CLE1_GLORO
ID CLE1_GLORO Reviewed; 204 AA.
AC D1FNJ7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 1 {ECO:0000303|PubMed:19656047};
DE Contains:
DE RecName: Full=CLE1-1 {ECO:0000303|PubMed:19656047};
DE Flags: Precursor;
GN Name=CLE-1 {ECO:0000303|PubMed:19656047};
OS Globodera rostochiensis (Golden nematode worm) (Heterodera rostochiensis).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=31243;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=19656047; DOI=10.1094/mpmi-22-9-1128;
RA Lu S.-W., Chen S., Wang J., Yu H., Chronis D., Mitchum M.G., Wang X.;
RT "Structural and functional diversity of CLAVATA3/ESR (CLE)-like genes from
RT the potato cyst nematode Globodera rostochiensis.";
RL Mol. Plant Microbe Interact. 22:1128-1142(2009).
RN [2]
RP FUNCTION, PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21750229; DOI=10.1104/pp.111.180554;
RA Guo Y., Ni J., Denver R., Wang X., Clark S.E.;
RT "Mechanisms of molecular mimicry of plant CLE peptide ligands by the
RT parasitic nematode Globodera rostochiensis.";
RL Plant Physiol. 157:476-484(2011).
CC -!- FUNCTION: [CLE1-1]: Mimics host plant CLE extracellular signal peptides
CC that regulate cell fate. May play a role in the differentiation or
CC division of feeding cells (syncytia) induced in plant roots during
CC infection. {ECO:0000269|PubMed:19656047, ECO:0000269|PubMed:21750229}.
CC -!- SUBCELLULAR LOCATION: [CLE1-1]: Secreted
CC {ECO:0000250|UniProtKB:Q9BN21}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q9BN21}. Host extracellular space
CC {ECO:0000250|UniProtKB:Q9BN21}. Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q9BN21}. 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:0000250|UniProtKB:Q9BN21}.
CC -!- TISSUE SPECIFICITY: Highly expressed exclusively within the dorsal
CC esophageal gland cell during syncytium formation in host plants.
CC {ECO:0000269|PubMed:19656047}.
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:19656047}.
CC -!- PTM: Preprocessing of the precursor by host proteases leads first to
CC the production of 21-mer CLE-containing peptides (Arg-130 to Lys-150,
CC Arg-151 to Lys-171 and Arg-172 to LYS-192) followed by an ultimate C-
CC term trimming to give the mature 12-mer CLE1-1 peptide.
CC {ECO:0000269|PubMed:21750229}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
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DR EMBL; EU386829; ACY70448.1; -; mRNA.
DR EMBL; EU386830; ACY70449.1; -; Genomic_DNA.
DR AlphaFoldDB; D1FNJ7; -.
DR SMR; D1FNJ7; -.
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.
DR InterPro; IPR039616; CLE1/3/4.
DR PANTHER; PTHR33869; PTHR33869; 1.
PE 1: Evidence at protein level;
KW Apoplast; Differentiation; Glycoprotein; Host cytoplasm; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..204
FT /note="CLAVATA3/ESR (CLE)-related protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5000539258"
FT PEPTIDE 130..141
FT /note="CLE1-1"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443331"
FT PROPEP 142..150
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443332"
FT PEPTIDE 151..162
FT /note="CLE1-1"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443333"
FT PROPEP 163..171
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443334"
FT PEPTIDE 172..183
FT /note="CLE1-1"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443335"
FT PROPEP 184..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:21750229"
FT /id="PRO_0000443336"
FT REGION 21..83
FT /note="Required for secretion from the host cytoplasm to
FT the host apoplasm"
FT /evidence="ECO:0000250"
FT REGION 116..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 204 AA; 22428 MW; 5882116C46A39EB9 CRC64;
MAKNAMLCLL ILSVVLALAF ATNEKDDKEA GNLSTGIFGK AGRFVTVALA MSSRLGGAGA
SQGGGAVHGE SLKSNQLQNA YRMALPPPMQ IKSAEIDGWK PSPDEYLKKF AQEFRRNTGM
KPQSYNEEKR VTPGGPDPLH NREKILEEQK RVTPGGPDPL HNREKTLEEQ KRVTPGGPDP
LHNREKTLEE QKRVTPGVPD RQHR
