TATD1_HUMAN
ID TATD1_HUMAN Reviewed; 297 AA.
AC Q6P1N9; B2R5J0; Q8TD02; Q9BY40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Deoxyribonuclease TATDN1;
DE EC=3.1.21.-;
DE AltName: Full=Hepatocarcinoma high expression protein;
GN Name=TATDN1; ORFNames=CDA11;
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=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Xu Y., Wu C., He G., Huang Y., Cao Y., Ying K., Xie Y., Mao Y.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 5-295.
RG Structural genomics consortium (SGC);
RT "Structure of putative deoxyribonuclease TATDN1 isoform A.";
RL Submitted (JUL-2010) to the PDB data bank.
CC -!- FUNCTION: Deoxyribonuclease which catalyzes (in vitro) the decatenation
CC of kinetoplast DNA, which are circular DNA catenated to each other,
CC producing linear DNA molecules (By similarity). Plays an important role
CC in chromosomal segregation and cell cycle progression during eye
CC development probably via its DNA decatenation activity (By similarity).
CC {ECO:0000250|UniProtKB:Q6GML7}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q17R31};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q17R31};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1N9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1N9-2; Sequence=VSP_030045;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
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DR EMBL; AF212250; AAK14933.1; -; mRNA.
DR EMBL; AY071865; AAL61823.1; -; mRNA.
DR EMBL; AK312204; BAG35137.1; -; mRNA.
DR EMBL; CH471060; EAW92066.1; -; Genomic_DNA.
DR EMBL; CH471060; EAW92067.1; -; Genomic_DNA.
DR EMBL; BC064964; AAH64964.1; -; mRNA.
DR CCDS; CCDS55273.1; -. [Q6P1N9-2]
DR CCDS; CCDS6351.1; -. [Q6P1N9-1]
DR RefSeq; NP_001139632.1; NM_001146160.1. [Q6P1N9-2]
DR RefSeq; NP_001304819.1; NM_001317890.1.
DR RefSeq; NP_001304820.1; NM_001317891.1.
DR RefSeq; NP_114415.1; NM_032026.3. [Q6P1N9-1]
DR RefSeq; XP_016869387.1; XM_017013898.1. [Q6P1N9-2]
DR PDB; 2XIO; X-ray; 1.19 A; A=5-295.
DR PDBsum; 2XIO; -.
DR AlphaFoldDB; Q6P1N9; -.
DR SMR; Q6P1N9; -.
DR BioGRID; 123823; 86.
DR IntAct; Q6P1N9; 3.
DR STRING; 9606.ENSP00000276692; -.
DR iPTMnet; Q6P1N9; -.
DR PhosphoSitePlus; Q6P1N9; -.
DR BioMuta; TATDN1; -.
DR DMDM; 166227295; -.
DR EPD; Q6P1N9; -.
DR jPOST; Q6P1N9; -.
DR MassIVE; Q6P1N9; -.
DR MaxQB; Q6P1N9; -.
DR PaxDb; Q6P1N9; -.
DR PeptideAtlas; Q6P1N9; -.
DR PRIDE; Q6P1N9; -.
DR ProteomicsDB; 66858; -. [Q6P1N9-1]
DR ProteomicsDB; 66859; -. [Q6P1N9-2]
DR Antibodypedia; 13907; 95 antibodies from 19 providers.
DR DNASU; 83940; -.
DR Ensembl; ENST00000276692.11; ENSP00000276692.6; ENSG00000147687.19. [Q6P1N9-1]
DR Ensembl; ENST00000519548.5; ENSP00000428336.1; ENSG00000147687.19. [Q6P1N9-2]
DR GeneID; 83940; -.
DR KEGG; hsa:83940; -.
DR MANE-Select; ENST00000276692.11; ENSP00000276692.6; NM_032026.4; NP_114415.1.
DR UCSC; uc003yrd.4; human. [Q6P1N9-1]
DR CTD; 83940; -.
DR DisGeNET; 83940; -.
DR GeneCards; TATDN1; -.
DR HGNC; HGNC:24220; TATDN1.
DR HPA; ENSG00000147687; Low tissue specificity.
DR MIM; 619364; gene.
DR neXtProt; NX_Q6P1N9; -.
DR OpenTargets; ENSG00000147687; -.
DR PharmGKB; PA134971804; -.
DR VEuPathDB; HostDB:ENSG00000147687; -.
DR eggNOG; KOG3020; Eukaryota.
DR GeneTree; ENSGT00940000156272; -.
DR InParanoid; Q6P1N9; -.
DR OMA; PNEAPRI; -.
DR OrthoDB; 1224437at2759; -.
DR PhylomeDB; Q6P1N9; -.
DR TreeFam; TF324192; -.
DR PathwayCommons; Q6P1N9; -.
DR SignaLink; Q6P1N9; -.
DR BioGRID-ORCS; 83940; 14 hits in 1033 CRISPR screens.
DR ChiTaRS; TATDN1; human.
DR EvolutionaryTrace; Q6P1N9; -.
DR GenomeRNAi; 83940; -.
DR Pharos; Q6P1N9; Tbio.
DR PRO; PR:Q6P1N9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6P1N9; protein.
DR Bgee; ENSG00000147687; Expressed in body of pancreas and 105 other tissues.
DR ExpressionAtlas; Q6P1N9; baseline and differential.
DR Genevisible; Q6P1N9; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01310; TatD_DNAse; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Reference proteome.
FT CHAIN 1..297
FT /note="Deoxyribonuclease TATDN1"
FT /id="PRO_0000313590"
FT BINDING 112
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 112
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q17R31"
FT MOD_RES 27
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P8M1"
FT MOD_RES 46
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P8M1"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_030045"
FT CONFLICT 161
FT /note="M -> T (in Ref. 5; AAH64964)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:2XIO"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:2XIO"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2XIO"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:2XIO"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:2XIO"
SQ SEQUENCE 297 AA; 33602 MW; D8671A4A50E5D9B5 CRC64;
MSRFKFIDIG INLTDPMFRG IYRGVQKHQD DLQDVIGRAV EIGVKKFMIT GGNLQDSKDA
LHLAQTNGMF FSTVGCHPTR CGEFEKNNPD LYLKELLNLA ENNKGKVVAI GECGLDFDRL
QFCPKDTQLK YFEKQFELSE QTKLPMFLHC RNSHAEFLDI MKRNRDRCVG GVVHSFDGTK
EAAAALIDLD LYIGFNGCSL KTEANLEVLK SIPSEKLMIE TDAPWCGVKS THAGSKYIRT
AFPTKKKWES GHCLKDRNEP CHIIQILEIM SAVRDEDPLE LANTLYNNTI KVFFPGI