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Q99424

- ACOX2_HUMAN

UniProt

Q99424 - ACOX2_HUMAN

Protein

Peroxisomal acyl-coenzyme A oxidase 2

Gene

ACOX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.

    Catalytic activityi

    (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestan-26-oyl-CoA + reduced acceptor.

    Cofactori

    FAD.By similarity

    GO - Molecular functioni

    1. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity Source: UniProtKB-EC
    2. acyl-CoA dehydrogenase activity Source: InterPro
    3. acyl-CoA oxidase activity Source: Reactome
    4. flavin adenine dinucleotide binding Source: InterPro
    5. pristanoyl-CoA oxidase activity Source: Reactome
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. bile acid biosynthetic process Source: Reactome
    2. bile acid metabolic process Source: Reactome
    3. cellular lipid metabolic process Source: Reactome
    4. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09732-MONOMER.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_17017. Beta-oxidation of pristanoyl-CoA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal acyl-coenzyme A oxidase 2 (EC:1.17.99.3)
    Alternative name(s):
    3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
    3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
    Trihydroxycoprostanoyl-CoA oxidase
    Short name:
    THCA-CoA oxidase
    Short name:
    THCCox
    Gene namesi
    Name:ACOX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:120. ACOX2.

    Subcellular locationi

    GO - Cellular componenti

    1. peroxisomal matrix Source: Reactome
    2. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24444.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 681681Peroxisomal acyl-coenzyme A oxidase 2PRO_0000204681Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei66 – 661N6-succinyllysineBy similarity
    Modified residuei137 – 1371N6-succinyllysineBy similarity
    Modified residuei453 – 4531N6-succinyllysineBy similarity
    Modified residuei561 – 5611N6-succinyllysineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99424.
    PaxDbiQ99424.
    PRIDEiQ99424.

    PTM databases

    PhosphoSiteiQ99424.

    Expressioni

    Tissue specificityi

    Present in all tissues tested: heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Most abundant in heart, liver and kidney.

    Gene expression databases

    ArrayExpressiQ99424.
    BgeeiQ99424.
    CleanExiHS_ACOX2.
    GenevestigatoriQ99424.

    Organism-specific databases

    HPAiHPA038280.

    Interactioni

    Subunit structurei

    Heterodimer.By similarity

    Protein-protein interaction databases

    BioGridi113906. 1 interaction.
    STRINGi9606.ENSP00000307697.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99424.
    SMRiQ99424. Positions 18-671.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi679 – 6813Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the acyl-CoA oxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG1960.
    HOGENOMiHOG000181256.
    HOVERGENiHBG050451.
    InParanoidiQ99424.
    KOiK10214.
    OMAiAFDFTDQ.
    PhylomeDBiQ99424.
    TreeFamiTF300672.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR029320. Acyl-CoA_ox_N.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMiSSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q99424-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSPVHRVSL GDTWSRQMHP DIESERYMQS FDVERLTNIL DGGAQNTALR    50
    RKVESIIHSY PEFSCKDNYF MTQNERYKAA MRRAFHIRLI ARRLGWLEDG 100
    RELGYAYRAL SGDVALNIHR VFVRALRSLG SEEQIAKWDP LCKNIQIIAT 150
    YAQTELGHGT YLQGLETEAT YDAATQEFVI HSPTLTATKW WPGDLGRSAT 200
    HALVQAQLIC SGARRGMHAF IVPIRSLQDH TPLPGIIIGD IGPKMDFDQT 250
    DNGFLQLNHV RVPRENMLSR FAQVLPDGTY VKLGTAQSNY LPMVVVRVEL 300
    LSGEILPILQ KACVIAMRYS VIRRQSRLRP SDPEAKVLDY QTQQQKLFPQ 350
    LAISYAFHFL AVSLLEFFQH SYTAILNQDF SFLPELHALS TGMKAMMSEF 400
    CTQGAEMCRR ACGGHGYSKL SGLPSLVTKL SASCTYEGEN TVLYLQVARF 450
    LVKSYLQTQM SPGSTPQRSL SPSVAYLTAP DLARCPAQRA ADFLCPELYT 500
    TAWAHVAVRL IKDSVQHLQT LTQSGADQHE AWNQTTVIHL QAAKVHCYYV 550
    TVKGFTEALE KLENEPAIQQ VLKRLCDLHA IHGILTNSGD FLHDAFLSGA 600
    QVDMARTAYL DLLRLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF 650
    QWAQKSPTNT QENPAYEEYI RPLLQSWRSK L 681
    Length:681
    Mass (Da):76,827
    Last modified:May 1, 1997 - v1
    Checksum:i7FAE9236FCBE6D4D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95190 mRNA. Translation: CAA64489.1.
    AJ001541
    , AJ001542, AJ001543, AJ001544, AJ001545, AJ001546, AJ001547, AJ001548 Genomic DNA. Translation: CAB65596.1.
    AK313512 mRNA. Translation: BAG36292.1.
    AC116036 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65375.1.
    BC047700 mRNA. Translation: AAH47700.1.
    CCDSiCCDS33775.1.
    RefSeqiNP_003491.1. NM_003500.3.
    XP_005265562.1. XM_005265505.1.
    UniGeneiHs.444959.

    Genome annotation databases

    EnsembliENST00000302819; ENSP00000307697; ENSG00000168306.
    GeneIDi8309.
    KEGGihsa:8309.
    UCSCiuc003dkl.3. human.

    Polymorphism databases

    DMDMi17366636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95190 mRNA. Translation: CAA64489.1 .
    AJ001541
    , AJ001542 , AJ001543 , AJ001544 , AJ001545 , AJ001546 , AJ001547 , AJ001548 Genomic DNA. Translation: CAB65596.1 .
    AK313512 mRNA. Translation: BAG36292.1 .
    AC116036 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65375.1 .
    BC047700 mRNA. Translation: AAH47700.1 .
    CCDSi CCDS33775.1.
    RefSeqi NP_003491.1. NM_003500.3.
    XP_005265562.1. XM_005265505.1.
    UniGenei Hs.444959.

    3D structure databases

    ProteinModelPortali Q99424.
    SMRi Q99424. Positions 18-671.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113906. 1 interaction.
    STRINGi 9606.ENSP00000307697.

    PTM databases

    PhosphoSitei Q99424.

    Polymorphism databases

    DMDMi 17366636.

    Proteomic databases

    MaxQBi Q99424.
    PaxDbi Q99424.
    PRIDEi Q99424.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302819 ; ENSP00000307697 ; ENSG00000168306 .
    GeneIDi 8309.
    KEGGi hsa:8309.
    UCSCi uc003dkl.3. human.

    Organism-specific databases

    CTDi 8309.
    GeneCardsi GC03M058490.
    HGNCi HGNC:120. ACOX2.
    HPAi HPA038280.
    MIMi 601641. gene.
    neXtProti NX_Q99424.
    PharmGKBi PA24444.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1960.
    HOGENOMi HOG000181256.
    HOVERGENi HBG050451.
    InParanoidi Q99424.
    KOi K10214.
    OMAi AFDFTDQ.
    PhylomeDBi Q99424.
    TreeFami TF300672.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09732-MONOMER.
    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_17017. Beta-oxidation of pristanoyl-CoA.

    Miscellaneous databases

    GenomeRNAii 8309.
    NextBioi 31117.
    PROi Q99424.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99424.
    Bgeei Q99424.
    CleanExi HS_ACOX2.
    Genevestigatori Q99424.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR029320. Acyl-CoA_ox_N.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR012258. Acyl-CoA_oxidase.
    IPR002655. Acyl-CoA_oxidase_C.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF01756. ACOX. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF14749. Acyl-CoA_ox_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000168. Acyl-CoA_oxidase. 1 hit.
    SUPFAMi SSF47203. SSF47203. 2 hits.
    SSF56645. SSF56645. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger's syndrome."
      Baumgart E., Vanhooren J.C.T., Fransen M., Marynen P., Puype M., Vandekerckhove J., Leunissen J.A.M., Fahimi H.D., Mannaerts G.P., Van Veldhoven P.P.
      Proc. Natl. Acad. Sci. U.S.A. 93:13748-13753(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-14; 271-282; 337-346; 450-468 AND 656-664.
      Tissue: Liver.
    2. "Genomic sequence of peroxisomal human branched chain acyl-CoA oxidase."
      Fournier B., Baumgart E., Fahimi D., Mannaerts G.P., Van Veldhoven P.P.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
      Tissue: Kidney.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.

    Entry informationi

    Entry nameiACOX2_HUMAN
    AccessioniPrimary (citable) accession number: Q99424
    Secondary accession number(s): A6NF16, B2R8U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3