ID   TRIR_HUMAN              Reviewed;         176 AA.
AC   Q9BQ61;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Telomerase RNA component interacting RNase {ECO:0000303|PubMed:28322335, ECO:0000312|HGNC:HGNC:28424};
DE            EC=3.1.13.- {ECO:0000269|PubMed:28322335};
DE   AltName: Full=Exoribonuclease TRIR {ECO:0000305};
GN   Name=TRIR {ECO:0000303|PubMed:28322335, ECO:0000312|HGNC:HGNC:28424};
GN   Synonyms=C19orf43 {ECO:0000312|HGNC:HGNC:28424};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Muscle, and Placenta;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-146, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [5]
RP   IDENTIFICATION IN THE TELOMERASE RNA 3' END PROCESSING COMPLEX, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   DOMAIN.
RX   PubMed=28322335; DOI=10.1038/srep45207;
RA   Xie J., Chen Z., Zhang X., Chen H., Guan W.;
RT   "Identification of an RNase that preferentially cleaves A/G nucleotides.";
RL   Sci. Rep. 7:45207-45207(2017).
CC   -!- FUNCTION: Exoribonuclease that is part of the telomerase RNA 3' end
CC       processing complex and which has the ability to all four unpaired RNA
CC       nucleotides from 5' end or 3' end with higher efficiency for purine
CC       bases (PubMed:28322335). {ECO:0000269|PubMed:28322335}.
CC   -!- ACTIVITY REGULATION: Zn(2+) inhibits the RNase activity while Mg(2+),
CC       Ca(2+), Mn(2+), K(+), Na(+), EDTA and EGTA show little effect on the
CC       exoribonuclease activity (PubMed:28322335).
CC       {ECO:0000269|PubMed:28322335}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-12. {ECO:0000269|PubMed:28322335};
CC       Temperature dependence:
CC         Optimum temperature is 37-75 degrees Celsius.
CC         {ECO:0000269|PubMed:28322335};
CC   -!- SUBUNIT: Part of the telomerase RNA 3' end complex which contains about
CC       488 proteins (PubMed:28322335). {ECO:0000269|PubMed:28322335}.
CC   -!- INTERACTION:
CC       Q9BQ61; P09012: SNRPA; NbExp=10; IntAct=EBI-744881, EBI-607085;
CC   -!- DOMAIN: The C-terminus contains a key domain which is responsible for
CC       the RNA digestion activity (PubMed:28322335).
CC       {ECO:0000269|PubMed:28322335}.
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DR   EMBL; BC000216; AAH00216.1; -; mRNA.
DR   EMBL; BC004533; AAH04533.1; -; mRNA.
DR   EMBL; BC015347; AAH15347.1; -; mRNA.
DR   CCDS; CCDS12279.1; -.
DR   RefSeq; NP_001316667.1; NM_001329738.1.
DR   RefSeq; NP_076943.1; NM_024038.3.
DR   AlphaFoldDB; Q9BQ61; -.
DR   SMR; Q9BQ61; -.
DR   BioGRID; 122473; 49.
DR   CORUM; Q9BQ61; -.
DR   IntAct; Q9BQ61; 16.
DR   MINT; Q9BQ61; -.
DR   STRING; 9606.ENSP00000242784; -.
DR   GlyGen; Q9BQ61; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BQ61; -.
DR   PhosphoSitePlus; Q9BQ61; -.
DR   BioMuta; TRIR; -.
DR   DMDM; 74732813; -.
DR   EPD; Q9BQ61; -.
DR   jPOST; Q9BQ61; -.
DR   MassIVE; Q9BQ61; -.
DR   MaxQB; Q9BQ61; -.
DR   PaxDb; 9606-ENSP00000242784; -.
DR   PeptideAtlas; Q9BQ61; -.
DR   ProteomicsDB; 78631; -.
DR   Pumba; Q9BQ61; -.
DR   TopDownProteomics; Q9BQ61; -.
DR   Antibodypedia; 26146; 47 antibodies from 15 providers.
DR   DNASU; 79002; -.
DR   Ensembl; ENST00000242784.5; ENSP00000242784.3; ENSG00000123144.11.
DR   GeneID; 79002; -.
DR   KEGG; hsa:79002; -.
DR   MANE-Select; ENST00000242784.5; ENSP00000242784.3; NM_024038.4; NP_076943.1.
DR   UCSC; uc002muu.4; human.
DR   AGR; HGNC:28424; -.
DR   CTD; 79002; -.
DR   GeneCards; TRIR; -.
DR   HGNC; HGNC:28424; TRIR.
DR   HPA; ENSG00000123144; Low tissue specificity.
DR   neXtProt; NX_Q9BQ61; -.
DR   OpenTargets; ENSG00000123144; -.
DR   PharmGKB; PA144596476; -.
DR   VEuPathDB; HostDB:ENSG00000123144; -.
DR   eggNOG; ENOG502S83W; Eukaryota.
DR   GeneTree; ENSGT00390000012267; -.
DR   HOGENOM; CLU_126877_0_0_1; -.
DR   InParanoid; Q9BQ61; -.
DR   OMA; GDAWSKY; -.
DR   OrthoDB; 5405606at2759; -.
DR   PhylomeDB; Q9BQ61; -.
DR   TreeFam; TF323808; -.
DR   PathwayCommons; Q9BQ61; -.
DR   SignaLink; Q9BQ61; -.
DR   BioGRID-ORCS; 79002; 134 hits in 1134 CRISPR screens.
DR   ChiTaRS; C19orf43; human.
DR   GenomeRNAi; 79002; -.
DR   Pharos; Q9BQ61; Tdark.
DR   PRO; PR:Q9BQ61; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9BQ61; Protein.
DR   Bgee; ENSG00000123144; Expressed in granulocyte and 185 other cell types or tissues.
DR   ExpressionAtlas; Q9BQ61; baseline and differential.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR   InterPro; IPR038838; TRIR.
DR   PANTHER; PTHR34753; TELOMERASE RNA COMPONENT INTERACTING RNASE; 1.
DR   PANTHER; PTHR34753:SF1; TELOMERASE RNA COMPONENT INTERACTING RNASE; 1.
DR   Genevisible; Q9BQ61; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..176
FT                   /note="Telomerase RNA component interacting RNase"
FT                   /id="PRO_0000280762"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
SQ   SEQUENCE   176 AA;  18419 MW;  7A96B523F5C05CB5 CRC64;
     MAARGRRAEP QGREAPGPAG GGGGGSRWAE SGSGTSPESG DEEVSGAGSS PVSGGVNLFA
     NDGSFLELFK RKMEEEQRQR QEEPPPGPQR PDQSAAAAGP GDPKRKGGPG STLSFVGKRR
     GGNKLALKTG IVAKKQKTED EVLTSKGDAW AKYMAEVKKY KAHQCGDDDK TRPLVK
//