GAR1_MOUSE
ID GAR1_MOUSE Reviewed; 231 AA.
AC Q9CY66; Q80X93; Q8C6C5; Q8VDH0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=FVB/N; TISSUE=Limb, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CY66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CY66-2; Sequence=VSP_011427;
CC Name=3;
CC IsoId=Q9CY66-3; Sequence=VSP_011426, VSP_011427;
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}.
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; AK021256; BAB32351.1; -; mRNA.
DR EMBL; AK075923; BAC36056.1; -; mRNA.
DR EMBL; BC021873; AAH21873.1; -; mRNA.
DR EMBL; BC048685; AAH48685.1; -; mRNA.
DR CCDS; CCDS38634.1; -. [Q9CY66-1]
DR RefSeq; NP_080854.1; NM_026578.3. [Q9CY66-1]
DR RefSeq; XP_011238510.1; XM_011240208.2. [Q9CY66-1]
DR AlphaFoldDB; Q9CY66; -.
DR SMR; Q9CY66; -.
DR BioGRID; 212682; 29.
DR ComplexPortal; CPX-1124; Telomerase holoenzyme complex.
DR IntAct; Q9CY66; 3.
DR MINT; Q9CY66; -.
DR STRING; 10090.ENSMUSP00000029643; -.
DR iPTMnet; Q9CY66; -.
DR PhosphoSitePlus; Q9CY66; -.
DR EPD; Q9CY66; -.
DR MaxQB; Q9CY66; -.
DR PaxDb; Q9CY66; -.
DR PRIDE; Q9CY66; -.
DR ProteomicsDB; 273028; -. [Q9CY66-1]
DR ProteomicsDB; 273029; -. [Q9CY66-2]
DR ProteomicsDB; 273030; -. [Q9CY66-3]
DR Antibodypedia; 26373; 134 antibodies from 24 providers.
DR DNASU; 68147; -.
DR Ensembl; ENSMUST00000029643; ENSMUSP00000029643; ENSMUSG00000028010. [Q9CY66-1]
DR GeneID; 68147; -.
DR KEGG; mmu:68147; -.
DR UCSC; uc008rim.2; mouse. [Q9CY66-1]
DR CTD; 54433; -.
DR MGI; MGI:1930948; Gar1.
DR VEuPathDB; HostDB:ENSMUSG00000028010; -.
DR eggNOG; KOG3262; Eukaryota.
DR GeneTree; ENSGT00730000111223; -.
DR HOGENOM; CLU_080002_0_1_1; -.
DR InParanoid; Q9CY66; -.
DR OMA; HSCEGEM; -.
DR OrthoDB; 1530008at2759; -.
DR PhylomeDB; Q9CY66; -.
DR TreeFam; TF350747; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 68147; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Gar1; mouse.
DR PRO; PR:Q9CY66; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CY66; protein.
DR Bgee; ENSMUSG00000028010; Expressed in ileal epithelium and 266 other tissues.
DR ExpressionAtlas; Q9CY66; baseline and differential.
DR Genevisible; Q9CY66; MM.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:MGI.
DR GO; GO:0090661; C:box H/ACA telomerase RNP complex; ISO:MGI.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0001651; C:dense fibrillar component; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0030515; F:snoRNA binding; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..231
FT /note="H/ACA ribonucleoprotein complex subunit 1"
FT /id="PRO_0000208553"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..68
FT /note="RGG-box 1"
FT REGION 167..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..231
FT /note="RGG-box 2"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NY12"
FT VAR_SEQ 26..37
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011426"
FT VAR_SEQ 49..50
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011427"
FT CONFLICT 52
FT /note="F -> L (in Ref. 1; BAC36056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 23474 MW; FDD03BBEE258D662 CRC64;
MSFRGGGRGG FNRGGGGGGF NRGGGSNNHF RGGGGGGGGS FRGGGGGGGG SFRGGGRGGF
GRGGGRGGFN KFQDQGPPER VVLLGEFMHP CEDDIVCKCT TEENKVPYFN APVYLENKEQ
VGKVDEIFGQ LRDFYFSVKL SENMKASSFK KLQKFYIDPY KLLPLQRFLP RPPGEKGPPR
GGGGGGRGGR GGGRGGGGRG GGRGGGFRGG RGGGGGFRGG RGGGGFRGRG H
