NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-36 AND 74-87, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CLEAVAGE AT GLU-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1023/B:PLAN.0000036373.84579.13; PubMed=15284496 [NCBI, ExPASy, EBI, Israel, Japan]
Carter C.J., Thornburg R.W.;
"Tobacco nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities.";
Plant Mol. Biol. 54:415-425(2004).

Comments

FUNCTION: Bifunctional enzyme which has both carbonate dehydratase and monodehydroascorbate reductase activities. May be involved in regulation of nectar pH. May also regulate nectar ascorbate concentration, protecting floral tissues from free radical damage.
CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD⁺ + 2 ascorbate.
CATALYTIC ACTIVITY: H₂CO₃ = CO₂ + H₂O.
COFACTOR: Zinc (By similarity).
SUBCELLULAR LOCATION: Secreted. Note=Found in the nectar.
TISSUE SPECIFICITY: Expressed most strongly in nectary gland. Also at lower levels in the ovary, style, stigma, floral tube and at low levels in anthers/filaments.
DEVELOPMENTAL STAGE: Expressed at low levels in stage 2 nectaries. Levels then increase and expression is even throughout subsequent stages of nectary development.
PTM: Proteolytically cleaved to produce a shorter protein, nectarin-2.
SIMILARITY: Belongs to the alpha-carbonic anhydrase 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

AF492468; AAO85482.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q50940; 1KOQ. [HSSP ENTRY / PDB]

ModBase

Q84UV8.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from direct assay from UniProtKB).
GO:0004089;	Molecular function: carbonate dehydratase activity (inferred from direct assay from UniProtKB).
GO:0016656;	Molecular function: monodehydroascorbate reductase (NADH) activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006885;	Biological process: regulation of pH (non-traceable author statement from UniProtKB).
GO:0000305;	Biological process: response to oxygen radical (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001148; Euk_COanhd.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.200.10; Euk_COanhd; 1.

PANTHER

PTHR18952; Euk_COanhd; 1.

Pfam

PF00194; Carb_anhydrase; 1.
Pfam graphical view of domain structure.

ProDom

PD000865; Euk_COanhd; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00162; ALPHA_CA_1; 1.
PS51144; ALPHA_CA_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Direct protein sequencing; Glycoprotein; Lyase; Metal-binding; NAD; Oxidoreductase; Secreted; Signal; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`
`CHAIN`	`26 274`	`249`	`Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3.`	`PRO_0000248263`
`CHAIN`	`74 274`	`201`	`Nectarin-2.`	`PRO_0000248264`
`ACT_SITE`	`97 97`		`By similarity.`
`METAL`	`122 122`		`Zinc; catalytic (By similarity).`
`METAL`	`124 124`		`Zinc; catalytic (By similarity).`
`METAL`	`141 141`		`Zinc; catalytic (By similarity).`
`SITE`	`73 74`	`2`	`Cleavage.`
`CARBOHYD`	`89 89`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`112 112`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`262 262`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 274 AA [This is the length of the unprocessed precursor]

Molecular weight: 31495 Da [This is the MW of the unprocessed precursor]

CRC64: 4E116CF99B6BCC99 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRMAAITKML FISFLFLSSV FLARSGEVDD ESEFSYDEKS ENGPANWGNI RPDWKECSGK 

        70         80         90        100        110        120 
LQSPIDIFDL RAEVVSNLRI LQKDYKPSNA TLLNRGHDIM LRLDDGGYLK INETQYQLKQ 

       130        140        150        160        170        180 
LHWHTPSEHT INGERFNLEA HLVHESNNGK FVVIGIVYEI GLWPDPFLSM IENDLKVPAN 

       190        200        210        220        230        240 
KKGIERGIGI IDPNQIKLDG KKYFRYIGSL TTPPCTEGVV WIIDRKVKTV TRRQIKLLQE 

       250        260        270 
AVHDGFETNA RPTQPENERY INSTYHSFGI EKQQ

Q84UV8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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