DKC1_RAT
ID DKC1_RAT Reviewed; 509 AA.
AC P40615; Q499M9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit DKC1;
DE EC=5.4.99.- {ECO:0000250|UniProtKB:O60832};
DE AltName: Full=Dyskerin;
DE AltName: Full=Nopp140-associated protein of 57 kDa {ECO:0000303|PubMed:7798307};
DE AltName: Full=Nucleolar protein NAP57 {ECO:0000303|PubMed:7798307};
DE AltName: Full=Nucleolar protein family A member 4;
DE AltName: Full=snoRNP protein DKC1;
GN Name=Dkc1; Synonyms=Nap57 {ECO:0000303|PubMed:7798307};
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 [MRNA], PROTEIN SEQUENCE OF 21-43; 83-96 AND 98-119,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NOLC1.
RC TISSUE=Liver;
RX PubMed=7798307; DOI=10.1083/jcb.127.6.1505;
RA Meier U., Blobel G.;
RT "NAP57, a mammalian nucleolar protein with a putative homolog in yeast and
RT bacteria.";
RL J. Cell Biol. 127:1505-1514(1994).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Meier U.;
RL Submitted (DEC-1997) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 FUNCTION, INTERACTION WITH GAR1; NHP2; NOP10 AND NOLC1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12446766; DOI=10.1128/mcb.22.24.8457-8466.2002;
RA Wang C., Query C.C., Meier U.T.;
RT "Immunopurified small nucleolar ribonucleoprotein particles pseudouridylate
RT rRNA independently of their association with phosphorylated Nopp140.";
RL Mol. Cell. Biol. 22:8457-8466(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-454, AND
RP IDENTIFICATION BY 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: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein
CC (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA
CC (PubMed:12446766). This involves the isomerization of uridine such that
CC the ribose is subsequently attached to C5, instead of the normal N1 (By
CC similarity). Each rRNA can contain up to 100 pseudouridine ('psi')
CC residues, which may serve to stabilize the conformation of rRNAs (By
CC similarity). Required for ribosome biogenesis and telomere maintenance
CC (By similarity). Also required for correct processing or intranuclear
CC trafficking of TERC, the RNA component of the telomerase reverse
CC transcriptase (TERT) holoenzyme (By similarity).
CC {ECO:0000250|UniProtKB:O60832, ECO:0000269|PubMed:12446766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:O60832};
CC -!- SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA
CC snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3,
CC and DKC1/NOLA4, which is presumed to be the catalytic subunit
CC (PubMed:12446766). The complex contains a stable core formed by binding
CC of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds
CC to this core via DKC1 (By similarity). The complex binds a box H/ACA
CC small nucleolar RNA (snoRNA), which may target the specific site of
CC modification within the RNA substrate (By similarity). During assembly,
CC the complex contains NAF1 instead of GAR1/NOLA1 (By similarity). The
CC complex also interacts with TERC, which contains a 3'-terminal domain
CC related to the box H/ACA snoRNAs (By similarity). Specific interactions
CC with snoRNAs or TERC are mediated by GAR1 and NHP2 (By similarity).
CC Associates with NOLC1/NOPP140 (By similarity). H/ACA snoRNPs interact
CC with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1,
CC DDX20/GEMIN3, and GEMIN4 (By similarity). This is mediated by
CC interaction between GAR1 and SMN1 or SMN2 (By similarity). The SMN
CC complex may be required for correct assembly of the H/ACA snoRNP
CC complex (By similarity). Component of the telomerase holoenzyme complex
CC composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two
CC molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2
CC and GAR1, and a telomerase RNA template component (TERC) (By
CC similarity). The telomerase holoenzyme complex is associated with TEP1,
CC SMG6/EST1A and POT1 (By similarity). Interacts with SHQ1; this
CC interaction may lead to the stabilization of DKC1, from the time of its
CC synthesis until its association with NOP10, NHP2, and NAF1 at the
CC nascent H/ACA RNA (By similarity). Interacts with HMBOX1 (By
CC similarity). Interacts with DHX36 (By similarity).
CC {ECO:0000250|UniProtKB:O60832, ECO:0000269|PubMed:12446766}.
CC -!- INTERACTION:
CC P40615; D3ZMP6: Nop10; NbExp=4; IntAct=EBI-5746997, EBI-8792072;
CC P40615; Q96HR8: NAF1; Xeno; NbExp=3; IntAct=EBI-5746997, EBI-2515597;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:7798307}.
CC Nucleus, Cajal body {ECO:0000269|PubMed:7798307}. Note=Also localized
CC to Cajal bodies (coiled bodies). {ECO:0000269|PubMed:7798307}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; Z34922; CAA84402.1; -; mRNA.
DR EMBL; BC099832; AAH99832.1; -; mRNA.
DR PIR; A55163; A55163.
DR RefSeq; NP_596910.1; NM_133419.1.
DR AlphaFoldDB; P40615; -.
DR SMR; P40615; -.
DR BioGRID; 251042; 1.
DR CORUM; P40615; -.
DR IntAct; P40615; 5.
DR STRING; 10116.ENSRNOP00000064024; -.
DR iPTMnet; P40615; -.
DR PhosphoSitePlus; P40615; -.
DR jPOST; P40615; -.
DR PRIDE; P40615; -.
DR GeneID; 170944; -.
DR KEGG; rno:170944; -.
DR CTD; 1736; -.
DR RGD; 621780; Dkc1.
DR eggNOG; KOG2529; Eukaryota.
DR InParanoid; P40615; -.
DR OrthoDB; 1070373at2759; -.
DR PhylomeDB; P40615; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR PRO; PR:P40615; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; IDA:RGD.
DR GO; GO:0090661; C:box H/ACA telomerase RNP complex; ISO:RGD.
DR GO; GO:0015030; C:Cajal body; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:RGD.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:RGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003720; F:telomerase activity; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0033979; P:box H/ACA RNA metabolic process; ISO:RGD.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; ISO:RGD.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; ISO:RGD.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; ISO:RGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:RGD.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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 InterPro; IPR004521; Uncharacterised_CHP00451.
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 TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isomerase; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CHAIN 2..509
FT /note="H/ACA ribonucleoprotein complex subunit DKC1"
FT /id="PRO_0000121985"
FT DOMAIN 297..372
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..22
FT /note="Nucleolar localization"
FT /evidence="ECO:0000250"
FT REGION 381..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..509
FT /note="Nuclear and nucleolar localization"
FT /evidence="ECO:0000250"
FT COMPBIAS 444..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P60340"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESX5"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 395
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60832"
FT CONFLICT 459..508
FT /note="ATPTTTPRVKKEKKKKKEKADGGEEAAEDGDGDATRKKKKKKARAAEELS
FT -> RRPLPRP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 56615 MW; 038862EBBF2A1E2F CRC64;
MADAEAAMTF PKKHKKKKER KPLPEADVAE IQHAEDFLIK PESKAAQLDT SQWPLLLKNF
DRLNVRTTHY TPIPCGSNPL KREIGEYVRT GFINLDKPSN PSSHEVVAWI RRILRVEKTG
HSGTLDPKVT GCLIVCIERA TRLVKSQQSA GKEYVGVVRL HNAIEGTAQL SRALETLTGA
LFQRPPLIAA VKRQLRVRTI YESRVVEYDP ERRLGVFWVS CEAGTYIRTL CVHLGLLLGV
GGQMQELRRV RSGVVGERDH MVTMHDVLDA QYLYDHHRDE SYLRRVVFPL EKLLTSHKRL
VMKDSAVNAI CYGAKIMLPG LLRYEDGIEV NQEVVVITTK GEAVCVAIAL MTTAVISTCD
HGVVAKIKRV IMERDTYPRK WGLGPKASQK KQLIKQGLLD KHGRPTDGTP ASWTRDYVDY
SDSSKKATAA EATPGPGVTA DAASIVKRKR DSDSDADEAT PTTTPRVKKE KKKKKEKADG
GEEAAEDGDG DATRKKKKKK ARAAEELSG
