CLE1_HETGL
ID CLE1_HETGL Reviewed; 139 AA.
AC Q9BN21;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 1;
DE Short=CLE-like peptide 1;
DE Short=Hg-SYV46;
DE AltName: Full=Esophageal gland cell secretory protein 1;
DE Flags: Precursor;
GN Name=CLE1; Synonyms=2B10, HSP1, SYV46;
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=11310741; DOI=10.1094/mpmi.2001.14.4.536;
RA Wang X., Allen R., Ding X., Goellner M., Maier T., de Boer J.M., Baum T.J.,
RA Hussey R.S., Davis E.L.;
RT "Signal peptide-selection of cDNA cloned directly from the esophageal gland
RT cells of the soybean cyst nematode Heterodera glycines.";
RL Mol. Plant Microbe Interact. 14:536-544(2001).
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 TISSUE SPECIFICITY.
RC TISSUE=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 [4]
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 [5]
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 [6]
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:20497349,
CC 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 from the host cytoplasm to the
CC host apoplasm via a plant secretory pathway.
CC {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:11310741,
CC ECO:0000269|PubMed:12906116, ECO:0000269|PubMed:20497349,
CC 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 -!- MISCELLANEOUS: Failed to trigger CLE-like cell fate regulation in
CC Arabidopsis thaliana, a non-host plant.
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; AF273728; AAG21331.2; -; mRNA.
DR EMBL; FJ503004; ACT32609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BN21; -.
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; Coiled coil; Differentiation; Glycoprotein; Host cytoplasm;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..139
FT /note="CLAVATA3/ESR (CLE)-related protein 1"
FT /id="PRO_0000401215"
FT REGION 23..90
FT /note="Required for secretion from the host cytoplasm to
FT the host apoplasm"
FT REGION 66..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..125
FT /evidence="ECO:0000255"
FT MOTIF 128..139
FT /note="CLE"
FT COMPBIAS 104..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 139 AA; 14504 MW; B29F9676CA3A73BC CRC64;
MPNIFKILLI VLLAVVSFRL SASTGDKKTA NDGSGNNSSA GIGTKIKRIV TAGLLFTSLA
TGGAEAIGRS NAQGGNAAGL VPSHLTNRSM APPPPPAQFE KGAATRVEKM RAQLRELAEK
MTDKDPKRLS PSGPDPHHH
