GAR1_RAT
ID GAR1_RAT Reviewed; 226 AA.
AC Q6AYA1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit 1;
DE AltName: Full=Nucleolar protein family A member 1;
DE AltName: Full=snoRNP protein GAR1;
GN Name=Gar1; Synonyms=Nola1;
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=Kidney;
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).
CC -!- FUNCTION: Required for ribosome biogenesis and telomere maintenance.
CC Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP)
CC complex, which catalyzes pseudouridylation of rRNA. This involves the
CC isomerization of uridine such that the ribose is subsequently attached
CC to C5, instead of the normal N1. Each rRNA can contain up to 100
CC pseudouridine ('psi') residues, which may serve to stabilize the
CC conformation of rRNAs. May also be required for correct processing or
CC intranuclear trafficking of TERC, the RNA component of the telomerase
CC reverse transcriptase (TERT) holoenzyme (By similarity). {ECO:0000250}.
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. The
CC complex contains a stable core formed by binding of one or two NOP10-
CC DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via
CC DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which
CC may target the specific site of modification within the RNA substrate.
CC The complex also interacts with TERC, which contains a 3'-terminal
CC domain related to the box H/ACA snoRNAs. Specific interactions with
CC snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with
CC NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting
CC of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is
CC mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex
CC may be required for correct assembly of the H/ACA snoRNP complex.
CC Component of the telomerase holoenzyme complex composed of one molecule
CC of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA
CC ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a
CC telomerase RNA template component (TERC). The telomerase holoenzyme
CC complex is associated with TEP1, SMG6/EST1A and POT1.
CC {ECO:0000250|UniProtKB:Q9NY12}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal
CC body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled
CC bodies). {ECO:0000250}.
CC -!- DOMAIN: Interaction with SMN1 requires at least one of the RGG-box
CC regions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAR1 family. {ECO:0000305}.
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DR EMBL; BC079131; AAH79131.1; -; mRNA.
DR RefSeq; NP_001019477.1; NM_001024306.1.
DR AlphaFoldDB; Q6AYA1; -.
DR SMR; Q6AYA1; -.
DR CORUM; Q6AYA1; -.
DR STRING; 10116.ENSRNOP00000013149; -.
DR iPTMnet; Q6AYA1; -.
DR PhosphoSitePlus; Q6AYA1; -.
DR jPOST; Q6AYA1; -.
DR PaxDb; Q6AYA1; -.
DR PRIDE; Q6AYA1; -.
DR GeneID; 499709; -.
DR KEGG; rno:499709; -.
DR UCSC; RGD:1563995; rat.
DR CTD; 54433; -.
DR RGD; 1563995; Gar1.
DR VEuPathDB; HostDB:ENSRNOG00000061146; -.
DR eggNOG; KOG3262; Eukaryota.
DR HOGENOM; CLU_080002_0_1_1; -.
DR InParanoid; Q6AYA1; -.
DR OMA; HSCEGEM; -.
DR OrthoDB; 1530008at2759; -.
DR TreeFam; TF350747; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR PRO; PR:Q6AYA1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000061146; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q6AYA1; baseline and differential.
DR Genevisible; Q6AYA1; RN.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
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:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IDA:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..226
FT /note="H/ACA ribonucleoprotein complex subunit 1"
FT /id="PRO_0000208554"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..59
FT /note="RGG-box 1"
FT REGION 158..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..226
FT /note="RGG-box 2"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY12"
SQ SEQUENCE 226 AA; 23011 MW; B81ADE63E02F151D CRC64;
MSFRGGGRGG FNRGGGGGGF NRGGGSNNHF RGGGGGGGGG GNFRGGGRGG FGRGGGRGGF
NKFQDQGPPE RVVLLGEFMH PCEDDIVCKC TTEENKVPYF NAPVYLENKE QIGKVDEIFG
QLRDFYFSVK LSENMKASSF KKLQKFYIDP YKLLPLQRFL PRPPGEKGPP RGGGGGGGGG
RGGRGGGRGG GGRGGGRGGG FRGGRGGGGG FRGGRGGGGG FRGRGH
