Reviewed, UniProtKB/Swiss-Prot Q7Z6V5 (ADAT2_HUMAN)

Names and origin

Protein names

Recommended name:
    tRNA-specific adenosine deaminase 2
    EC=3.5.4.-
Alternative name(s):
    tRNA-specific adenosine-34 deaminase subunit ADAT2
    Deaminase domain-containing protein 1

Gene names

Name:	ADAT2
Synonyms:	DEADC1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably participates in deamination of adenosine-34 to inosine in many tRNAs By similarity.
Cofactor	Zinc By similarity.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily.

Ontologies

Keywords
Biological process	tRNA processing
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7Z6V5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q7Z6V5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

tRNA-specific adenosine deaminase 2

PRO_0000287653

Sites

Active site

73

1

Proton donor By similarity

Metal binding

71

1

Zinc; catalytic

Metal binding

107

1

Zinc; catalytic

Metal binding

110

1

Zinc; catalytic

Natural variations

Alternative sequence

1 – 47

47

Missing in isoform 2.

VSP_025582

Secondary structure

1

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191

Helix Strand Turn

Details...

Helix

20 – 38

19

Beta strand

47 – 50

4

Helix

62 – 65

4

Helix

72 – 86

15

Helix

91 – 95

5

Beta strand

98 – 101

4

Helix

108 – 117

10

Beta strand

121 – 123

3

Beta strand

153 – 155

3

Helix

160 – 170

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7F2881A100A1782E	FASTA	191	21,046
	10 20 30 40 50 60 MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN 70 80 90 100 110 120 EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP 130 140 150 160 170 180 LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK 190 SKVRKKECQK S
	Isoform 2. Checksum: 4A697F09E3651358	FASTA	144	16,100
	10 20 30 40 50 60 MVYNNEVVGK GRNEVNQTKN ATRHAEMVAI DQVLDWCRQS GKSPSEVFEH TVLYVTVEPC 70 80 90 100 110 120 IMCAAALRLM KIPLVVYGCQ NERFGGCGSV LNIASADLPN TGRPFQCIPG YRAEEAVEML 130 140 KTFYKQENPN APKSKVRKKE CQKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Thymus.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Oesophageal carcinoma.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-191 (ISOFORM 1). Tissue: Duodenum.
[6]	"RNA editing by adenosine deaminases generates RNA and protein diversity." Schaub M., Keller W. Biochimie 84:791-803(2002) [PubMed: 12457566] [Abstract] Cited for: IDENTIFICATION.
[7]	"Crystal structure of human tRNA-specific adenosine-34 deaminase subunit ADAT2." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-185 IN COMPLEX WITH ZINC IONS.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AK126201 mRNA. Translation: BAG54295.1.
BX538182 mRNA. Translation: CAD98054.1.
AL031320 Genomic DNA. Translation: CAD92490.1.
CH471051 Genomic DNA. Translation: EAW47868.1.
BC037955 mRNA. Translation: AAH37955.2. Different initiation.

IPI

IPI00217631.
IPI00845439.

RefSeq

NP_872309.2.

UniGene

Hs.709561
Hs.7277

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DH1	X-ray	2.80	A/B/C/D	20-185	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q7Z6V5.

Proteomic databases

PRIDE

Q7Z6V5.

Genome annotation databases

Ensembl

ENST00000237283; ENSP00000237283; ENSG00000189007; Homo sapiens. [Genome view]

GeneID

134637.

KEGG

hsa:134637.

UCSC

uc003qjj.1. human.

Organism-specific databases

CTD

134637.

GeneCards

GC06M143789.

HGNC

HGNC:21172. ADAT2.

PharmGKB

PA134948508.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q7Z6V5.

OMA

QVLDWCH

OrthoDB

EOG9CJZ2V

Gene expression databases

ArrayExpress

Q7Z6V5.

Bgee

Q7Z6V5.

CleanEx

HS_ADAT2.

Genevestigator

Q7Z6V5.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

83413.

Entry information

Entry name

ADAT2_HUMAN

Accession

Primary (citable) accession number: Q7Z6V5
Secondary accession number(s): A6NL12 , B3KWY3, Q7Z327, Q8IY39

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	October 1, 2003
Last modified:	November 24, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.