HTP1_SAPPC
ID HTP1_SAPPC Reviewed; 198 AA.
AC D3JZP7; A0A067CTQ5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=RxLR effector protein Htp1 {ECO:0000303|PubMed:20659163};
DE AltName: Full=Host targeting protein 1 {ECO:0000303|PubMed:20659163};
DE Flags: Precursor;
GN Name=Htp1 {ECO:0000303|PubMed:20659163}; ORFNames=SPRG_19749;
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 [MRNA], INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=CBS 223.65;
RX PubMed=20659163; DOI=10.1111/j.1574-6968.2010.02055.x;
RA van West P., de Bruijn I., Minor K.L., Phillips A.J., Robertson E.J.,
RA Wawra S., Bain J., Anderson V.L., Secombes C.J.;
RT "The putative RxLR effector protein SpHtp1 from the fish pathogenic
RT oomycete Saprolegnia parasitica is translocated into fish cells.";
RL FEMS Microbiol. Lett. 310:127-137(2010).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22308362; DOI=10.1073/pnas.1113775109;
RA Wawra S., Bain J., Durward E., de Bruijn I., Minor K.L., Matena A.,
RA Loebach L., Whisson S.C., Bayer P., Porter A.J., Birch P.R., Secombes C.J.,
RA van West P.;
RT "Host-targeting protein 1 (SpHtp1) from the oomycete Saprolegnia parasitica
RT translocates specifically into fish cells in a tyrosine-O-sulphate-
RT dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:2096-2101(2012).
RN [4]
RP FUNCTION, AND INTERACTION WITH HTP3.
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 (Probable). Within the host fish cells, Htp1 is involved in
CC the uptake of the S.parasitica effector Htp3 at a neutral pH (pH 7.5)
CC and its release from vesicles into host cytosol where it degrades
CC nucleic acids (PubMed:29904064). {ECO:0000269|PubMed:29904064,
CC ECO:0000305|PubMed:20659163}.
CC -!- SUBUNIT: Interacts with the effector Htp3 within the host cells.
CC {ECO:0000269|PubMed:29904064}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20659163}. Host cell
CC {ECO:0000269|PubMed:20659163}. Note=Host cell surface binding and
CC uptake is mediated by an interaction with tyrosine-O-sulfate-modified
CC cell surface molecules and not via phospholipids, as has been reported
CC for RxLR-effectors from plant pathogenic oomycetes.
CC {ECO:0000269|PubMed:22308362}.
CC -!- INDUCTION: Highly expressed in zoospores/cysts from S.parasitica and in
CC the very early stages of infection on Oncorhynchus mykiss (rainbow
CC trout) cells. {ECO:0000269|PubMed:20659163}.
CC -!- DOMAIN: Has a conserved RxLR motif that acts to carry the protein into
CC the host cell cytoplasm. Lacks the 'so-called' EER motif, which is
CC found closely behind the RxLR motif in most of RxLR effector family
CC members, but the presence of an EER motif is not always essential for
CC the translocation of every RxLR effector into host cells, or for
CC inducing a hypersensitive response. {ECO:0000269|PubMed:22308362}.
CC -!- SIMILARITY: Belongs to the RxLR effector family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KDO29921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GU345745; ADB84848.1; -; mRNA.
DR EMBL; KK583204; KDO29921.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_012199566.1; XM_012344176.1.
DR AlphaFoldDB; D3JZP7; -.
DR EnsemblProtists; KDO29921; KDO29921; SPRG_19749.
DR GeneID; 24141037; -.
DR KEGG; spar:SPRG_19749; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..198
FT /note="RxLR effector protein Htp1"
FT /id="PRO_5003046573"
FT REGION 48..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..49
FT /note="RxLR"
FT /evidence="ECO:0000305|PubMed:20659163"
FT COMPBIAS 68..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 198 AA; 21444 MW; 79505A73C5585C0F CRC64;
MRIHHPLTLA ALCVVLHESL GAAQHSNNVA RLEHYRIAEI EHWEKRHLRS DSRGHRHHAH
HGQVIDKENN NSQEQATTGN SVETNQVPST EPTKDKTTPM KNALFKLFRE KKLKTKNAGN
GHAHDDDDDS DFSDDDVPTN APTDAPTGAP TDAPTDAPTV APTDAPTDAP TEAPTNAPTG
TDAPTDAPTD AQVVPTFD
