NEC1_NICPL
ID NEC1_NICPL Reviewed; 229 AA.
AC Q9SPV5;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Nectarin-1;
DE EC=1.15.1.1;
DE AltName: Full=Superoxide dismutase [Mn];
DE Flags: Precursor;
GN Name=NEC1;
OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex 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=4092;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 129-137.
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).
CC -!- FUNCTION: May interact with bacterial adhesins thereby protecting the
CC reproductive tissues from microbial attack. Has no oxalate oxidase
CC activity (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per monomer. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable.;
CC -!- SUBUNIT: Monomer. In the absence of manganese, it forms tetrameric and
CC pentameric forms which show superoxide dismutase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250}. Note=Secreted in the nectar. {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; AF132671; AAF03355.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9SPV5; -.
DR SMR; Q9SPV5; -.
DR PRIDE; Q9SPV5; -.
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:0000250"
FT CHAIN 33..229
FT /note="Nectarin-1"
FT /id="PRO_0000010841"
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 /evidence="ECO:0000255"
FT DISULFID 42..57
FT /evidence="ECO:0000250"
SQ SEQUENCE 229 AA; 24765 MW; DBB8AE087F8256DE CRC64;
MAAFGIKSKI FQIMEMTILF LFAISIDRYC FAADEDMLQD VCVADLHSKV KVNGFPCKTN
FTAADFSSFA ISKPGATNNK FGSKVTTANV EQVPGLNTLG VSLARIDYAP GGINPPHTHP
RASEMVFVME GELDVGFITT ANVLVSKQIT KGEVFVFPRG LVHFQKNNGK IPAAVVSAFN
SQLPGTQSIP ITLFGASPTV PDDVLAQTFQ INIEDVQQIK SKFAPAKKF