[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-48. STRAIN=cv. Ebisu Nankin; DOI=10.1111/j.1432-1033.1990.tb19154.x; PubMed=2143984 [NCBI, ExPASy, EBI, Israel, Japan] Esaka M., Hattori T., Fujisawa K., Sakajo S., Asahi T.; "Molecular cloning and nucleotide sequence of full-length cDNA for ascorbate oxidase from cultured pumpkin cells."; Eur. J. Biochem. 191:537-541(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9210335 [NCBI, ExPASy, EBI, Israel, Japan] Kisu Y., Harada Y., Goto M., Esaka M.; "Cloning of the pumpkin ascorbate oxidase gene and analysis of a cis-acting region involved in induction by auxin."; Plant Cell Physiol. 38:631-637(1997).

Comments

FUNCTION: May be involved in a redox system involving ascorbic acid.
CATALYTIC ACTIVITY: 2 L-ascorbate + O₂ = 2 dehydroascorbate + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
SUBUNIT: Dimer (By similarity).
SUBCELLULAR LOCATION: Secreted (Potential).
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 3 plastocyanin-like domains.

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

X55779; CAA39300.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D55677; BAA09528.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11027; S11027.

3D structure databases

HSSP

P37064; 1AOZ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P24792; 31-579.

ModBase

P24792.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008447;	Molecular function: L-ascorbate oxidase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
IPR017760; L-ascorbate_oxidase_pln.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

ProDom

PD001235; Copper_blue_sub; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 1.
PS00080; MULTICOPPER_OXIDASE2; 1.

Other

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

Keywords

Copper; Direct protein sequencing; Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`
`CHAIN`	`31 579`	`549`	`L-ascorbate oxidase.`	`PRO_0000002907`
`DOMAIN`	`33 152`	`120`	`Plastocyanin-like 1.`
`DOMAIN`	`164 330`	`167`	`Plastocyanin-like 2.`
`DOMAIN`	`374 553`	`180`	`Plastocyanin-like 3.`
`METAL`	`90 90`		`Copper 1; type 2 (By similarity).`
`METAL`	`92 92`		`Copper 2; type 3 (By similarity).`
`METAL`	`134 134`		`Copper 2; type 3 (By similarity).`
`METAL`	`136 136`		`Copper 3; type 3 (By similarity).`
`METAL`	`475 475`		`Copper 4; type 1 (By similarity).`
`METAL`	`478 478`		`Copper 1; type 2 (By similarity).`
`METAL`	`480 480`		`Copper 3; type 3 (By similarity).`
`METAL`	`536 536`		`Copper 3; type 3 (By similarity).`
`METAL`	`537 537`		`Copper 4; type 1 (By similarity).`
`METAL`	`538 538`		`Copper 2; type 3 (By similarity).`
`METAL`	`542 542`		`Copper 4; type 1 (By similarity).`
`METAL`	`547 547`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`122 122`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`355 355`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`470 470`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`49 231`		`By similarity.`
`DISULFID`	`111 568`		`By similarity.`
`DISULFID`	`210 223`		`By similarity.`
`CONFLICT`	`175 175`		`W -> C (in Ref. 1; CAA39300).`

Sequence information

Length: 579 AA [This is the length of the unprocessed precursor]

Molecular weight: 64668 Da [This is the MW of the unprocessed precursor]

CRC64: 8F5AF4CB07B276B9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLQMGKAREP NFLILFFFGL ILAFGISSEG SQIRHYKWEV EYMFWAPDCN ENIVMGINGQ 

        70         80         90        100        110        120 
FPGPTIRANA GDTVVVELIN KLHTEGVVIH WHGILQRGTP WADGTASISQ CAINPGETFF 

       130        140        150        160        170        180 
YNFTVDNPGT FFYHGHLGMQ RSAGLYGSLI VDPPQGKKEP FHYDGEINLL LSDWWHQSIH 

       190        200        210        220        230        240 
KQEVGLSSKP IRWIGEPQTI LLNGRGQFDC SIAAKYDSNL EPCKLKGSEP CAPYIFHVMP 

       250        260        270        280        290        300 
KKTYRIRIAS TTALAALNFA IGNHPLLVVE ADGNYVQPFY TSDIDIYSGE SYSVLITTDQ 

       310        320        330        340        350        360 
NPSENYWVSV GTRGRHPNTP PGLTLLNYLP NSVSKLPTSP PPETPAWDDF DRSKNFTYRI 

       370        380        390        400        410        420 
TAAMGSPKPP VKSNRRIFLL NTQNVINGYV KWAINDVSLA LPPTPYLGAM KFNLLHAFDQ 

       430        440        450        460        470        480 
NPPPEVFPED YDIDTPPTNE KTKIGNGVYQ FKIGEIVDVI LQNANMMKEN LSEIHPWHLH 

       490        500        510        520        530        540 
GHDFWVLGYG DGKFTAEEES SLNLKNPPLR NTVVIFPYGW TAIRFVADNP GVWAFHCHIE 

       550        560        570 
PHLHMGMGVV FAEGVEKVGR IPTKALACGG TAKSLINNP

P24792 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