DTWD1_HUMAN
ID DTWD1_HUMAN Reviewed; 304 AA.
AC Q8N5C7; Q567Q3; Q8WVG9; Q9NRU6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=tRNA-uridine aminocarboxypropyltransferase 1 {ECO:0000305};
DE EC=2.5.1.25 {ECO:0000269|PubMed:31804502};
DE AltName: Full=DTW domain-containing protein 1 {ECO:0000305};
GN Name=DTWD1 {ECO:0000303|PubMed:31804502, ECO:0000312|HGNC:HGNC:30926};
GN ORFNames=MDS009 {ECO:0000303|Ref.1};
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] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Zhang C., Tu Y., Gu W., Wang Y., Han Z., Chen Z., Zhou J., Gu J.,
RA Huang Q., Yu Y., Xu S., Ren S., Fu G.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndromes patient.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Skin, and Thyroid;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=31804502; DOI=10.1038/s41467-019-13525-3;
RA Takakura M., Ishiguro K., Akichika S., Miyauchi K., Suzuki T.;
RT "Biogenesis and functions of aminocarboxypropyluridine in tRNA.";
RL Nat. Commun. 10:5542-5542(2019).
CC -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC (acp3U) at position 20 in the D-loop of several cytoplasmic tRNAs
CC (acp3U(20)). {ECO:0000269|PubMed:31804502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC Evidence={ECO:0000269|PubMed:31804502};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31804502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N5C7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5C7-2; Sequence=VSP_028922;
CC Name=3;
CC IsoId=Q8N5C7-3; Sequence=VSP_028923;
CC -!- DOMAIN: Contains 1 DXTW motif.
CC -!- SIMILARITY: Belongs to the TDD superfamily. DTWD1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87319.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF168717; AAF87319.1; ALT_FRAME; mRNA.
DR EMBL; AC018927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018028; AAH18028.1; -; mRNA.
DR EMBL; BC032535; AAH32535.1; -; mRNA.
DR EMBL; BC093073; AAH93073.1; -; mRNA.
DR CCDS; CCDS10132.1; -. [Q8N5C7-1]
DR RefSeq; NP_001138427.1; NM_001144955.1. [Q8N5C7-1]
DR RefSeq; NP_064619.2; NM_020234.5. [Q8N5C7-1]
DR RefSeq; XP_016877908.1; XM_017022419.1. [Q8N5C7-1]
DR RefSeq; XP_016877909.1; XM_017022420.1. [Q8N5C7-1]
DR RefSeq; XP_016877910.1; XM_017022421.1. [Q8N5C7-1]
DR RefSeq; XP_016877911.1; XM_017022422.1. [Q8N5C7-1]
DR RefSeq; XP_016877916.1; XM_017022427.1. [Q8N5C7-2]
DR RefSeq; XP_016877917.1; XM_017022428.1. [Q8N5C7-2]
DR RefSeq; XP_016877918.1; XM_017022429.1. [Q8N5C7-2]
DR RefSeq; XP_016877919.1; XM_017022430.1. [Q8N5C7-2]
DR RefSeq; XP_016877920.1; XM_017022431.1.
DR AlphaFoldDB; Q8N5C7; -.
DR BioGRID; 121303; 18.
DR IntAct; Q8N5C7; 2.
DR STRING; 9606.ENSP00000251250; -.
DR iPTMnet; Q8N5C7; -.
DR PhosphoSitePlus; Q8N5C7; -.
DR BioMuta; DTWD1; -.
DR DMDM; 74728976; -.
DR EPD; Q8N5C7; -.
DR jPOST; Q8N5C7; -.
DR MassIVE; Q8N5C7; -.
DR MaxQB; Q8N5C7; -.
DR PaxDb; Q8N5C7; -.
DR PeptideAtlas; Q8N5C7; -.
DR PRIDE; Q8N5C7; -.
DR ProteomicsDB; 72032; -. [Q8N5C7-1]
DR ProteomicsDB; 72033; -. [Q8N5C7-2]
DR ProteomicsDB; 72034; -. [Q8N5C7-3]
DR TopDownProteomics; Q8N5C7-2; -. [Q8N5C7-2]
DR Antibodypedia; 65167; 156 antibodies from 20 providers.
DR DNASU; 56986; -.
DR Ensembl; ENST00000251250.7; ENSP00000251250.6; ENSG00000104047.15. [Q8N5C7-1]
DR Ensembl; ENST00000403028.8; ENSP00000385399.3; ENSG00000104047.15. [Q8N5C7-1]
DR Ensembl; ENST00000557968.5; ENSP00000452628.1; ENSG00000104047.15. [Q8N5C7-3]
DR Ensembl; ENST00000558653.5; ENSP00000453529.1; ENSG00000104047.15. [Q8N5C7-1]
DR GeneID; 56986; -.
DR KEGG; hsa:56986; -.
DR MANE-Select; ENST00000403028.8; ENSP00000385399.3; NM_001144955.2; NP_001138427.1.
DR UCSC; uc001zxq.4; human. [Q8N5C7-1]
DR CTD; 56986; -.
DR DisGeNET; 56986; -.
DR GeneCards; DTWD1; -.
DR HGNC; HGNC:30926; DTWD1.
DR HPA; ENSG00000104047; Low tissue specificity.
DR neXtProt; NX_Q8N5C7; -.
DR OpenTargets; ENSG00000104047; -.
DR PharmGKB; PA142671942; -.
DR VEuPathDB; HostDB:ENSG00000104047; -.
DR eggNOG; KOG3795; Eukaryota.
DR GeneTree; ENSGT00940000153766; -.
DR HOGENOM; CLU_069451_0_1_1; -.
DR InParanoid; Q8N5C7; -.
DR OMA; VNAWGLN; -.
DR OrthoDB; 824721at2759; -.
DR PhylomeDB; Q8N5C7; -.
DR TreeFam; TF324733; -.
DR PathwayCommons; Q8N5C7; -.
DR SignaLink; Q8N5C7; -.
DR BioGRID-ORCS; 56986; 25 hits in 1035 CRISPR screens.
DR ChiTaRS; DTWD1; human.
DR GeneWiki; DTWD1; -.
DR GenomeRNAi; 56986; -.
DR Pharos; Q8N5C7; Tdark.
DR PRO; PR:Q8N5C7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8N5C7; protein.
DR Bgee; ENSG00000104047; Expressed in calcaneal tendon and 173 other tissues.
DR ExpressionAtlas; Q8N5C7; baseline and differential.
DR Genevisible; Q8N5C7; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR InterPro; IPR005636; DTW.
DR Pfam; PF03942; DTW; 1.
DR SMART; SM01144; DTW; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..304
FT /note="tRNA-uridine aminocarboxypropyltransferase 1"
FT /id="PRO_0000308212"
FT MOTIF 206..209
FT /note="DXTW"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..88
FT /note="MSLNPPIFLKRSEENSSKFVETKQSQTTSIASEDPLQNLCLASQEVLQKAQQ
FT SGRSKCLKCGGSRMFYCYTCYVPVENVPIEQIPLVK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028922"
FT VAR_SEQ 89..304
FT /note="LPLKIDIIKHPNETDGKSTAIHAKLLAPEFVNIYTYPCIPEYEEKDHEVALI
FT FPGPQSISIKDISFHLQKRIQNNVRGKNDDPDKPSFKRKRTEEQEFCDLNDSKCKGTTL
FT KKIIFIDSTWNQTNKIFTDERLQGLLQVELKTRKTCFWRHQKGKPDTFLSTIEAIYYFL
FT VDYHTDILKEKYRGQYDNLLFFYSFMYQLIKNAKCSGDKETGKLTH -> FSLYHLGQS
FT MVSSASKITCIG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028923"
FT VARIANT 9
FT /note="L -> P (in dbSNP:rs11539522)"
FT /id="VAR_036757"
FT VARIANT 13
FT /note="E -> K (in dbSNP:rs11539519)"
FT /id="VAR_036758"
FT VARIANT 25
FT /note="S -> P (in dbSNP:rs11539521)"
FT /id="VAR_036759"
SQ SEQUENCE 304 AA; 35248 MW; 8756C5CE34BA0C28 CRC64;
MSLNPPIFLK RSEENSSKFV ETKQSQTTSI ASEDPLQNLC LASQEVLQKA QQSGRSKCLK
CGGSRMFYCY TCYVPVENVP IEQIPLVKLP LKIDIIKHPN ETDGKSTAIH AKLLAPEFVN
IYTYPCIPEY EEKDHEVALI FPGPQSISIK DISFHLQKRI QNNVRGKNDD PDKPSFKRKR
TEEQEFCDLN DSKCKGTTLK KIIFIDSTWN QTNKIFTDER LQGLLQVELK TRKTCFWRHQ
KGKPDTFLST IEAIYYFLVD YHTDILKEKY RGQYDNLLFF YSFMYQLIKN AKCSGDKETG
KLTH
