CLE2_HETGL
ID CLE2_HETGL Reviewed; 138 AA.
AC Q86RQ1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 2;
DE Short=CLE-like peptide 2;
DE AltName: Full=Gland-specific protein G4G12;
DE Short=Hg-G4G12;
DE Flags: Precursor;
GN Name=CLE2; Synonyms=G4G12;
OS Heterodera glycines (Soybean cyst nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Heterodera.
OX NCBI_TaxID=51029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Esophagus, and Gland;
RX PubMed=12906116; DOI=10.1094/mpmi.2003.16.8.720;
RA Gao B., Allen R., Maier T., Davis E.L., Baum T.J., Hussey R.S.;
RT "The parasitome of the phytonematode Heterodera glycines.";
RL Mol. Plant Microbe Interact. 16:720-726(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=20497349; DOI=10.1111/j.1469-8137.2010.03300.x;
RA Wang J., Lee C., Replogle A., Joshi S., Korkin D., Hussey R., Baum T.J.,
RA Davis E.L., Wang X., Mitchum M.G.;
RT "Dual roles for the variable domain in protein trafficking and host-
RT specific recognition of Heterodera glycines CLE effector proteins.";
RL New Phytol. 187:1003-1017(2010).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20565649; DOI=10.1111/j.1364-3703.2005.00270.x;
RA Wang X., Mitchum M.G., Gao B., Li C., Diab H., Baum T.J., Hussey R.S.,
RA Davis E.L.;
RT "A parasitism gene from a plant-parasitic nematode with function similar to
RT CLAVATA3/ESR (CLE) of Arabidopsis thaliana.";
RL Mol. Plant Pathol. 6:187-191(2005).
RN [4]
RP ERRATUM OF PUBMED:20565649.
RX DOI=10.1111/j.1364-3703.2008.00533.x;
RA Davis E.L.;
RL Mol. Plant Pathol. 10:151-151(2009).
RN [5]
RP REVIEW.
RX PubMed=18078779; DOI=10.1016/j.pbi.2007.10.010;
RA Mitchum M.G., Wang X., Davis E.L.;
RT "Diverse and conserved roles of CLE peptides.";
RL Curr. Opin. Plant Biol. 11:75-81(2008).
CC -!- FUNCTION: Mimics host plant CLE extracellular signal peptides that
CC regulate cell fate. May play a role in the differentiation or division
CC of feeding cells (syncytia) induced in plant roots during infection.
CC {ECO:0000269|PubMed:20497349, ECO:0000269|PubMed:20565649}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20497349}. Host
CC cytoplasm {ECO:0000269|PubMed:20497349}. Host extracellular space
CC {ECO:0000269|PubMed:20497349}. Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:20497349}. Note=Present in secretory granules
CC within the dorsal esophageal gland secretory cell and in the dorsal
CC gland ampulla (collecting reservoir) at the base of the nematode
CC stylet. Secreted into host root cells via the nematode stylet to
CC transform the recipient cells into enlarged multinucleate feeding cells
CC called giant-cells or syncytia. Secreted to the host apoplasm from its
CC cytoplasm via a plant secretory pathway. {ECO:0000269|PubMed:20497349}.
CC -!- TISSUE SPECIFICITY: Highly expressed exclusively within the dorsal
CC esophageal gland cell during syncytium formation in host plants (at
CC protein level). {ECO:0000269|PubMed:12906116,
CC ECO:0000269|PubMed:20497349, ECO:0000269|PubMed:20565649}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated during root colonization,
CC from the onset of syncytium formation by parasitic second-stage
CC juveniles (pJ2) through the J3?J4 molts of sedentary life stages that
CC become adult females. {ECO:0000269|PubMed:20497349}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=the root of the problem
CC - Issue 151 of July 2013;
CC URL="https://web.expasy.org/spotlight/back_issues/151/";
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DR EMBL; AF473827; AAO33474.1; -; mRNA.
DR EMBL; FJ503005; ACT32610.1; -; Genomic_DNA.
DR AlphaFoldDB; Q86RQ1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Apoplast; Differentiation; Glycoprotein; Host cytoplasm; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..138
FT /note="CLAVATA3/ESR (CLE)-related protein 2"
FT /id="PRO_0000401216"
FT REGION 23..90
FT /note="Required for secretion from the host cytoplasm to
FT the host apoplasm"
FT REGION 66..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 127..138
FT /note="CLE"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 138 AA; 14456 MW; 7AA362FC5D9C38C8 CRC64;
MPNIFKILLI VLLAVVSFRL SASTGDKKTA NDGSGNNSSA GIGTKIKRIV TAGLLFTSLA
TGGAEAIGRS NAQGGNAAGL VPSHVTNRSM APPPPPVQFE MGANRLEKMR AHLRELAEKM
PVNESKRLSP SGPDPHHH
