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UniProtKB/Swiss-Prot entry Q9NYQ3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HAOX2_HUMAN
Primary accession number Q9NYQ3
Secondary accession number Q9UJS6
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name Hydroxyacid oxidase 2
Synonyms HAOX2
EC 1.1.3.15
(S)-2-hydroxy-acid oxidase, peroxisomal
Long chain alpha-hydroxy acid oxidase
Long-chain L-2-hydroxy acid oxidase
Gene name
Name: HAO2
Synonyms: HAOX2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.275.17.12590; PubMed=10777549 [NCBI, ExPASy, EBI, Israel, Japan]
Jones J.M., Morrell J.C., Gould S.J.;
"Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.";
J. Biol. Chem. 275:12590-12597(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Spielbauer B., Conzelmann E.;
"Human long-chain L-2-hydroxy acid oxidase.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF231917; AAF40200.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF203975; AAF14000.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL359553; CAC19798.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020863; AAH20863.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001005783.1; -.
NP_057611.1; -.
UniGene Hs.659767
3D structure databases
HSSP P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q9NYQ3.
Organism-specific databases
H-InvDB HIX0000947; -.
HGNC HGNC:4810; HAO2.
GenAtlas HAO2.
MIM 605176; gene. [NCBI / EBI]
PharmGKB PA29186; -.
GeneCards Q9NYQ3.
Gene expression databases
ArrayExpress Q9NYQ3; -.
CleanEx HS_HAO2; -.
GermOnline ENSG00000116882; Homo sapiens.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (traceable author statement from UniProtKB).
GO:0003973; Molecular function: (S)-2-hydroxy-acid oxidase activity (traceable author statement from UniProtKB).
GO:0001561; Biological process: fatty acid alpha-oxidation (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000138; Al-hdrx_acd_dh; 1.
PROSITE PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9NYQ3.
Genome annotation databases
Ensembl ENSG00000116882; Homo sapiens. [Contig view]
GeneID 51179; -.
KEGG hsa:51179; -.
Phylogenomic databases
HOGENOM Q9NYQ3; -.
HOVERGEN Q9NYQ3; -.
Other
SOURCE HAO2; Homo sapiens.
ProtoNet Q9NYQ3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Flavoprotein; FMN; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   351  351     Hydroxyacid oxidase 2. PRO_0000206320
DOMAIN   1   351  351     FMN hydroxy acid dehydrogenase. 
NP_BIND   277   301  25     FMN (By similarity). 
MOTIF   349   351  3     Microbody targeting signal (Potential). 
ACT_SITE   246   246        Proton acceptor (By similarity). 
BINDING   106   106        FMN (By similarity). 
BINDING   128   128        FMN (By similarity). 
BINDING   130   130        Substrate (By similarity). 
BINDING   156   156        FMN (By similarity). 
BINDING   165   165        Substrate (By similarity). 
BINDING   222   222        FMN (By similarity). 
BINDING   249   249        Substrate (Potential). 
CONFLICT   80    80        F -> Y (in Ref. 2; AAF14000). 
CONFLICT   292   294        LGA -> HED (in Ref. 2; AAF14000). 
Sequence information
Length: 351 AA [This is the length of the unprocessed precursor] Molecular weight: 38839 Da [This is the MW of the unprocessed precursor] CRC64: 7330DE44E282947D [This is a checksum on the sequence]
        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 

Q9NYQ3 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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