[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3036800 [NCBI, ExPASy, EBI, Israel, Japan] Miyazawa S., Hayashi H., Hijikata M., Ishii N., Furuta S., Kagamiyama H., Osumi T., Hashimoto T.; "Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase."; J. Biol. Chem. 262:8131-8137(1987).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. PubMed=3036801 [NCBI, ExPASy, EBI, Israel, Japan] Osumi T., Ishii N., Miyazawa S., Hashimoto T.; "Isolation and structural characterization of the rat acyl-CoA oxidase gene."; J. Biol. Chem. 262:8138-8143(1987).

Comments

FUNCTION: Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs.
CATALYTIC ACTIVITY: Acyl-CoA + O₂ = trans-2,3-dehydroacyl-CoA + H₂O₂.
COFACTOR: FAD.
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation .
SUBUNIT: The enzyme contains three components A, B and C, the latter two being produced from the first by a proteolytic cleavage.
SUBCELLULAR LOCATION: Peroxisome.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID P07872-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID P07872-2

Features which should be applied to build the isoform sequence: VSP_000147.
SIMILARITY: Belongs to the acyl-CoA oxidase family.

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

J02752; AAA40666.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC085743; AAH85743.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02753; AAA40667.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29328; OXRTA1.
B29328; OXRTA2.

RefSeq

NP_059036.1; -.

UniGene

Rn.31796

3D structure databases

PDB

1IS2; X-ray; 2.20 A; A/B=1-661.	[ExPASy / RCSB / EBI]
2DDH; X-ray; 2.07 A; A=1-661.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1IS2; -.
2DDH; -.

PTM databases

P07872; -.

Organism-specific databases

RGD

619757; Acox1.

Gene expression databases

ArrayExpress

P07872; -.

GermOnline

ENSRNOG00000008755; Rattus norvegicus.

Ontologies

GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997;	Molecular function: acyl-CoA oxidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0006091;	Biological process: generation of precursor metabolites and energy (inferred from sequence or structural similarity from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006693;	Biological process: prostaglandin metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

Genome annotation databases

Ensembl

ENSRNOG00000008755; Rattus norvegicus. [Contig view]

GeneID

50681; -.

KEGG

rno:50681; -.

Phylogenomic databases

HOVERGEN

P07872; -.

Other

610520; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Alternative splicing; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 661`	`661`	`Peroxisomal acyl-CoA oxidase 1, A chain.`	`PRO_0000000552`
`CHAIN`	`1 438`	`438`	`Peroxisomal acyl-CoA oxidase 1, B chain.`	`PRO_0000000553`
`CHAIN`	`439 661`	`223`	`Peroxisomal acyl-CoA oxidase 1, C chain.`	`PRO_0000000554`
`MOTIF`	`659 661`	`3`	`Microbody targeting signal.`
`MOD_RES`	`26 26`		`Phosphoserine (By similarity).`
`MOD_RES`	`267 267`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`310 310`		`Phosphoserine (By similarity).`
`MOD_RES`	`643 643`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`649 649`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`90 133`		`KLYLANFVEPVGLNYSMFIPTLLNQGTTAQQEKWMRPSQ` `ELQII -> NSVHRGHPEPLDLHLGMFLPTLLHQATAEQQERFFMPAW` `NLEIT (in isoform 2).`	`VSP_000147`
`HELIX`	`3 11`	`9`
`HELIX`	`16 24`	`9`
`HELIX`	`27 41`	`15`
`HELIX`	`44 46`	`3`
`HELIX`	`51 53`	`3`
`HELIX`	`56 77`	`22`
`HELIX`	`82 93`	`12`
`HELIX`	`101 105`	`5`
`HELIX`	`107 114`	`8`
`HELIX`	`117 123`	`7`
`HELIX`	`125 127`	`3`
`TURN`	`128 130`	`3`
`STRAND`	`134 137`	`4`
`STRAND`	`143 145`	`3`
`HELIX`	`147 149`	`3`
`STRAND`	`153 157`	`5`
`TURN`	`158 161`	`4`
`STRAND`	`162 166`	`5`
`TURN`	`170 172`	`3`
`STRAND`	`173 178`	`6`
`TURN`	`179 183`	`5`
`STRAND`	`185 195`	`11`
`STRAND`	`198 208`	`11`
`TURN`	`212 214`	`3`
`STRAND`	`221 225`	`5`
`STRAND`	`229 231`	`3`
`STRAND`	`237 248`	`12`
`HELIX`	`249 251`	`3`
`HELIX`	`275 281`	`7`
`HELIX`	`285 306`	`22`
`HELIX`	`321 323`	`3`
`HELIX`	`325 359`	`35`
`TURN`	`360 362`	`3`
`HELIX`	`367 394`	`28`
`HELIX`	`395 401`	`7`
`TURN`	`403 405`	`3`
`HELIX`	`407 414`	`8`
`HELIX`	`415 418`	`4`
`TURN`	`419 421`	`3`
`HELIX`	`424 443`	`20`
`HELIX`	`451 457`	`7`
`HELIX`	`480 506`	`27`
`TURN`	`507 509`	`3`
`HELIX`	`512 517`	`6`
`HELIX`	`520 542`	`23`
`HELIX`	`543 545`	`3`
`HELIX`	`549 569`	`21`
`HELIX`	`571 576`	`6`
`HELIX`	`582 599`	`18`
`HELIX`	`600 602`	`3`
`HELIX`	`603 608`	`6`
`HELIX`	`614 617`	`4`
`HELIX`	`628 637`	`10`
`HELIX`	`640 642`	`3`
`STRAND`	`643 646`	`4`
`HELIX`	`649 653`	`5`

Sequence information

Length: 661 AA [This is the length of the unprocessed precursor]

Molecular weight: 74679 Da [This is the MW of the unprocessed precursor]

CRC64: 24B1F10DF066C29E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY 

        70         80         90        100        110        120 
EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV GLNYSMFIPT LLNQGTTAQQ 

       130        140        150        160        170        180 
EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITQGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL 

       250        260        270        280        290        300 
KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA 

       310        320        330        340        350        360 
IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE TYLRINESIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKIYD QVRSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTMVDINSL 

       490        500        510        520        530        540 
EGLTEAYKLR AARLVEIAAK NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS 

       550        560        570        580        590        600 
DKLPKIQDKA VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR 

       610        620        630        640        650        660 
PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKHLKPLQSK 


L

P07872 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools