Q99424 (ACOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ACOX2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	681 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids.
Catalytic activity	(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.
Cofactor	FAD By similarity.
Subunit structure	Heterodimer By similarity.
Subcellular location	Peroxisome.
Tissue specificity	Present in all tissues tested: heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Most abundant in heart, liver and kidney.
Sequence similarities	Belongs to the acyl-CoA oxidase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bile acid biosynthetic process Traceable author statement. Source: Reactome fatty acid beta-oxidation using acyl-CoA oxidase Traceable author statement. Source: Reactome
Cellular_component	peroxisomal matrix Traceable author statement. Source: Reactome
Molecular_function	3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity Inferred from electronic annotation. Source: EC acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro pristanoyl-CoA oxidase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 681	681	Peroxisomal acyl-coenzyme A oxidase 2		PRO_0000204681
Regions
	Motif	679 – 681	3	Microbody targeting signal Potential
Amino acid modifications
	Modified residue	3	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99424 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 7FAE9236FCBE6D4D	FASTA	681	76,827
	10 20 30 40 50 60 MGSPVHRVSL GDTWSRQMHP DIESERYMQS FDVERLTNIL DGGAQNTALR RKVESIIHSY 70 80 90 100 110 120 PEFSCKDNYF MTQNERYKAA MRRAFHIRLI ARRLGWLEDG RELGYAYRAL SGDVALNIHR 130 140 150 160 170 180 VFVRALRSLG SEEQIAKWDP LCKNIQIIAT YAQTELGHGT YLQGLETEAT YDAATQEFVI 190 200 210 220 230 240 HSPTLTATKW WPGDLGRSAT HALVQAQLIC SGARRGMHAF IVPIRSLQDH TPLPGIIIGD 250 260 270 280 290 300 IGPKMDFDQT DNGFLQLNHV RVPRENMLSR FAQVLPDGTY VKLGTAQSNY LPMVVVRVEL 310 320 330 340 350 360 LSGEILPILQ KACVIAMRYS VIRRQSRLRP SDPEAKVLDY QTQQQKLFPQ LAISYAFHFL 370 380 390 400 410 420 AVSLLEFFQH SYTAILNQDF SFLPELHALS TGMKAMMSEF CTQGAEMCRR ACGGHGYSKL 430 440 450 460 470 480 SGLPSLVTKL SASCTYEGEN TVLYLQVARF LVKSYLQTQM SPGSTPQRSL SPSVAYLTAP 490 500 510 520 530 540 DLARCPAQRA ADFLCPELYT TAWAHVAVRL IKDSVQHLQT LTQSGADQHE AWNQTTVIHL 550 560 570 580 590 600 QAAKVHCYYV TVKGFTEALE KLENEPAIQQ VLKRLCDLHA IHGILTNSGD FLHDAFLSGA 610 620 630 640 650 660 QVDMARTAYL DLLRLIRKDA ILLTDAFDFT DQCLNSALGC YDGNVYERLF QWAQKSPTNT 670 680 QENPAYEEYI RPLLQSWRSK L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00293125.
RefSeq	NP_003491.1. NM_003500.3.
UniGene	Hs.444959.
3D structure databases
ProteinModelPortal	Q99424.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000307697.
PTM databases
PhosphoSite	Q99424.
Polymorphism databases
DMDM	17366636.
Proteomic databases
PaxDb	Q99424.
PRIDE	Q99424.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302819; ENSP00000307697; ENSG00000168306.
GeneID	8309.
KEGG	hsa:8309.
UCSC	uc003dkl.3. human.
Organism-specific databases
CTD	8309.
GeneCards	GC03M058465.
HGNC	HGNC:120. ACOX2.
HPA	HPA038280.
MIM	601641. gene.
neXtProt	NX_Q99424.
PharmGKB	PA24444.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1960.
HOGENOM	HOG000181256.
HOVERGEN	HBG050451.
InParanoid	Q99424.
KO	K10214.
OMA	DIGPKMD.
OrthoDB	EOG46143J.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09732-MONOMER.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q99424.
Bgee	Q99424.
CleanEx	HS_ACOX2.
Genevestigator	Q99424.
GermOnline	ENSG00000168306. Homo sapiens.
Family and domain databases
Gene3D	1.10.540.10. 1 hit. 2.40.110.10. 1 hit.
InterPro	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. [Graphical view]
PANTHER	PTHR10909:SF11. PTHR10909:SF11. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNet	Search...
Other
GenomeRNAi	8309.
NextBio	31117.
SOURCE	Search...

Entry information

Entry name

ACOX2_HUMAN

Accession

Primary (citable) accession number: Q99424
Secondary accession number(s): A6NF16, B2R8U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 122 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.