Reviewed, UniProtKB/Swiss-Prot P24792 (ASO_CUCMA)

Names and origin

Protein names

Recommended name:
    L-ascorbate oxidase
      Short name=Ascorbase
      Short name=ASO
    EC=1.10.3.3

Gene names

Name:

AAO

Organism

Cucurbita maxima (Pumpkin) (Winter squash)

Taxonomic identifier

3661 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Cucurbita

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Dimer By similarity.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbate oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Ref.1
	Chain	31 – 579	549	L-ascorbate oxidase		PRO_0000002907
Regions
	Domain	33 – 152	120	Plastocyanin-like 1
	Domain	164 – 330	167	Plastocyanin-like 2
	Domain	374 – 553	180	Plastocyanin-like 3
Sites
	Metal binding	90	1	Copper 1; type 2 By similarity
	Metal binding	92	1	Copper 2; type 3 By similarity
	Metal binding	134	1	Copper 2; type 3 By similarity
	Metal binding	136	1	Copper 3; type 3 By similarity
	Metal binding	475	1	Copper 4; type 1 By similarity
	Metal binding	478	1	Copper 1; type 2 By similarity
	Metal binding	480	1	Copper 3; type 3 By similarity
	Metal binding	536	1	Copper 3; type 3 By similarity
	Metal binding	537	1	Copper 4; type 1 By similarity
	Metal binding	538	1	Copper 2; type 3 By similarity
	Metal binding	542	1	Copper 4; type 1 By similarity
	Metal binding	547	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	122	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Glycosylation	470	1	N-linked (GlcNAc...) Potential
	Disulfide bond	49 ↔ 231		By similarity
	Disulfide bond	111 ↔ 568		By similarity
	Disulfide bond	210 ↔ 223		By similarity
Experimental info
	Sequence conflict	175	1	W → C in CAA39300. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24792-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 8F5AF4CB07B276B9	FASTA	579	64,668
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	X55779 mRNA. Translation: CAA39300.1. D55677 Genomic DNA. Translation: BAA09528.1.
PIR	S11027.
3D structure databases
HSSP	HSSP built from PDB template 1AOZ based on UniProtKB P37064.
SMR	P24792. Positions 31-579.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.3. 2176.
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]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 3 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
ProDom	PD001235. Copper_blue_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03388. ascorbase. 1 hit.
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASO_CUCMA

Accession

Primary (citable) accession number: P24792
Secondary accession number(s): Q39539

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)