NAF1_RAT
ID NAF1_RAT Reviewed; 457 AA.
AC Q52KK4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=H/ACA ribonucleoprotein complex non-core subunit NAF1;
GN Name=Naf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; BC094302; AAH94302.1; -; mRNA.
DR RefSeq; NP_001019943.1; NM_001024772.1.
DR AlphaFoldDB; Q52KK4; -.
DR SMR; Q52KK4; -.
DR STRING; 10116.ENSRNOP00000031163; -.
DR iPTMnet; Q52KK4; -.
DR PhosphoSitePlus; Q52KK4; -.
DR PaxDb; Q52KK4; -.
DR PRIDE; Q52KK4; -.
DR Ensembl; ENSRNOT00000033916; ENSRNOP00000031163; ENSRNOG00000026403.
DR GeneID; 306387; -.
DR KEGG; rno:306387; -.
DR UCSC; RGD:1306802; rat.
DR CTD; 92345; -.
DR RGD; 1306802; Naf1.
DR eggNOG; KOG2236; Eukaryota.
DR GeneTree; ENSGT00390000004697; -.
DR InParanoid; Q52KK4; -.
DR OrthoDB; 1453365at2759; -.
DR PhylomeDB; Q52KK4; -.
DR PRO; PR:Q52KK4; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IBA:GO_Central.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:RGD.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR GO; GO:0043489; P:RNA stabilization; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:RGD.
DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:RGD.
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..457
FT /note="H/ACA ribonucleoprotein complex non-core subunit
FT NAF1"
FT /id="PRO_0000315639"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..447
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 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96HR8"
SQ SEQUENCE 457 AA; 49764 MW; 08D131A43D54250D CRC64;
MEVVEAAAQL QTLKFGGSGP GSAASPPPEE RPDAEQAEQA PPAGEQPPPA PSSDAGENPP
PPSGPCATAP DAAEPLPELQ DSDSSDSDSD SETDSDSSSS SSSSSSSSSS CGSLPPVLSD
GEEDVQVEKE NKNFPLKTKD ELLLNELPSV EELTVTLPED IALKPLGKVS SIIEQLVIIE
SMTNIPPVNE DTVIFKSDRQ AAGKIFEIFG PVAHPFYVLR FNSSEHIESK GIKIKDTMYF
APSMKDFTQY IFTEKLKQDR GSDASWKNDQ EPPPEALDFS DDEKEKEAKQ RKKSQIQGRK
KLKSELNESG EDFGEVHQNW NANSSSEHSK GYHNREFTRG FPRGRYSRGS HGRPPPQQYY
NSDPMASQES LGFPPQRQDN PVMPHYPFPP PMFDMHNFPL PPPPPPPPTV SMGWAAPSMT
SHPVLNLPYS LPPPPLPPPP PPPSPGESNS SHFGSYY
