ID   NEC1_NICLS              Reviewed;         229 AA.
AC   Q94EG3;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nectarin-1;
DE            EC=1.15.1.1;
DE   AltName: Full=Superoxide dismutase [Mn];
DE   Flags: Precursor;
GN   Name=NECI;
OS   Nicotiana langsdorffii x Nicotiana sanderae (Ornamental tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=164110 {ECO:0000312|EMBL:AAK95664.1};
RN   [1] {ECO:0000312|EMBL:AAK95664.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Carter C., Thornburg R.W.;
RT   "Cloning and characterization of a Nectarin I cDNA from Nicotiana
RT   langsdorffii x Nicotiana sanderae.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 33-77, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10579488; DOI=10.1023/a:1006363508648;
RA   Carter C., Graham R.A., Thornburg R.W.;
RT   "Nectarin I is a novel, soluble germin-like protein expressed in the nectar
RT   of Nicotiana sp.";
RL   Plant Mol. Biol. 41:207-216(1999).
RN   [3] {ECO:0000305}
RP   COFACTOR, SUBUNIT, AND MASS SPECTROMETRY.
RX   PubMed=10952990; DOI=10.1074/jbc.m006461200;
RA   Carter C., Thornburg R.W.;
RT   "Tobacco nectarin I. Purification and characterization as a germin-like,
RT   manganese superoxide dismutase implicated in the defense of floral
RT   reproductive tissues.";
RL   J. Biol. Chem. 275:36726-36733(2000).
CC   -!- FUNCTION: May interact with bacterial adhesins thereby protecting the
CC       reproductive tissues from microbial attack. Has no oxalate oxidase
CC       activity. {ECO:0000269|PubMed:10579488, ECO:0000303|PubMed:10579488}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10952990};
CC       Note=Binds 1 Mn(2+) ion per monomer. {ECO:0000269|PubMed:10952990};
CC   -!- SUBUNIT: Monomer. In the absence of manganese, it forms tetrameric and
CC       pentameric forms which show superoxide dismutase activity.
CC       {ECO:0000269|PubMed:10579488, ECO:0000269|PubMed:10952990}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:10579488}. Note=Found in the nectar.
CC   -!- TISSUE SPECIFICITY: Nectary tissues and to a lower level ovary. Not
CC       detected in petals, stems, leaves, roots or other floral tissues.
CC       {ECO:0000269|PubMed:10579488}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during nectar secretion, while the
CC       flowers remain open. {ECO:0000269|PubMed:10579488}.
CC   -!- MASS SPECTROMETRY: Mass=22533; Mass_error=58; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10952990};
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AF411917; AAK95664.1; -; mRNA.
DR   AlphaFoldDB; Q94EG3; -.
DR   SMR; Q94EG3; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Manganese; Metal-binding; Oxidoreductase; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:10579488"
FT   CHAIN           33..229
FT                   /note="Nectarin-1"
FT                   /id="PRO_0000010840"
FT   DOMAIN          69..217
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000250"
FT   CONFLICT        59
FT                   /note="T -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   229 AA;  24622 MW;  AEC7C89FD3E1AF63 CRC64;
     MAAFGINSKI FQSMEMAILF LLAISIDRYC FAADEDMLQD VCVADLHSKV KVNGFPCKTN
     FTAADFSSLA ISKPGATNNK FGSVVTTANV EQVPGLNTLG VSLARIDYAP GGINPPHTHP
     RASEMVFVME GELDVGFITT ANVLVSKKII KGEVFVFPRG LVHFQKNNGE VPAAVISAFN
     SQLPGTQSIP ITLFGASPPV PDDVLAQTFQ INTEDVQQIK SKFAPVKKF