Tag | Content |
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CPLM ID | CPLM-011502 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Hydroxyacid oxidase 2 |
Protein Synonyms/Alias | HAOX2; (S)-2-hydroxy-acid oxidase, peroxisomal; Long chain alpha-hydroxy acid oxidase; Long-chain L-2-hydroxy acid oxidase |
Gene Name | Hao2 |
Gene Synonyms/Alias | Hao3; Haox2 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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10 | LVCLADFKAHAQKQL | acetylation | [1] | 19 | HAQKQLSKTSWDFIE | acetylation | [1] | 57 | RYLRDMSKVDTRTTI | acetylation | [1] | 139 | KSDWDFNKQMVQRAE | acetylation | [1] | 182 | LEANILLKDLRALKE | acetylation | [1] | 188 | LKDLRALKEEKPTQS | acetylation | [1] | 191 | LRALKEEKPTQSVPV | acetylation | [1] | 229 | ILKGILTKEDAELAM | acetylation | [1] | 237 | EDAELAMKHNVQGIV | acetylation | [1] | 271 | REVVAAVKGKIEVYM | acetylation | [1] | 273 | VVAAVKGKIEVYMDG | acetylation | [1] | 290 | RTGTDVLKALALGAR | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids. |
Sequence Annotation | DOMAIN 2 353 FMN hydroxy acid dehydrogenase. NP_BIND 279 303 FMN. MOTIF 351 353 Microbody targeting signal (Potential). ACT_SITE 248 248 Proton acceptor (By similarity). BINDING 106 106 FMN. BINDING 128 128 FMN. BINDING 130 130 Substrate. BINDING 156 156 FMN. BINDING 165 165 Substrate. BINDING 224 224 FMN. BINDING 251 251 Substrate (By similarity). BINDING 303 303 FMN. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase; Peroxisome; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 353 AA |
Protein Sequence | MPLVCLADFK AHAQKQLSKT SWDFIEGEAD DGITYSENIA AFKRIRLRPR YLRDMSKVDT 60 RTTIQGQEIS APICISPTAF HSIAWPDGEK STARAAQEAN ICYVISSYAS YSLEDIVAAA 120 PEGFRWFQLY MKSDWDFNKQ MVQRAEALGF KALVITIDTP VLGNRRRDKR NQLNLEANIL 180 LKDLRALKEE KPTQSVPVSF PKASFCWNDL SLLQSITRLP IILKGILTKE DAELAMKHNV 240 QGIVVSNHGG RQLDEVSASI DALREVVAAV KGKIEVYMDG GVRTGTDVLK ALALGARCIF 300 LGRPILWGLA CKGEDGVKEV LDILTAELHR CMTLSGCQSV AEISPDLIQF SRL 353 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:Compara. GO:0005777; C:peroxisome; IDA:HGNC. GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IDA:RGD. GO:0010181; F:FMN binding; IDA:RGD. GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:EC. GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:EC. GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:EC. GO:0019395; P:fatty acid oxidation; IEA:Compara. GO:0018924; P:mandelate metabolic process; IDA:RGD. GO:0051260; P:protein homooligomerization; IDA:RGD. |
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