NVL_MOUSE
ID NVL_MOUSE Reviewed; 855 AA.
AC Q9DBY8; Q3USC4; Q8BW27; Q8K2B5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Nuclear valosin-containing protein-like;
DE Short=NVLp;
DE Short=Nuclear VCP-like protein;
GN Name=Nvl {ECO:0000312|MGI:MGI:1914709};
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=C57BL/6J; TISSUE=Cerebellum, Lung, and Ovary;
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].
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-190, 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-190, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Spleen;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP STRUCTURE BY NMR OF 1-74, SUBCELLULAR LOCATION, INTERACTION WITH
RP NCL/NUCLEOLIN, AND NUCLEOLAR LOCALIZATION SIGNAL.
RX PubMed=21474449; DOI=10.1074/jbc.m110.174680;
RA Fujiwara Y., Fujiwara K., Goda N., Iwaya N., Tenno T., Shirakawa M.,
RA Hiroaki H.;
RT "Structure and function of the N-terminal nucleolin binding domain of
RT nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar
RT localization signal.";
RL J. Biol. Chem. 286:21732-21741(2011).
CC -!- FUNCTION: Participates in the assembly of the telomerase holoenzyme and
CC effecting of telomerase activity via its interaction with TERT.
CC Involved in both early and late stages of the pre-rRNA processing
CC pathways. Spatiotemporally regulates 60S ribosomal subunit biogenesis
CC in the nucleolus. Catalyzes the release of specific assembly factors,
CC such as WDR74, from pre-60S ribosomal particles through the ATPase
CC activity. {ECO:0000250|UniProtKB:O15381}.
CC -!- SUBUNIT: Interacts with NCL/nucleolin (PubMed:21474449). Isoform 1 and
CC isoform 2 interact with TERT and isoform 1 exhibits a higher binding
CC affinity for TERT compared to isoform 2. Isoform 1 interacts with MTREX
CC in an ATP-dependent manner; the interaction is required to associate
CC NVL with nuclear RNA exosome. Isoform 1 interacts with RPL5 in an ATP-
CC dependent manner. Interacts with WDR74 (through WDR repeats); the
CC interaction is independent of RNA or pre-60S ribosome particles (By
CC similarity). {ECO:0000250|UniProtKB:O15381,
CC ECO:0000269|PubMed:21474449}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21474449}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O15381}. Note=Associates
CC with pre-ribosomal particles in the nucleus.
CC {ECO:0000250|UniProtKB:O15381}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AK004676; BAB23464.1; -; mRNA.
DR EMBL; AK054502; BAC35806.1; -; mRNA.
DR EMBL; AK140509; BAE24409.1; -; mRNA.
DR EMBL; BC031847; AAH31847.1; -; mRNA.
DR CCDS; CCDS15581.1; -.
DR RefSeq; NP_080447.1; NM_026171.2.
DR PDB; 2RRE; NMR; -; A=1-74.
DR PDBsum; 2RRE; -.
DR AlphaFoldDB; Q9DBY8; -.
DR BMRB; Q9DBY8; -.
DR SMR; Q9DBY8; -.
DR BioGRID; 212203; 27.
DR IntAct; Q9DBY8; 1.
DR MINT; Q9DBY8; -.
DR STRING; 10090.ENSMUSP00000027797; -.
DR iPTMnet; Q9DBY8; -.
DR PhosphoSitePlus; Q9DBY8; -.
DR EPD; Q9DBY8; -.
DR jPOST; Q9DBY8; -.
DR MaxQB; Q9DBY8; -.
DR PaxDb; Q9DBY8; -.
DR PeptideAtlas; Q9DBY8; -.
DR PRIDE; Q9DBY8; -.
DR ProteomicsDB; 287865; -.
DR Antibodypedia; 34637; 223 antibodies from 27 providers.
DR DNASU; 67459; -.
DR Ensembl; ENSMUST00000027797; ENSMUSP00000027797; ENSMUSG00000026516.
DR GeneID; 67459; -.
DR KEGG; mmu:67459; -.
DR UCSC; uc007dxb.1; mouse.
DR CTD; 4931; -.
DR MGI; MGI:1914709; Nvl.
DR VEuPathDB; HostDB:ENSMUSG00000026516; -.
DR eggNOG; KOG0733; Eukaryota.
DR GeneTree; ENSGT00570000079239; -.
DR HOGENOM; CLU_000688_8_3_1; -.
DR InParanoid; Q9DBY8; -.
DR OMA; RQVFMRA; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q9DBY8; -.
DR TreeFam; TF314681; -.
DR BioGRID-ORCS; 67459; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Nvl; mouse.
DR EvolutionaryTrace; Q9DBY8; -.
DR PRO; PR:Q9DBY8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9DBY8; protein.
DR Bgee; ENSMUSG00000026516; Expressed in embryonic post-anal tail and 242 other tissues.
DR Genevisible; Q9DBY8; MM.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:1990275; F:preribosome binding; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISS:UniProtKB.
DR GO; GO:1904749; P:regulation of protein localization to nucleolus; ISS:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 1.10.10.2010; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR038100; NLV2_N_sf.
DR InterPro; IPR031996; NVL2_nucleolin-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF16725; Nucleolin_bd; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..855
FT /note="Nuclear valosin-containing protein-like"
FT /id="PRO_0000084589"
FT REGION 1..219
FT /note="Interaction with RPL5"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT REGION 83..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..473
FT /note="Interaction with WDR74"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT REGION 496..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..52
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:21474449"
FT MOTIF 85..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT MOTIF 217..231
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT COMPBIAS 94..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 621..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT CONFLICT 513
FT /note="E -> K (in Ref. 2; AAH31847)"
FT /evidence="ECO:0000305"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:2RRE"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2RRE"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:2RRE"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:2RRE"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:2RRE"
SQ SEQUENCE 855 AA; 94476 MW; F69A173AB40E0AE9 CRC64;
MKPRPGVFVD RKLKQRVIQY LSSNRCGKYV DTGILASDLQ RLYSVDYGRR KRNAFRIQVE
KVFSIISSEK ELKNLKELED GHLAKRARQD EEDEYTESYS DDDSNMEDYP DPQSANPMNS
SLLSLYRRGN SESVSTTPKW GQREATTSTP LLTSKTGSVP LKTPARESEG GWFIDKTPGG
KKESLPLDLS DDQSNSKKQD SEIQILKDSS LLESDKKRKG RAKGKGNKRK TENLQEVDGE
IEALLQKKAK ARSTELQISN VKFEDVGGND ATLKEVCKML IHMRHPEVYQ HLGVVPPRGV
LLHGPPGCGK TLLAHAIAGE LDLPILKVAA PEIVSGVSGE SEQKLRELFD QAVSNAPCIV
FIDEIDAITP KREVASKDME RRIVAQLLTC MDDLNNVAAT ARVLVIGATN RPDSLDPALR
RAGRFDREVC LGIPDEAARE RILQTLCRKL RLPETFNFCH LAHLTPGFVG ADLMALCREA
AMCAVNRVLM KQQAQQKKKP EIEGLPSEGD QEERLGAEPT SETQDELQRL LGLLRDQDPL
SEEQMQGLCI ELNDFIVALA EVQPSAKREG FVTVPNVTWA DIGALEDIRD ELIMAILAPV
RNPDQFRTLG LGTPAGILLA GPPGCGKTLL AKAVANESGL NFISVKGPEL LNMYVGESER
AVRQVFQRAK NSAPCVIFFD EVDALCPRRS DRETGASVRV VNQLLTEMDG LETRQQVFIL
AATNRPDIID PAILRPGRLD KTLFVGLPPP ADRVAILKTI TKNGTKPPLD EDVNLETIAN
DLRCNCYTGA DLTALVREAS LCALRQEITA QKNGVGAGEL KVSHKHFEDA FKKVKPSISI
KDQVMYEALQ RSLSQ
