ID   NEC3_NICLS              Reviewed;         274 AA.
AC   Q84UV8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 25.
DE   RecName: Full=Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3;
DE            EC=1.6.5.4;
DE            EC=4.2.1.1;
DE   AltName: Full=Nectarin-III;
DE   Contains:
DE     RecName: Full=Nectarin-2;
DE   Flags: Precursor;
GN   Name=NEC3;
OS   Nicotiana langsdorffii x Nicotiana sanderae (Ornamental tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=164110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-36 AND 74-87,
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, CLEAVAGE AT GLU-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15284496; DOI=10.1023/B:PLAN.0000036373.84579.13;
RA   Carter C.J., Thornburg R.W.;
RT   "Tobacco nectarin III is a bifunctional enzyme with
RT   monodehydroascorbate reductase and carbonic anhydrase activities.";
RL   Plant Mol. Biol. 54:415-425(2004).
CC   -!- FUNCTION: Bifunctional enzyme which has both carbonate dehydratase
CC       and monodehydroascorbate reductase activities. May be involved in
CC       regulation of nectar pH. May also regulate nectar ascorbate
CC       concentration, protecting floral tissues from free radical damage.
CC   -!- CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD(+) + 2
CC       ascorbate.
CC   -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Found in the nectar.
CC   -!- TISSUE SPECIFICITY: Expressed most strongly in nectary gland. Also
CC       at lower levels in the ovary, style, stigma, floral tube and at
CC       low levels in anthers/filaments.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels in stage 2 nectaries.
CC       Levels then increase and expression is even throughout subsequent
CC       stages of nectary development.
CC   -!- PTM: Proteolytically cleaved to produce a shorter protein,
CC       nectarin-2.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
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DR   EMBL; AF492468; AAO85482.1; -; mRNA.
DR   HSSP; Q50940; 1KOQ.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006885; P:regulation of pH; NAS:UniProtKB.
DR   GO; GO:0000305; P:response to oxygen radical; NAS:UniProtKB.
DR   InterPro; IPR001148; Euk_COanhd.
DR   Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1.
DR   PANTHER; PTHR18952; Euk_COanhd; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   ProDom; PD000865; Euk_COanhd; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Lyase; Metal-binding; NAD;
KW   Oxidoreductase; Secreted; Signal; Zinc.
FT   SIGNAL        1     25
FT   CHAIN        26    274       Bifunctional monodehydroascorbate
FT                                reductase and carbonic anhydrase
FT                                nectarin-3.
FT                                /FTId=PRO_0000248263.
FT   CHAIN        74    274       Nectarin-2.
FT                                /FTId=PRO_0000248264.
FT   ACT_SITE     97     97       By similarity.
FT   METAL       122    122       Zinc; catalytic (By similarity).
FT   METAL       124    124       Zinc; catalytic (By similarity).
FT   METAL       141    141       Zinc; catalytic (By similarity).
FT   SITE         73     74       Cleavage.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    112    112       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    262    262       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   274 AA;  31495 MW;  4E116CF99B6BCC99 CRC64;
     MRMAAITKML FISFLFLSSV FLARSGEVDD ESEFSYDEKS ENGPANWGNI RPDWKECSGK
     LQSPIDIFDL RAEVVSNLRI LQKDYKPSNA TLLNRGHDIM LRLDDGGYLK INETQYQLKQ
     LHWHTPSEHT INGERFNLEA HLVHESNNGK FVVIGIVYEI GLWPDPFLSM IENDLKVPAN
     KKGIERGIGI IDPNQIKLDG KKYFRYIGSL TTPPCTEGVV WIIDRKVKTV TRRQIKLLQE
     AVHDGFETNA RPTQPENERY INSTYHSFGI EKQQ
//