LECR_PEA
ID LECR_PEA Reviewed; 270 AA.
AC Q40987;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Nodule lectin;
DE AltName: Full=PsNlec-1;
DE Flags: Precursor;
GN Name=NLEC1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC49367.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-56, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC STRAIN=cv. Wisconsin Perfection {ECO:0000312|EMBL:AAC49367.1};
RC TISSUE=Root nodule {ECO:0000312|EMBL:AAC49367.1};
RX PubMed=8685275; DOI=10.1104/pp.111.1.49;
RA Kardailsky I.V., Sherrier D.J., Brewin N.J.;
RT "Identification of a new pea gene, PsNlec1, encoding a lectin-like
RT glycoprotein isolated from the symbiosomes of root nodules.";
RL Plant Physiol. 111:49-60(1996).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=9414555; DOI=10.1104/pp.115.4.1431;
RA Dahiya P., Kardailsky I.V., Brewin N.J.;
RT "Immunolocalization of PsNLEC-1, a lectin-like glycoprotein expressed in
RT developing pea nodules.";
RL Plant Physiol. 115:1431-1442(1997).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RA Balestrini B., Perotto N., Gasverde E., Dahiya P., Guldmann L.-L.,
RA Brewin N.J., Bonfante P.;
RT "Transcription of a gene encoding a lectin-like glycoprotein is induced in
RT root cells harboring arbuscular mycorrhizal fungi in Pisum sativum.";
RL Mol. Plant Microbe Interact. 12:785-791(1999).
RN [4] {ECO:0000305}
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=11332730; DOI=10.1094/mpmi.2001.14.5.663;
RA Bolanos L., Cebrian A., Redondo-Nieto M., Rivilla R., Bonilla I.;
RT "Lectin-like glycoprotein PsNLEC-1 is not correctly glycosylated and
RT targeted in boron-deficient pea nodules.";
RL Mol. Plant Microbe Interact. 14:663-670(2001).
RN [5] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11921448;
RX DOI=10.1002/1615-9861(200203)2:3<325::aid-prot325>3.0.co;2-w;
RA Saalbach G., Erik P., Wienkoop S.;
RT "Characterisation by proteomics of peribacteroid space and peribacteroid
RT membrane preparations from pea (Pisum sativum) symbiosomes.";
RL Proteomics 2:325-337(2002).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=14964535; DOI=10.1094/mpmi.2004.17.2.216;
RA Bolanos L., Redondo-Nieto M., Rivilla R., Brewin N.J., Bonilla I.;
RT "Cell surface interactions of Rhizobium bacteroids and other bacterial
RT strains with symbiosomal and peribacteroid membrane components from pea
RT nodules.";
RL Mol. Plant Microbe Interact. 17:216-223(2004).
CC -!- FUNCTION: Involved in symbiosome development.
CC {ECO:0000269|PubMed:11332730}.
CC -!- SUBCELLULAR LOCATION: Symbiosome, peribacteroid space. Symbiosome,
CC peribacteroid membrane. Note=Also associates directly or indirectly
CC with the cell surface of Rhizobium bacteroids within the symbiosome.
CC Glycosylation variants NLEC-1A and NLEC-1B are abundant in the
CC peribacterial space while NLEC-1C is probably cytoplasmic.
CC -!- TISSUE SPECIFICITY: Expressed in nodules of Rhizobium-infected and
CC uninfected roots and in the root stele near the nodule attachment
CC point. In roots which have been colonized by the endomycorrhizal fungus
CC G.versiforme, detected only in cortical cells colonized by the fungus,
CC mainly those containing arbuscules. {ECO:0000269|PubMed:8685275,
CC ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Expression increases gradually as nodules develop
CC and then remains constant from 4 weeks to 2 months. Expressed at lower
CC levels in senescing and non-fixing nodules.
CC {ECO:0000269|PubMed:8685275}.
CC -!- INDUCTION: By infection with the endomycorrhizal fungus G.versiforme.
CC {ECO:0000269|Ref.3}.
CC -!- PTM: Glycosylated in a boron-dependent manner. Glycosylation is
CC required for localization to symbiosomes. 3 different glycosylation
CC variants, NLEC-1A, NLEC-1B and NLEC-1C, have been identified.
CC {ECO:0000269|PubMed:11332730, ECO:0000269|PubMed:8685275,
CC ECO:0000269|PubMed:9414555}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR EMBL; U31981; AAC49367.1; -; mRNA.
DR PIR; T06528; T06528.
DR AlphaFoldDB; Q40987; -.
DR SMR; Q40987; -.
DR GO; GO:0043662; C:peribacteroid fluid; IEA:UniProtKB-SubCell.
DR GO; GO:0043661; C:peribacteroid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0044403; P:biological process involved in symbiotic interaction; NAS:UniProtKB.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Lectin; Membrane; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..41
FT /evidence="ECO:0000255, ECO:0000269|PubMed:8685275"
FT /id="PRO_0000245800"
FT CHAIN 42..270
FT /note="Nodule lectin"
FT /evidence="ECO:0000269|PubMed:8685275"
FT /id="PRO_0000245801"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="F -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 28958 MW; 648D9CDBF8E5E2E3 CRC64;
MAFYRTNLPT RELFSLVSVV IVLLATNINS VQALSFNFTK LTTANSGVTF QGDAQILPSG
LIALTKSSPF PPGQYFTTVG RALSSNLVPL WDSATGKAAS FVTSFSFVID TTEGPITDGL
IFFIAPPGTV IPQNSTTPFL GVVDSETSIN RFVGLEFDLY RNSWDPEGRH IGIDINSIIS
TKTVTYNLVS GSLTKVIIIY DSPSSTLSAA IIYENGKIST ISQVIDLKTV LPNTVQIGLS
AATLTGESYS IHSWSFVSDL ETTASYVSNI
