DKC1_DROME
ID DKC1_DROME Reviewed; 508 AA.
AC O44081; A8E745; Q0GLB4; Q0MVP1; Q8T408; Q9UAN8; Q9V3Z5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit 4;
DE EC=5.4.99.-;
DE AltName: Full=Nucleolar protein AT band 60B;
DE AltName: Full=Protein minifly;
GN Name=Nop60B; Synonyms=mfl; ORFNames=CG3333;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9829824; DOI=10.1007/s004380050866;
RA Phillips B., Billin A.N., Cadwell C., Buchholz R., Erickson C.,
RA Merriam J.R., Carbon J., Poole S.J.;
RT "The Nop60B gene of Drosophila encodes an essential nucleolar protein that
RT functions in yeast.";
RL Mol. Gen. Genet. 260:20-29(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10087258; DOI=10.1083/jcb.144.6.1123;
RA Giordano E., Peluso I., Senger S., Furia M.;
RT "minifly, a Drosophila gene required for ribosome biogenesis.";
RL J. Cell Biol. 144:1123-1133(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), AND DEVELOPMENTAL STAGE.
RX PubMed=17328797; DOI=10.1186/1471-2199-8-15;
RA Riccardo S., Tortoriello G., Giordano E., Turano M., Furia M.;
RT "The coding/non-coding overlapping architecture of the gene encoding the
RT Drosophila pseudouridine synthase.";
RL BMC Mol. Biol. 8:15-15(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-468 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-468 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=12645924; DOI=10.1016/s0012-1606(02)00013-1;
RA Kauffman T., Tran J., DiNardo S.;
RT "Mutations in Nop60B, the Drosophila homolog of human dyskeratosis
RT congenita 1, affect the maintenance of the germ-line stem cell lineage
RT during spermatogenesis.";
RL Dev. Biol. 253:189-199(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442; THR-443; SER-444;
RP SER-445; THR-449; SER-455 AND THR-458, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays a central role in ribosomal RNA processing. Probable
CC catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA
CC snoRNP) complex, which catalyzes pseudouridylation of rRNA. This
CC involves the isomerization of uridine such that the ribose is
CC subsequently attached to C5, instead of the normal N1. Pseudouridine
CC ('psi') residues may serve to stabilize the conformation of rRNAs.
CC Required for maintenance of the germline stem cell lineage during
CC spermatogenesis. {ECO:0000269|PubMed:10087258,
CC ECO:0000269|PubMed:12645924, ECO:0000269|PubMed:9829824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in RNA = a pseudouridine in RNA;
CC Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particle
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10087258,
CC ECO:0000269|PubMed:9829824}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=B;
CC IsoId=O44081-1; Sequence=Displayed;
CC Name=C; Synonyms=alpha;
CC IsoId=O44081-2; Sequence=VSP_036583, VSP_036584;
CC -!- DEVELOPMENTAL STAGE: Isoform C is expressed both maternally and
CC zygotically. Isoform A is expressed at the same level in adult females
CC but at a much lower level in ovaries. {ECO:0000269|PubMed:17328797}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV82369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF017230; AAC97117.1; -; mRNA.
DR EMBL; AF089837; AAD16092.1; -; mRNA.
DR EMBL; AF097634; AAD19897.1; -; Genomic_DNA.
DR EMBL; DQ841550; ABH08965.1; -; mRNA.
DR EMBL; DQ857345; ABI17547.1; -; mRNA.
DR EMBL; DQ857346; ABI17548.1; -; mRNA.
DR EMBL; AE013599; AAF47178.1; -; Genomic_DNA.
DR EMBL; AE013599; AAX52682.1; -; Genomic_DNA.
DR EMBL; AY089408; AAL90146.1; -; mRNA.
DR EMBL; BT030987; ABV82369.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014547.1; NM_001014547.4. [O44081-1]
DR RefSeq; NP_001163286.1; NM_001169815.3. [O44081-1]
DR RefSeq; NP_001163289.1; NM_001169818.3. [O44081-1]
DR RefSeq; NP_525120.1; NM_080381.5. [O44081-1]
DR AlphaFoldDB; O44081; -.
DR SMR; O44081; -.
DR BioGRID; 63449; 11.
DR DIP; DIP-20128N; -.
DR IntAct; O44081; 3.
DR STRING; 7227.FBpp0099583; -.
DR iPTMnet; O44081; -.
DR PaxDb; O44081; -.
DR EnsemblMetazoa; FBtr0072258; FBpp0072166; FBgn0259937. [O44081-1]
DR EnsemblMetazoa; FBtr0100213; FBpp0099583; FBgn0259937. [O44081-1]
DR EnsemblMetazoa; FBtr0300227; FBpp0289464; FBgn0259937. [O44081-1]
DR EnsemblMetazoa; FBtr0300861; FBpp0290083; FBgn0259937. [O44081-1]
DR GeneID; 37873; -.
DR KEGG; dme:Dmel_CG3333; -.
DR UCSC; CG3333-RB; d. melanogaster.
DR CTD; 37873; -.
DR FlyBase; FBgn0259937; Nop60B.
DR VEuPathDB; VectorBase:FBgn0259937; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00510000047092; -.
DR HOGENOM; CLU_032087_3_2_1; -.
DR InParanoid; O44081; -.
DR OMA; GPFKEDE; -.
DR PhylomeDB; O44081; -.
DR Reactome; R-DME-171319; Telomere Extension By Telomerase.
DR SignaLink; O44081; -.
DR BioGRID-ORCS; 37873; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Nop60B; fly.
DR GenomeRNAi; 37873; -.
DR PRO; PR:O44081; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0259937; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; O44081; baseline and differential.
DR Genevisible; O44081; DM.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0001522; P:pseudouridine synthesis; IMP:FlyBase.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:FlyBase.
DR GO; GO:0006364; P:rRNA processing; IMP:FlyBase.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR Gene3D; 2.30.130.10; -; 1.
DR InterPro; IPR012960; Dyskerin-like.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR InterPro; IPR032819; TruB_C.
DR PANTHER; PTHR23127; PTHR23127; 1.
DR Pfam; PF08068; DKCLD; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SMART; SM01136; DKCLD; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00425; CBF5; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..508
FT /note="H/ACA ribonucleoprotein complex subunit 4"
FT /id="PRO_0000121989"
FT DOMAIN 294..369
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 212..253
FT /note="GVFWVSCEAGSYIRTMCVHLGLVLGVGGQMLELRRVRSGIQS -> DLLIRS
FT CNIWTITLIKEISSKIFLKIIECHRNLKSSHDTLLR (in isoform C)"
FT /evidence="ECO:0000303|PubMed:17328797"
FT /id="VSP_036583"
FT VAR_SEQ 254..508
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:17328797"
FT /id="VSP_036584"
FT CONFLICT 69
FT /note="P -> R (in Ref. 2; AAD19897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56831 MW; 3CAE3F91C84E0A94 CRC64;
MADVEVRKEK KKKKIKEEPL DGDDIGTLQK QGNFQIKPSS KIAELDTSQW PLLLKNFDKL
NIRSNHYTPL AHGSSPLNRD IKEYMKTGFI NLDKPSNPSS HEVVAWIKKI LKVEKTGHSG
TLDPKVTGCL IVCIDRATRL VKSQQSAGKE YVAIFKLHGA VESVAKVRQG LEKLRGALFQ
RPPLISAVKR QLRVRTVYDS KLLDYDETRN MGVFWVSCEA GSYIRTMCVH LGLVLGVGGQ
MLELRRVRSG IQSERDGMVT MHDVLDAMWL YENHKDESML RRVIKPLEGL LVNHKRIIMK
DSSVNAVCYG AKITLPGVLR YEDGIEIDQE IVICTTKGEA ICLAIALMTT ATMASCDHGV
VAKIKRVIME RDTYPRKWGL GPKASAKKAL IAAGKLDKFG RPNENTPKEW LTGYVDYNAK
KPAAQEVSPT NGSSEPSKRK LSTSSVEETA AAAVSEETPS KDKKKKKKKH KGDEEAPEAA
EEEAEPVEKE KKKKKKKDKD RDRDEAQE
