cord, Spleen,
RC Sympathetic ganglion, Testis, and Thymus;
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] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 687-1064 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-443 AND 855-1064 (ISOFORM 1).
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Embryo, Mammary tumor, and Retina;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-737, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [5]
RP MUTAGENESIS OF ARG-86; 106-ASP--LYS-1064 AND ARG-487.
RX PubMed=32934225; DOI=10.1038/s41467-020-18327-6;
RA Martin P.B., Kigoshi-Tansho Y., Sher R.B., Ravenscroft G., Stauffer J.E.,
RA Kumar R., Yonashiro R., Mueller T., Griffith C., Allen W., Pehlivan D.,
RA Harel T., Zenker M., Howting D., Schanze D., Faqeih E.A.,
RA Almontashiri N.A.M., Maroofian R., Houlden H., Mazaheri N., Galehdari H.,
RA Douglas G., Posey J.E., Ryan M., Lupski J.R., Laing N.G., Joazeiro C.A.P.,
RA Cox G.A.;
RT "NEMF mutations that impair ribosome-associated quality control are
RT associated with neuromuscular disease.";
RL Nat. Commun. 11:4625-4625(2020).
CC -!- FUNCTION: As part of the ribosome quality control complex (RQC), a
CC ribosome-associated complex, mediates the extraction of incompletely
CC synthesized nascent chains from stalled ribosomes as well as their
CC ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes
CC from the stalled translation complex and prevents the accumulation of
CC nascent polypeptide chains that are potentially toxic for the cell. It
CC is responsible both for selective recognition of stalled 60S subunits
CC by recognizing an exposed, nascent chain-conjugated tRNA moiety and the
CC recruitment of the E3 ubiquitin-protein ligase LTN1 to the ribosome
CC quality control complex. May indirectly play a role in nuclear export.
CC {ECO:0000250|UniProtKB:O60524}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of at least the E3 ubiquitin ligase LTN1 and NEMF associated
CC with the 60S ribosomal subunit. The complex probably also contains
CC TCF25 as well as VCP/p97 and its ubiquitin-binding cofactors. Interacts
CC (via its N-terminus) with Xpo1. {ECO:0000250|UniProtKB:O60524,
CC ECO:0000250|UniProtKB:Q12532}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CCP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCP0-2; Sequence=VSP_008397, VSP_008398;
CC Name=3;
CC IsoId=Q8CCP0-3; Sequence=VSP_010465, VSP_010466;
CC Name=4;
CC IsoId=Q8CCP0-4; Sequence=VSP_010463, VSP_010464;
CC -!- DOMAIN: The N-terminal domain contains a nuclear export signal. The C-
CC terminal domain may interact with cargo proteins (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27272.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53488.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53488.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB30366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB30366.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27849.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK005212; BAB23886.1; -; mRNA.
DR EMBL; AK016662; BAB30366.1; ALT_FRAME; mRNA.
DR EMBL; AK017826; BAB30959.1; -; mRNA.
DR EMBL; AK032388; BAC27849.1; ALT_SEQ; mRNA.
DR EMBL; AK039497; BAC30369.1; -; mRNA.
DR EMBL; AK041458; BAC30950.1; -; mRNA.
DR EMBL; AK089000; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK149005; BAE28715.1; -; mRNA.
DR EMBL; AK171652; BAE42589.1; -; mRNA.
DR EMBL; BC027272; AAH27272.1; ALT_INIT; mRNA.
DR EMBL; BC037106; AAH37106.2; -; mRNA.
DR EMBL; BC053488; AAH53488.2; ALT_FRAME; mRNA.
DR EMBL; BC080716; AAH80716.1; -; mRNA.
DR CCDS; CCDS25951.1; -. [Q8CCP0-1]
DR RefSeq; NP_079717.2; NM_025441.3. [Q8CCP0-1]
DR AlphaFoldDB; Q8CCP0; -.
DR SMR; Q8CCP0; -.
DR BioGRID; 211322; 2.
DR IntAct; Q8CCP0; 2.
DR MINT; Q8CCP0; -.
DR STRING; 10090.ENSMUSP00000021368; -.
DR iPTMnet; Q8CCP0; -.
DR PhosphoSitePlus; Q8CCP0; -.
DR EPD; Q8CCP0; -.
DR jPOST; Q8CCP0; -.
DR MaxQB; Q8CCP0; -.
DR PaxDb; Q8CCP0; -.
DR PeptideAtlas; Q8CCP0; -.
DR PRIDE; Q8CCP0; -.
DR ProteomicsDB; 252882; -. [Q8CCP0-1]
DR ProteomicsDB; 252883; -. [Q8CCP0-2]
DR ProteomicsDB; 252884; -. [Q8CCP0-3]
DR ProteomicsDB; 252885; -. [Q8CCP0-4]
DR Antibodypedia; 140; 219 antibodies from 29 providers.
DR DNASU; 66244; -.
DR Ensembl; ENSMUST00000021368; ENSMUSP00000021368; ENSMUSG00000020982. [Q8CCP0-1]
DR GeneID; 66244; -.
DR KEGG; mmu:66244; -.
DR UCSC; uc007nse.2; mouse. [Q8CCP0-1]
DR UCSC; uc007nsg.2; mouse. [Q8CCP0-3]
DR UCSC; uc007nsh.2; mouse. [Q8CCP0-4]
DR CTD; 9147; -.
DR MGI; MGI:1918305; Nemf.
DR VEuPathDB; HostDB:ENSMUSG00000020982; -.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00390000018516; -.
DR HOGENOM; CLU_003612_1_0_1; -.
DR InParanoid; Q8CCP0; -.
DR OMA; MGAWWVN; -.
DR OrthoDB; 131285at2759; -.
DR PhylomeDB; Q8CCP0; -.
DR TreeFam; TF300515; -.
DR BioGRID-ORCS; 66244; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Nemf; mouse.
DR PRO; PR:Q8CCP0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CCP0; protein.
DR Bgee; ENSMUSG00000020982; Expressed in manus and 228 other tissues.
DR ExpressionAtlas; Q8CCP0; baseline and differential.
DR Genevisible; Q8CCP0; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; ISS:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0140708; P:CAT tailing; ISS:UniProtKB.
DR GO; GO:0051168; P:nuclear export; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR021846; NFACT-C.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1064
FT /note="Ribosome quality control complex subunit NEMF"
FT /id="PRO_0000097643"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 296..359
FT /evidence="ECO:0000255"
FT COILED 481..512
FT /evidence="ECO:0000255"
FT COILED 858..882
FT /evidence="ECO:0000255"
FT COMPBIAS 731..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60524"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 412..415
FT /note="NPYL -> GGRW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010463"
FT VAR_SEQ 416..1064
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010464"
FT VAR_SEQ 638..641
FT /note="KKNF -> NSLT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010465"
FT VAR_SEQ 642..1064
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010466"
FT VAR_SEQ 889..892
FT /note="SAGS -> VSII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008397"
FT VAR_SEQ 893..1064
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008398"
FT MUTAGEN 86
FT /note="R->S: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 106..1064
FT /note="Missing: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 487
FT /note="R->G: Induces an age-dependent neurodegenerative
FT phenotype."
FT /evidence="ECO:0000269|PubMed:32934225"
FT CONFLICT 84
FT /note="S -> G (in Ref. 1; BAE42589)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> P (in Ref. 1; BAB23886)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="H -> Q (in Ref. 1; BAB30959)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="L -> S (in Ref. 1; BAB23886)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Q -> K (in Ref. 2; AAH80716)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="E -> G (in Ref. 1; BAB30366)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="K -> R (in Ref. 2; AAH53488)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="H -> Y (in Ref. 2; AAH53488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 121188 MW; F74F6ED7552AB183 CRC64;
MKSRFSTVDL RAVLAELNAS LLGMRVNNVY DVDNKTYLIR LQKPDFKATL LLESGIRIHT
TEFEWPKNMM PSSFAMKCRK HLKSRRLVSA KQLGVDRIVD FQFGSDEAAY HLIIELYDRG
NIVLTDYEYL ILNILRFRTD EADDVKFAVR ERYPIDHARA AEPLLTLERL TEVIAAAPKG
EVLKRVLNPL LPYGPALIEH CLIESGFSGN AKVDEKLESK DIEKILVCVQ RAEDYLRKTS
NFNGKGYIIQ KREAKPSLDA DKPAEDILTY EEFHPFLFSQ HLQCPYIEFE SFDKAVDEFY
SKIEGQKIDL KALQQEKQAL KKLDNVRKDH ENRLEALQQA QEIDKLKGEL IEMNLQIVDR
AIQVVRSALA NQIDWTEIGV IVKEAQAQGD PVACAIKELK LQTNHVTMLL RNPYLLSEEE
DGDGDASIEN SDAEAPKGKK KKQKNKQLQK PQKNKPLLVD VDLSLSAYAN AKKYYDHKRY
AAKKTQRTVE AAEKAFKSAE KKTKQTLKEV QTVTSIQKAR KVYWFEKFLW FISSENYLII
GGRDQQQNEI IVKRYLTPGD IYVHADLHGA TSCVIKNPTG EPIPPRTLTE AGTMALCYSA
AWDARVITSA WWVYHHQVSK TAPTGEYLTT GSFMIRGKKN FLPPSYLMMG FSFLFKVDES
CVWRHRGERK VRVQDEDMET LTSCTSELMA EEMEQLEGGD SSEEETEELH GMPGDVELMT
QVDQEDIAVH SGRDELSSED GEAKAVTKDQ EPIGEMKEEE EDTFEYPDTT IDLSHLQSQR
PLQKLAPREE SLNSNDSKSQ GRRHLSAKER REMKKKKLPC ESGDLEVIEE KDKERESAVH
TEAYQNTSKN VAAGQPMKRG QKSKMKKMKE KYKDQDDEDR ELIMKLLASA GSNKEEKGKK
GKKGKPKDEP VKKPPQKPRG GQRVLDVVKE PPSLQVLAHD LQDLAVDDPH DDKEEHDLDQ
QGNEENLFDS LTGQPHPEDV LMFAIPICAP YTIMTNYKYK VKLTPGVQKK GKAAKTALNS
FMHSKEATAR EKDLFRSVKD TDLSRNIPGK VKVSAPNLLH VKRK
