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TATD3_HUMAN
ID   TATD3_HUMAN             Reviewed;         274 AA.
AC   Q17R31; A6NGS3; B7Z1C1; B7Z978; B7ZLQ6; E9PJE5; E9PNH3; G3V151; Q4G0L1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Putative deoxyribonuclease TATDN3;
DE            EC=3.1.21.-;
GN   Name=TATDN3;
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] (ISOFORMS 3 AND 4).
RC   TISSUE=Uterus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   [5]
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   [6]
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-274 IN COMPLEX WITH ZINC IONS,
RP   AND COFACTOR.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the human tatD-domain protein 3 (TATDN3).";
RL   Submitted (DEC-2010) to the PDB data bank.
CC   -!- FUNCTION: Putative deoxyribonuclease.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0007744|PDB:2Y1H};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0007744|PDB:2Y1H};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q17R31-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q17R31-2; Sequence=VSP_030048;
CC       Name=3;
CC         IsoId=Q17R31-3; Sequence=VSP_044448;
CC       Name=4;
CC         IsoId=Q17R31-4; Sequence=VSP_045263;
CC       Name=5;
CC         IsoId=Q17R31-5; Sequence=VSP_044448, VSP_045742;
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH48115.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK293129; BAH11457.1; -; mRNA.
DR   EMBL; AK304557; BAH14214.1; -; mRNA.
DR   EMBL; AC104333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471100; EAW93376.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93377.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93378.1; -; Genomic_DNA.
DR   EMBL; BC048115; AAH48115.1; ALT_INIT; mRNA.
DR   EMBL; BC113638; AAI13639.1; -; mRNA.
DR   EMBL; BC117485; AAI17486.1; -; mRNA.
DR   EMBL; BC143956; AAI43957.1; -; mRNA.
DR   CCDS; CCDS31019.1; -. [Q17R31-1]
DR   CCDS; CCDS41465.1; -. [Q17R31-2]
DR   CCDS; CCDS53475.1; -. [Q17R31-3]
DR   CCDS; CCDS53476.1; -. [Q17R31-5]
DR   CCDS; CCDS53477.1; -. [Q17R31-4]
DR   RefSeq; NP_001036017.1; NM_001042552.2. [Q17R31-1]
DR   RefSeq; NP_001036018.1; NM_001042553.2. [Q17R31-2]
DR   RefSeq; NP_001139641.1; NM_001146169.1. [Q17R31-5]
DR   RefSeq; NP_001139642.1; NM_001146170.1. [Q17R31-4]
DR   RefSeq; NP_001139643.1; NM_001146171.1. [Q17R31-3]
DR   PDB; 2Y1H; X-ray; 2.50 A; A/B=5-274.
DR   PDBsum; 2Y1H; -.
DR   AlphaFoldDB; Q17R31; -.
DR   SMR; Q17R31; -.
DR   BioGRID; 126118; 6.
DR   IntAct; Q17R31; 4.
DR   STRING; 9606.ENSP00000431376; -.
DR   iPTMnet; Q17R31; -.
DR   PhosphoSitePlus; Q17R31; -.
DR   BioMuta; TATDN3; -.
DR   DMDM; 121948822; -.
DR   EPD; Q17R31; -.
DR   jPOST; Q17R31; -.
DR   MassIVE; Q17R31; -.
DR   MaxQB; Q17R31; -.
DR   PaxDb; Q17R31; -.
DR   PeptideAtlas; Q17R31; -.
DR   PRIDE; Q17R31; -.
DR   ProteomicsDB; 21114; -.
DR   ProteomicsDB; 22414; -.
DR   ProteomicsDB; 32260; -.
DR   ProteomicsDB; 61133; -. [Q17R31-1]
DR   ProteomicsDB; 61134; -. [Q17R31-2]
DR   Antibodypedia; 51781; 30 antibodies from 13 providers.
DR   DNASU; 128387; -.
DR   Ensembl; ENST00000366973.8; ENSP00000355940.4; ENSG00000203705.11. [Q17R31-2]
DR   Ensembl; ENST00000366974.9; ENSP00000355941.4; ENSG00000203705.11. [Q17R31-1]
DR   Ensembl; ENST00000526641.5; ENSP00000434801.1; ENSG00000203705.11. [Q17R31-4]
DR   Ensembl; ENST00000531963.5; ENSP00000433755.1; ENSG00000203705.11. [Q17R31-5]
DR   Ensembl; ENST00000532324.5; ENSP00000431376.1; ENSG00000203705.11. [Q17R31-3]
DR   GeneID; 128387; -.
DR   KEGG; hsa:128387; -.
DR   MANE-Select; ENST00000366974.9; ENSP00000355941.4; NM_001042552.3; NP_001036017.1.
DR   UCSC; uc001hjo.3; human. [Q17R31-1]
DR   CTD; 128387; -.
DR   GeneCards; TATDN3; -.
DR   HGNC; HGNC:27010; TATDN3.
DR   HPA; ENSG00000203705; Low tissue specificity.
DR   neXtProt; NX_Q17R31; -.
DR   OpenTargets; ENSG00000203705; -.
DR   PharmGKB; PA142670831; -.
DR   VEuPathDB; HostDB:ENSG00000203705; -.
DR   eggNOG; KOG3020; Eukaryota.
DR   GeneTree; ENSGT00720000108846; -.
DR   HOGENOM; CLU_031506_5_3_1; -.
DR   InParanoid; Q17R31; -.
DR   OMA; CHLDAGE; -.
DR   OrthoDB; 988732at2759; -.
DR   PhylomeDB; Q17R31; -.
DR   PathwayCommons; Q17R31; -.
DR   SignaLink; Q17R31; -.
DR   BioGRID-ORCS; 128387; 16 hits in 1083 CRISPR screens.
DR   ChiTaRS; TATDN3; human.
DR   GenomeRNAi; 128387; -.
DR   Pharos; Q17R31; Tdark.
DR   PRO; PR:Q17R31; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q17R31; protein.
DR   Bgee; ENSG00000203705; Expressed in left ventricle myocardium and 191 other tissues.
DR   ExpressionAtlas; Q17R31; baseline and differential.
DR   Genevisible; Q17R31; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   CDD; cd01310; TatD_DNAse; 1.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Metal-binding; Nuclease;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Putative deoxyribonuclease TATDN3"
FT                   /id="PRO_0000313595"
FT   BINDING         12
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         14
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         107
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         107
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         147
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         170
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   BINDING         218
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007744|PDB:2Y1H"
FT   VAR_SEQ         87..107
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045263"
FT   VAR_SEQ         200
FT                   /note="Q -> QLLSLFSK (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044448"
FT   VAR_SEQ         201
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030048"
FT   VAR_SEQ         228..274
FT                   /note="VRNEPWNISISAEYIAQVKGISVEEVIEVTTQNALKLFPKLRHLLQK -> Q
FT                   NILPR (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045742"
FT   CONFLICT        86
FT                   /note="K -> R (in Ref. 1; BAH11457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="A -> T (in Ref. 1; BAH11457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="E -> G (in Ref. 1; BAH14214)"
FT                   /evidence="ECO:0000305"
FT   STRAND          8..13
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           24..33
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           85..98
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           120..140
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           176..184
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           199..207
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           235..246
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           250..264
FT                   /evidence="ECO:0007829|PDB:2Y1H"
FT   HELIX           268..271
FT                   /evidence="ECO:0007829|PDB:2Y1H"
SQ   SEQUENCE   274 AA;  30333 MW;  D2428A5666E164A5 CRC64;
     MRAAGVGLVD CHCHLSAPDF DRDLDDVLEK AKKANVVALV AVAEHSGEFE KIMQLSERYN
     GFVLPCLGVH PVQGLPPEDQ RSVTLKDLDV ALPIIENYKD RLLAIGEVGL DFSPRFAGTG
     EQKEEQRQVL IRQIQLAKRL NLPVNVHSRS AGRPTINLLQ EQGAEKVLLH AFDGRPSVAM
     EGVRAGYFFS IPPSIIRSGQ KQKLVKQLPL TSICLETDSP ALGPEKQVRN EPWNISISAE
     YIAQVKGISV EEVIEVTTQN ALKLFPKLRH LLQK
 
 
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