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Reviewed, UniProtKB/Swiss-Prot Q84UV8 (NEC3_NICLS)

Last modified May 5, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3
    EC=1.6.5.4
    EC=4.2.1.1
Alternative name(s):
    Nectarin-III
Cleaved into the following chain:
    1- Recommended name:
            Nectarin-2
Gene names
Name: NEC3
OrganismNicotiana langsdorffii x Nicotiana sanderae (Ornamental tobacco)
Taxonomic identifier164110 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

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Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (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. Ref.1

Catalytic activity

NADH + 2 monodehydroascorbate = NAD+ + 2 ascorbate. Ref.1

H2CO3 = CO2 + H2O. Ref.1

Cofactor

Zinc By similarity. UniProtKB P00918

Subcellular location

Secreted. Note: Found in the nectar. Ref.1

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. Ref.1

Developmental stage

Expressed at low levels in stage 2 nectaries. Levels then increase and expression is even throughout subsequent stages of nectary development. Ref.1

Post-translational modification

Proteolytically cleaved to produce a shorter protein, nectarin-2. Ref.1

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.1
Chain26 – 274249Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3 Ref.1
PRO_0000248263
Chain74 – 274201Nectarin-2 Ref.1
PRO_0000248264

Sites

Active site971 By similarity UniProtKB P00918
Metal binding1221Zinc; catalytic By similarity UniProtKB P00918
Metal binding1241Zinc; catalytic By similarity UniProtKB P00918
Metal binding1411Zinc; catalytic By similarity UniProtKB P00918
Site73 – 742Cleavage Ref.1

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q84UV8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4E116CF99B6BCC99

FASTA27431,495
        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

« Hide

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References

[1]"Tobacco nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities."
Carter C.J., Thornburg R.W.
Plant Mol. Biol. 54:415-425(2004) [PubMed: 15284496] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-36 AND 74-87, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, CLEAVAGE AT GLU-73, IDENTIFICATION BY MASS SPECTROMETRY.

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Cross-references

Sequence databases

AF492468 mRNA. Translation: AAO85482.1.

3D structure databases

HSSPHSSP built from PDB template 1KOQ based on UniProtKB Q50940.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.6.5.4. 276345.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018340. Carbonic_anhydrase_CAH1-like.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF2. Carbonic_anhydrase_CAH1-like. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameNEC3_NICLS
AccessionPrimary (citable) accession number: Q84UV8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: May 5, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents