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Q99424

- ACOX2_HUMAN

UniProt

Q99424 - ACOX2_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ99424.
CleanExiHS_ACOX2.
ExpressionAtlasiQ99424. baseline and differential.
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.
GeneTreeiENSGT00530000062919.
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

        10         20         30         40         50
MGSPVHRVSL GDTWSRQMHP DIESERYMQS FDVERLTNIL DGGAQNTALR
60 70 80 90 100
RKVESIIHSY PEFSCKDNYF MTQNERYKAA MRRAFHIRLI ARRLGWLEDG
110 120 130 140 150
RELGYAYRAL SGDVALNIHR VFVRALRSLG SEEQIAKWDP LCKNIQIIAT
160 170 180 190 200
YAQTELGHGT YLQGLETEAT YDAATQEFVI HSPTLTATKW WPGDLGRSAT
210 220 230 240 250
HALVQAQLIC SGARRGMHAF IVPIRSLQDH TPLPGIIIGD IGPKMDFDQT
260 270 280 290 300
DNGFLQLNHV RVPRENMLSR FAQVLPDGTY VKLGTAQSNY LPMVVVRVEL
310 320 330 340 350
LSGEILPILQ KACVIAMRYS VIRRQSRLRP SDPEAKVLDY QTQQQKLFPQ
360 370 380 390 400
LAISYAFHFL AVSLLEFFQH SYTAILNQDF SFLPELHALS TGMKAMMSEF
410 420 430 440 450
CTQGAEMCRR ACGGHGYSKL SGLPSLVTKL SASCTYEGEN TVLYLQVARF
460 470 480 490 500
LVKSYLQTQM SPGSTPQRSL SPSVAYLTAP DLARCPAQRA ADFLCPELYT
510 520 530 540 550
TAWAHVAVRL IKDSVQHLQT LTQSGADQHE AWNQTTVIHL QAAKVHCYYV
560 570 580 590 600
TVKGFTEALE KLENEPAIQQ VLKRLCDLHA IHGILTNSGD FLHDAFLSGA
610 620 630 640 650
QVDMARTAYL DLLRLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF
660 670 680
QWAQKSPTNT QENPAYEEYI RPLLQSWRSK L
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.
GeneTreei ENSGT00530000062919.
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

Bgeei Q99424.
CleanExi HS_ACOX2.
ExpressionAtlasi Q99424. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 135 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