NAF1_MOUSE
ID NAF1_MOUSE Reviewed; 489 AA.
AC Q3UMQ8; Q8R2W2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=H/ACA ribonucleoprotein complex non-core subunit NAF1;
GN Name=Naf1;
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 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] OF 95-489.
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 249-489.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- FUNCTION: RNA-binding protein required for the maturation of box H/ACA
CC snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA
CC snoRNPs complex, it associates with the complex and disappears during
CC maturation of the complex and is replaced by NOLA1/GAR1 to yield mature
CC H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding
CC with DKC1/NOLA4 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: During assembly of the complex, component of the small
CC nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs
CC (H/ACA snoRNPs) which contains NOLA2/NHP2, NOLA3/NOP10, NAF1 and
CC DKC1/NOLA4. Interacts directly with DKC1/NOLA4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus. Absent from the
CC nucleolus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE26040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC116731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK144735; BAE26040.1; ALT_INIT; mRNA.
DR EMBL; BC027148; AAH27148.1; -; mRNA.
DR RefSeq; NP_001157036.1; NM_001163564.1.
DR AlphaFoldDB; Q3UMQ8; -.
DR SMR; Q3UMQ8; -.
DR BioGRID; 231512; 3.
DR STRING; 10090.ENSMUSP00000112640; -.
DR iPTMnet; Q3UMQ8; -.
DR PhosphoSitePlus; Q3UMQ8; -.
DR EPD; Q3UMQ8; -.
DR jPOST; Q3UMQ8; -.
DR MaxQB; Q3UMQ8; -.
DR PRIDE; Q3UMQ8; -.
DR ProteomicsDB; 287602; -.
DR GeneID; 234344; -.
DR KEGG; mmu:234344; -.
DR CTD; 92345; -.
DR MGI; MGI:2682306; Naf1.
DR InParanoid; Q3UMQ8; -.
DR OrthoDB; 1453365at2759; -.
DR PhylomeDB; Q3UMQ8; -.
DR BioGRID-ORCS; 234344; 21 hits in 72 CRISPR screens.
DR ChiTaRS; Naf1; mouse.
DR PRO; PR:Q3UMQ8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UMQ8; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IBA:GO_Central.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:0043489; P:RNA stabilization; IMP:BHF-UCL.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; TAS:BHF-UCL.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:MGI.
DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:MGI.
DR Gene3D; 2.40.10.230; -; 1.
DR InterPro; IPR038664; Gar1/Naf1_Cbf5-bd_sf.
DR InterPro; IPR007504; H/ACA_rnp_Gar1/Naf1.
DR InterPro; IPR040309; Naf1.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR31633; PTHR31633; 1.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..489
FT /note="H/ACA ribonucleoprotein complex non-core subunit
FT NAF1"
FT /id="PRO_0000315638"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96HR8"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96HR8"
SQ SEQUENCE 489 AA; 53246 MW; 2E752F90632375E8 CRC64;
MEVVEAAAQL QTLKFGGSGQ GSAAPQPPED RREAPPPGVQ PPPPAPSGRP PPPPAPSSDP
GGRPPPPPAP NWDAGGRPPP PPAPNSDPPP GGAWVTGRNA AEPPPVLQAS DSSDSDSDSE
TDSDSSSSSS SSSSSSSSCV SFPPVLSDGD EDFQLEKENK NFPLKTKDEL LLNELPSVEE
LTVILPEDIA LKPLGKVSSI IEQLVIIESV TNIPPVNEDT VIFKSDRQAA GKIFEIFGPV
AHPFYVLRFN SSDHIESKGI KINDTMYFAP SMKDFTQYIF TEKLKQDRGS DASWKNDQEP
PPEVLDFSDD EKEKEAKQRK KSQIQGRKKL KSELNESGED FGEVHENWNA YSSSEHSKGY
HHREFSRGFA RGRYSRRSHG RPPPQQYYNS DHMASQESLG FTPQRQDNPV MPHYPFPPPM
FDMHNFPLPP PPPPPPPPPP SMGWAAPSMA SHPVLNLPYS MPPPPLPPPP PPPPPSPGEN
NSSHFGPYF
