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 28-JAN-2026, entry version 101. 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 superoxide + 2 H(+) = 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF132671; AAF03355.1; -; Genomic_DNA. DR AlphaFoldDB; Q9SPV5; -. DR SMR; Q9SPV5; -. DR GlyCosmos; Q9SPV5; 1 site, No reported glycans. DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell. DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-ARBA. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IEA:UniProtKB-ARBA. DR GO; GO:2000280; P:regulation of root development; IEA:UniProtKB-ARBA. DR CDD; cd02241; cupin_OxOx; 1. DR FunFam; 2.60.120.10:FF:000025; germin-like protein subfamily 2 member 1; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 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 PANTHER; PTHR31238; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 3; 1. DR Pfam; PF00190; Cupin_1; 1. DR PRINTS; PR00325; GERMIN. DR SMART; SM00835; Cupin_1; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 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 //