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 22-FEB-2023, entry version 39. 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/"; 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; AF473827; AAO33474.1; -; mRNA. DR EMBL; FJ503005; ACT32610.1; -; Genomic_DNA. DR AlphaFoldDB; Q86RQ1; -. DR GlyCosmos; Q86RQ1; 3 sites, No reported glycans. 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 //