HTP3_SAPPC
ID HTP3_SAPPC Reviewed; 211 AA.
AC A0A067CMC7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Endonuclease Htp3 {ECO:0000303|PubMed:29904064};
DE EC=3.1.31.- {ECO:0000269|PubMed:29904064};
DE AltName: Full=Host targeting protein 3 {ECO:0000303|PubMed:29904064};
DE AltName: Full=RxLR effector protein Htp3 {ECO:0000303|PubMed:29904064};
DE Flags: Precursor;
GN Name=HTP3; ORFNames=SPRG_03573;
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65;
RX PubMed=23785293; DOI=10.1371/journal.pgen.1003272;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP INDUCTION, INTERACTION WITH HTP1 AND HOST GP96, DOMAIN, AND MUTAGENESIS OF
RP LYS-208 AND ARG-210.
RX PubMed=29904064; DOI=10.1038/s41467-018-04796-3;
RA Trusch F., Loebach L., Wawra S., Durward E., Wuensch A., Iberahim N.A.,
RA de Bruijn I., MacKenzie K., Willems A., Toloczko A., Dieguez-Uribeondo J.,
RA Rasmussen T., Schrader T., Bayer P., Secombes C.J., van West P.;
RT "Cell entry of a host-targeting protein of oomycetes requires gp96.";
RL Nat. Commun. 9:2347-2347(2018).
CC -!- FUNCTION: Effector involved in the disease saprolegniosis in salmonids
CC and other freshwater fish, resulting in considerable economic losses in
CC aquaculture (PubMed:29904064). Within the host fish cells, Htp3 is
CC released from vesicles into host cytosol where it degrades nucleic
CC acids (PubMed:29904064). {ECO:0000269|PubMed:29904064}.
CC -!- ACTIVITY REGULATION: The nuclease activity shows a general salt
CC dependency with a clear reduction by magnesium and sulfate ions.
CC {ECO:0000269|PubMed:29904064}.
CC -!- SUBUNIT: Interacts with the host cell surface endoplasmin gp96, in
CC order to get translocated into to host cell (PubMed:29904064).
CC Interacts with the effector Htp1, in order to get released from
CC vesicles into the host cytosol (PubMed:29904064).
CC {ECO:0000269|PubMed:29904064}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29904064}. Host
CC cytoplasm, host cytosol {ECO:0000269|PubMed:29904064}. Note=Uptake into
CC host cells is more efficient at a lower pH of 5.5. S.parasitica
CC acidifies the pH of its environment, which likely leads to the exposure
CC of a gp96 protein to the host cell surface. The gp96 protein is working
CC as a receptor and mediates the translocation of Htp3 via lipid rafts
CC into the cell. Finally, Htp3 is released from vesicles with the help of
CC other effector proteins, such as Htp1, into the cytosol where it is
CC functionally active as a nuclease. {ECO:0000269|PubMed:29904064}.
CC -!- DOMAIN: The conserved RxLR motif does not seem to be involved in self-
CC translocation into fish cells. {ECO:0000269|PubMed:29904064}.
CC -!- DOMAIN: The C-terminus (residues 200 to 211) is predicted to form a
CC short helix with charged amino acids and is required for the self-
CC translocation into fish cells. {ECO:0000269|PubMed:29904064}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the RxLR effector
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LCL3 family.
CC {ECO:0000305}.
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DR EMBL; KK583197; KDO31653.1; -; Genomic_DNA.
DR RefSeq; XP_012197543.1; XM_012342153.1.
DR AlphaFoldDB; A0A067CMC7; -.
DR SMR; A0A067CMC7; -.
DR STRING; 695850.A0A067CMC7; -.
DR EnsemblProtists; KDO31653; KDO31653; SPRG_03573.
DR GeneID; 24126067; -.
DR KEGG; spar:SPRG_03573; -.
DR VEuPathDB; FungiDB:SPRG_03573; -.
DR OMA; LLGWHWL; -.
DR OrthoDB; 1333771at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Endonuclease; Glycoprotein; Host cytoplasm; Hydrolase;
KW Metal-binding; Nuclease; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..211
FT /note="Endonuclease Htp3"
FT /id="PRO_0000446903"
FT DOMAIN 48..198
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 200..211
FT /note="Binding to the host cell surface"
FT /evidence="ECO:0000269|PubMed:29904064"
FT MOTIF 48..51
FT /note="RxLR"
FT /evidence="ECO:0000305|PubMed:29904064"
FT ACT_SITE 90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00644"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00644"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 208
FT /note="K->A: Impairs host cell surface association and
FT translocation into the host cell; when associated with A-
FT 210."
FT /evidence="ECO:0000269|PubMed:29904064"
FT MUTAGEN 210
FT /note="R->A: Impairs host cell surface association and
FT translocation into the host cell; when associated with A-
FT 208."
FT /evidence="ECO:0000269|PubMed:29904064"
SQ SEQUENCE 211 AA; 23841 MW; E3FE3F6F6836D526 CRC64;
MLEVPVWIPI LAFAVGLGLG LLIPHLQKPF QRFSTVNDIP KEFFEHERTL RGKVVSVTDG
DTIRVRHVPW LANGDGDFKG KLTETTLQLR VAGVDCPETA KFGRTGQPFG EEAKAWLKGE
LQDQVVSFKL LMKDQYSRAV CLVYYGSWAA PMNVSEELLR HGYANIYRQS GAVYGGLLET
FEALEAEARE KRVNIWSLDK RETPAQYKAR K
