CLE4D_GLORO
ID CLE4D_GLORO Reviewed; 210 AA.
AC D1FNK5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 4D;
DE Flags: Precursor;
GN Name=CLE-4D;
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).
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:19656047}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}. Host extracellular space {ECO:0000250}. Secreted,
CC extracellular space, apoplast {ECO:0000250}. Note=Present in secretory
CC granules within the dorsal esophageal gland secretory cell and in the
CC dorsal 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 (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
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DR EMBL; EU386837; ACY70456.1; -; mRNA.
DR EMBL; EU386844; ACY70463.1; -; Genomic_DNA.
DR AlphaFoldDB; D1FNK5; -.
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:0033612; F:receptor serine/threonine kinase binding; IEA:InterPro.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IEA:InterPro.
DR InterPro; IPR044962; CLV3/ESR.
DR PANTHER; PTHR36349; PTHR36349; 2.
PE 2: Evidence at transcript level;
KW Apoplast; Differentiation; Glycoprotein; Host cytoplasm; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..210
FT /note="CLAVATA3/ESR (CLE)-related protein 4D"
FT /evidence="ECO:0000255"
FT /id="PRO_5000539265"
FT REPEAT 127..135
FT /note="A-1"
FT REPEAT 136..147
FT /note="CLE-1"
FT REPEAT 148..156
FT /note="A-2"
FT REPEAT 157..168
FT /note="CLE-2"
FT REPEAT 169..177
FT /note="A-3"
FT REPEAT 178..189
FT /note="CLE-3"
FT REPEAT 190..198
FT /note="A-4"
FT REPEAT 199..210
FT /note="CLE-4"
FT REGION 21..83
FT /note="Required for secretion from the host cytoplasm to
FT the host apoplasm"
FT /evidence="ECO:0000250"
FT REGION 115..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..198
FT /note="4 X approximate repeat A"
FT REGION 136..210
FT /note="4 X approximate repeat CLE"
FT COMPBIAS 115..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..210
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"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 210 AA; 22979 MW; D78B68963E22A836 CRC64;
MAKNAMLCLL ILSVVLALAF ATNKKDDEEP ENHSTGIFGK VGRVVTVALA MSSRLGGANA
TRGGGAVYGR NLKSNQLPNN NWMAPPPPMA MRSAKVYDSK HSPAEYLKKF AQDFRRKTGT
HSQRHHEETT LEQEKRGAPA GPDPIHHQDT TFEQEKRGAP AGPDPIHHQD TTLEQEKRVA
GAGPDPIHHQ DTKFEQEKRG APAGPDPIHH