ID   TRPT1_MOUSE             Reviewed;         249 AA.
AC   Q8K3A2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=tRNA 2'-phosphotransferase 1;
DE            Short=mTPT1;
DE            EC=2.7.1.160;
GN   Name=Trpt1; Synonyms=Tpt1h;
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].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   FUNCTION, AND ENZYME ACTIVITY.
RX   PubMed=9826666; DOI=10.1073/pnas.95.24.14136;
RA   Spinelli S.L., Malik H.S., Consaul S.A., Phizicky E.M.;
RT   "A functional homolog of a yeast tRNA splicing enzyme is conserved in
RT   higher eukaryotes and in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14136-14141(1998).
CC   -!- FUNCTION: Catalyzes the last step of tRNA splicing, the transfer of the
CC       splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-
CC       ribose 1''-2'' cyclic phosphate. {ECO:0000269|PubMed:9826666}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-phospho-[ligated tRNA] + NAD(+) = ADP-beta-D-ribose
CC         1'',2''-cyclic phosphate + mature tRNA + nicotinamide;
CC         Xref=Rhea:RHEA:23324, Rhea:RHEA-COMP:11106, Rhea:RHEA-COMP:11107,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:76596,
CC         ChEBI:CHEBI:82883, ChEBI:CHEBI:85027; EC=2.7.1.160;
CC         Evidence={ECO:0000269|PubMed:9826666};
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27575.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC027575; AAH27575.1; ALT_INIT; mRNA.
DR   CCDS; CCDS50375.1; -.
DR   RefSeq; NP_705825.2; NM_153597.2.
DR   RefSeq; XP_006526640.1; XM_006526577.3.
DR   AlphaFoldDB; Q8K3A2; -.
DR   SMR; Q8K3A2; -.
DR   STRING; 10090.ENSMUSP00000085555; -.
DR   PhosphoSitePlus; Q8K3A2; -.
DR   PaxDb; Q8K3A2; -.
DR   PRIDE; Q8K3A2; -.
DR   ProteomicsDB; 300028; -.
DR   Antibodypedia; 51851; 34 antibodies from 14 providers.
DR   DNASU; 107328; -.
DR   Ensembl; ENSMUST00000088223; ENSMUSP00000085555; ENSMUSG00000047656.
DR   GeneID; 107328; -.
DR   KEGG; mmu:107328; -.
DR   UCSC; uc008gka.2; mouse.
DR   CTD; 83707; -.
DR   MGI; MGI:1333115; Trpt1.
DR   VEuPathDB; HostDB:ENSMUSG00000047656; -.
DR   eggNOG; KOG2278; Eukaryota.
DR   GeneTree; ENSGT00390000002731; -.
DR   HOGENOM; CLU_052998_1_1_1; -.
DR   InParanoid; Q8K3A2; -.
DR   OMA; YLYHGTV; -.
DR   OrthoDB; 1460780at2759; -.
DR   PhylomeDB; Q8K3A2; -.
DR   TreeFam; TF324127; -.
DR   BioGRID-ORCS; 107328; 4 hits in 73 CRISPR screens.
DR   PRO; PR:Q8K3A2; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8K3A2; protein.
DR   Bgee; ENSMUSG00000047656; Expressed in interventricular septum and 179 other tissues.
DR   Genevisible; Q8K3A2; MM.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IDA:MGI.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:MGI.
DR   Gene3D; 1.10.10.970; -; 1.
DR   Gene3D; 3.20.170.30; -; 1.
DR   InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR   InterPro; IPR042081; RNA_2'-PTrans_C.
DR   InterPro; IPR042080; RNA_2'-PTrans_N.
DR   PANTHER; PTHR12684; PTHR12684; 1.
DR   Pfam; PF01885; PTS_2-RNA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; NAD; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..249
FT                   /note="tRNA 2'-phosphotransferase 1"
FT                   /id="PRO_0000273364"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TN4"
SQ   SEQUENCE   249 AA;  27354 MW;  52BC90D83E9309F4 CRC64;
     MNAPGGRRKE GRRTHRPREQ DRNVQLSKAL SYALRHGALK LGLPMRADGF VPLQALLQLP
     QFHSFSIEDV QLVVNTNEKQ RFTLQPGEPS TGLLIRANQG HSLQVPELEL TPLETPQALP
     LTLVHGTFWK HWPSILLKGL SRQGRTHIHL ASGLPGDPGV ISGIRPNCEV AVFIDGPLAL
     TDGIPFFCSA NGVILTPGNA EGFLLPKYFK EALQLRPTRK PLSLAGDKET ETQSGPKLSS
     RGGRRKIQQ