Q9NYQ3 (HAOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxyacid oxidase 2
Short name=HAOX2
EC=1.1.3.15

Alternative name(s):
(S)-2-hydroxy-acid oxidase, peroxisomal
Cell growth-inhibiting gene 16 protein
Long chain alpha-hydroxy acid oxidase
Long-chain L-2-hydroxy acid oxidase

Gene names

Name:	HAO2
Synonyms:	HAOX2
ORF Names:	GIG16

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.
Catalytic activity	(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.
Cofactor	FMN.
Subunit structure	Homotetramer or homooctamer By similarity.
Subcellular location	Peroxisome.
Tissue specificity	Liver and kidney.
Sequence similarities	Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	(S)-2-hydroxy-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Hydroxyacid oxidase 2		PRO_0000206320
Regions
	Domain	1 – 351	351	FMN hydroxy acid dehydrogenase
	Nucleotide binding	277 – 301	25	FMN By similarity
	Motif	349 – 351	3	Microbody targeting signal Potential
Sites
	Active site	246	1	Proton acceptor By similarity
	Binding site	106	1	FMN By similarity
	Binding site	128	1	FMN By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	156	1	FMN By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	222	1	FMN By similarity
	Binding site	249	1	Substrate By similarity
	Binding site	301	1	FMN By similarity
Natural variations
	Natural variant	15	1	E → K. Corresponds to variant rs34638261 [ dbSNP | Ensembl ].		VAR_049087
	Natural variant	221	1	L → M. Corresponds to variant rs6661625 [ dbSNP | Ensembl ].		VAR_049088
Experimental info
	Sequence conflict	80	1	F → Y in AAF14000. Ref.2
	Sequence conflict	292 – 294	3	LGA → HED in AAF14000. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NYQ3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7330DE44E282947D	FASTA	351	38,839
	10 20 30 40 50 60 MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR YLRDVSEVDT 70 80 90 100 110 120 RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG ICYITSTFAS CSLEDIVIAA 130 140 150 160 170 180 PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF KALVITLDTP VCGNRRHDIR NQLRRNLTLT 190 200 210 220 230 240 DLQSPKKGNA IPYFQMTPIS TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG 250 260 270 280 290 300 IIVSNHGGRQ LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG 310 320 330 340 350 RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases." Jones J.M., Morrell J.C., Gould S.J. J. Biol. Chem. 275:12590-12597(2000) [PubMed: 10777549] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human long-chain L-2-hydroxy acid oxidase." Spielbauer B., Conzelmann E. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Identification of a human cell growth inhibiting gene." Kim J.W. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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]. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF231917 mRNA. Translation: AAF40200.1. AF203975 mRNA. Translation: AAF14000.1. AY513277 mRNA. Translation: AAT08030.1. AL359553 Genomic DNA. Translation: CAC19798.1. CH471122 Genomic DNA. Translation: EAW56699.1. BC020863 mRNA. Translation: AAH20863.1.
IPI	IPI00021109.
RefSeq	NP_001005783.1. NM_001005783.1. NP_057611.1. NM_016527.2.
UniGene	Hs.659767.
3D structure databases
ProteinModelPortal	Q9NYQ3.
SMR	Q9NYQ3. Positions 3-348.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NYQ3.
PTM databases
PhosphoSite	Q9NYQ3.
Polymorphism databases
DMDM	13124287.
Proteomic databases
PRIDE	Q9NYQ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000325945; ENSP00000316339; ENSG00000116882. ENST00000361035; ENSP00000354314; ENSG00000116882. ENST00000369420; ENSP00000358428; ENSG00000116882.
GeneID	51179.
KEGG	hsa:51179.
UCSC	uc001ehq.1. human.
Organism-specific databases
CTD	51179.
GeneCards	GC01P119913.
H-InvDB	HIX0199983.
HGNC	HGNC:4810. HAO2.
MIM	605176. gene.
neXtProt	NX_Q9NYQ3.
PharmGKB	PA29186.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000018717.
HOVERGEN	HBG051881.
InParanoid	Q9NYQ3.
PhylomeDB	Q9NYQ3.
Gene expression databases
ArrayExpress	Q9NYQ3.
Bgee	Q9NYQ3.
CleanEx	HS_HAO2.
Genevestigator	Q9NYQ3.
GermOnline	ENSG00000116882. Homo sapiens.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR012133. Alpha-hydoxy_acid_DH_FMN. IPR000262. FMN-dep_DH. IPR008259. FMN_hydac_DH_AS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K11517.
Pfam	PF01070. FMN_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITE	PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit. PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	54141.
SOURCE	Search...

Entry information

Entry name

HAOX2_HUMAN

Accession

Primary (citable) accession number: Q9NYQ3
Secondary accession number(s): Q2TU86, Q9UJS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 92 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.