Q9Y2T3 (GUAD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine deaminase
Short name=Guanase
Short name=Guanine aminase
EC=3.5.4.3

Alternative name(s):
Guanine aminohydrolase
Short name=GAH
p51-nedasin

Gene names

Name:	GDA
Synonyms:	KIAA1258

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia By similarity.
Catalytic activity	Guanine + H2O = xanthine + NH3.
Cofactor	Binds 1 zinc ion per subunit.
Pathway	Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the ATZ/TRZ family.
Sequence caution	The sequence BAA86572.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	guanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway nervous system development Traceable author statement Ref.2. Source: ProtInc purine nucleobase metabolic process Traceable author statement. Source: Reactome purine nucleotide catabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	guanine deaminase activity Inferred from experiment. Source: Reactome zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y2T3-1)

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: Q9Y2T3-2)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.

Isoform 3 (identifier: Q9Y2T3-3)

Also known as: a;

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: V → VKETIHLPASSPHPPPFP

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 454

454

Guanine deaminase

PRO_0000122298

Sites

Metal binding

82

1

Zinc; via tele nitrogen

Metal binding

84

1

Zinc; via tele nitrogen

Metal binding

240

1

Zinc; via tele nitrogen

Metal binding

330

1

Zinc By similarity

Binding site

87

1

Substrate

Binding site

213

1

Substrate

Binding site

243

1

Substrate

Binding site

279

1

Substrate

Natural variations

Alternative sequence

1 – 74

74

Missing in isoform 2.

VSP_042075

Alternative sequence

454

1

V → VKETIHLPASSPHPPPFP in isoform 3.

VSP_042076

Experimental info

Sequence conflict

316 – 318

3

LEV → ARI in AAG40469. Ref.3

Secondary structure

1

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454

Helix Strand Turn

Details...

Beta strand

11 – 19

9

Beta strand

27 – 36

10

Beta strand

40 – 47

8

Helix

48 – 50

3

Helix

51 – 57

7

Helix

62 – 64

3

Beta strand

65 – 67

3

Beta strand

73 – 76

4

Beta strand

78 – 84

7

Helix

85 – 90

6

Helix

99 – 105

7

Helix

107 – 112

6

Helix

113 – 115

3

Helix

117 – 133

17

Beta strand

136 – 142

7

Helix

147 – 160

14

Beta strand

163 – 167

5

Beta strand

175 – 177

3

Helix

184 – 201

18

Beta strand

204 – 208

5

Beta strand

210 – 212

3

Turn

215 – 217

3

Helix

220 – 232

13

Beta strand

237 – 242

6

Helix

245 – 254

10

Beta strand

258 – 260

3

Helix

261 – 266

6

Turn

267 – 269

3

Beta strand

275 – 279

5

Helix

285 – 294

10

Beta strand

297 – 300

4

Helix

302 – 307

6

Helix

315 – 320

6

Beta strand

324 – 327

4

Turn

331 – 333

3

Helix

339 – 355

17

Beta strand

358 – 361

4

Helix

365 – 372

8

Helix

374 – 379

6

Turn

383 – 385

3

Beta strand

386 – 388

3

Beta strand

397 – 400

4

Helix

414 – 417

4

Beta strand

418 – 420

3

Helix

423 – 431

9

Helix

434 – 436

3

Beta strand

437 – 442

6

Beta strand

445 – 448

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A45C868E6EEA7380	FASTA	454	51,003
	10 20 30 40 50 60 MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF 70 80 90 100 110 120 KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA 130 140 150 160 170 180 EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY 190 200 210 220 230 240 KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH 250 260 270 280 290 300 ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH 310 320 330 340 350 360 CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE 370 380 390 400 410 420 KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI 430 440 450 SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
	Isoform 2 (c) [UniParc]. Checksum: 6AD0F99117A467CE	FASTA	380	42,445
	10 20 30 40 50 60 MPGLVDTHIH ASQYSFAGSS IDLPLLEWLT KYTFPAEHRF QNIDFAEEVY TRVVRRTLKN 70 80 90 100 110 120 GTTTACYFAT IHTDSSLLLA DITDKFGQRA FVGKVCMDLN DTFPEYKETT EESIKETERF 130 140 150 160 170 180 VSEMLQKNYS RVKPIVTPRF SLSCSETLMG ELGNIAKTRD LHIQSHISEN RDEVEAVKNL 190 200 210 220 230 240 YPSYKNYTSV YDKNNLLTNK TVMAHGCYLS AEELNVFHER GASIAHCPNS NLSLSSGFLN 250 260 270 280 290 300 VLEVLKHEVK IGLGTDVAGG YSYSMLDAIR RAVMVSNILL INKVNEKSLT LKEVFRLATL 310 320 330 340 350 360 GGSQALGLDG EIGNFEVGKE FDAILINPKA SDSPIDLFYG DFFGDISEAV IQKFLYLGDD 370 380 RNIEEVYVGG KQVVPFSSSV
	Isoform 3 (a) [UniParc]. Checksum: 5B9BF9B0E1111F88	FASTA	471	52,837
	10 20 30 40 50 60 MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF 70 80 90 100 110 120 KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSSIDLPLL EWLTKYTFPA EHRFQNIDFA 130 140 150 160 170 180 EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MDLNDTFPEY 190 200 210 220 230 240 KETTEESIKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCSE TLMGELGNIA KTRDLHIQSH 250 260 270 280 290 300 ISENRDEVEA VKNLYPSYKN YTSVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH 310 320 330 340 350 360 CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE 370 380 390 400 410 420 KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI 430 440 450 460 470 SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSVKETIHL PASSPHPPPF P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein." Yuan G., Bin J.C., McKay D.J., Snyder F.F. J. Biol. Chem. 274:8175-8180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Brain.
[2]	"A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor." Kuwahara H., Araki N., Makino K., Masuko N., Honda S., Kaibuchi K., Fukunaga K., Miyamoto E., Ogawa M., Saya H. J. Biol. Chem. 274:32204-32214(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Molecular cloning of human guanine aminohydrolase." Park K.H., Seong Y.S., Park J.B. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Human guanine deaminase (GUAD) in complex with zinc and its product xanthine." Structural genomics consortium (SGC) Submitted (JAN-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND XANTHINE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF095286 mRNA. Translation: AAD25978.1.
AF019638 mRNA. Translation: AAF13301.1.
AF144745 mRNA. Translation: AAG40469.1.
AB033084 mRNA. Translation: BAA86572.1. Different initiation.
AK300418 mRNA. Translation: BAG62147.1.
AK315988 mRNA. Translation: BAH14359.1.
AL583829 Genomic DNA. No translation available.
AL590311, AL135924 Genomic DNA. Translation: CAI12631.1.
AL135924, AL590311 Genomic DNA. Translation: CAI16261.1.
CH471089 Genomic DNA. Translation: EAW62529.1.
BC053584 mRNA. Translation: AAH53584.1.

IPI

IPI00873506.
IPI00942902.

RefSeq

NP_001229434.1. NM_001242505.2.
NP_001229435.1. NM_001242506.2.
NP_001229436.1. NM_001242507.2.
NP_004284.1. NM_004293.4.

UniGene

Hs.494163.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UZ9	X-ray	2.30	A	1-454	[»]
3E0L	X-ray	2.37	A/B	1-454	[»]
4AQL	X-ray	1.99	A	1-454	[»]

ProteinModelPortal

Q9Y2T3.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-109340.

STRING

9606.ENSP00000351170.

Protein family/group databases

MEROPS

M38.981.

PTM databases

PhosphoSite

Q9Y2T3.

Polymorphism databases

DMDM

9910736.

Proteomic databases

PaxDb

Q9Y2T3.

PRIDE

Q9Y2T3.

Protocols and materials databases

DNASU

9615.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000238018; ENSP00000238018; ENSG00000119125.
ENST00000358399; ENSP00000351170; ENSG00000119125.
ENST00000475764; ENSP00000436619; ENSG00000119125.
ENST00000545168; ENSP00000437972; ENSG00000119125.

GeneID

9615.

KEGG

hsa:9615.

UCSC

uc004aiq.3. human.

Organism-specific databases

CTD

9615.

GeneCards

GC09P074729.

HGNC

HGNC:4212. GDA.

HPA

HPA019352.
HPA024099.
HPA030387.

MIM

139260. gene.

neXtProt

NX_Q9Y2T3.

PharmGKB

PA28625.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0402.

HOGENOM

HOG000257692.

HOVERGEN

HBG005930.

InParanoid

Q9Y2T3.

KO

K01487.

OMA

CFKPCEI.

PhylomeDB

Q9Y2T3.

Enzyme and pathway databases

BioCyc

MetaCyc:HS04276-MONOMER.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00603; UER00660.

Gene expression databases

ArrayExpress

Q9Y2T3.

Bgee

Q9Y2T3.

CleanEx

HS_GDA.

Genevestigator

Q9Y2T3.

GermOnline

ENSG00000119125. Homo sapiens.

Family and domain databases

InterPro

IPR006680. Amidohydro_1.
IPR014311. Guanine_deaminase.
[Graphical view]

PANTHER

PTHR11271:SF6. PTHR11271:SF6. 1 hit.

Pfam

PF01979. Amidohydro_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02967. guan_deamin. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q9Y2T3.

ChEMBL

CHEMBL3129.

EvolutionaryTrace

Q9Y2T3.

GenomeRNAi

9615.

NextBio

36069.

SOURCE

Search...

Entry information

Entry name

GUAD_HUMAN

Accession

Primary (citable) accession number: Q9Y2T3
Secondary accession number(s): B4DTY5 , Q5SZC7, Q9H335, Q9ULG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.