XLP1_PHYPN
ID XLP1_PHYPN Reviewed; 238 AA.
AC W2PDG1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Inactive glycoside hydrolase XLP1;
DE AltName: Full=Glycoside hydrolase family 12 protein XLP1 {ECO:0000303|Ref.2};
DE Short=GH12 protein XLP1 {ECO:0000303|Ref.2};
DE AltName: Full=XEG1-like protein 1 {ECO:0000303|Ref.2};
DE Flags: Precursor;
GN Name=XLP1 {ECO:0000303|PubMed:28082413}; ORFNames=PPTG_19378;
OS Phytophthora parasitica (strain INRA-310).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=761204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310;
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INRA-310;
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH HOST GIP1, DOMAIN, AND MUTAGENESIS OF TRP-25;
RP ASN-38; TRP-40; ASN-41; GLN-42; ASN-43; THR-75 AND GLN-76.
RX PubMed=28082413; DOI=10.1126/science.aai7919;
RA Ma Z., Zhu L., Song T., Wang Y., Zhang Q., Xia Y., Qiu M., Lin Y., Li H.,
RA Kong L., Fang Y., Ye W., Wang Y., Dong S., Zheng X., Tyler B.M., Wang Y.;
RT "A paralogous decoy protects Phytophthora sojae apoplastic effector PsXEG1
RT from a host inhibitor.";
RL Science 355:710-714(2017).
CC -!- FUNCTION: Non-functional secreted XEG1-like protein that binds to host
CC Nicotiana benthamiana apoplastic glucanase inhibitor protein GIP2 more
CC tightly than does XEG1, thus it outcompetes XEG1 for GIP2 binding and
CC frees functional XEG1 to support P.parasitica infection
CC (PubMed:28082413). With XEG1, is required to elevate apoplastic sugar
CC during P.parasitica infection (PubMed:28082413).
CC {ECO:0000269|PubMed:28082413}.
CC -!- SUBUNIT: Interacts with host apoplastic glucanase inhibitor GIP2.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G4ZHR3}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to its ortholog from P.sojae, still has the
CC conserved Glu residue in position 222 essential activity, but, as for
CC P.sojae XLP1, does not show xyloglucanase activity.
CC {ECO:0000269|PubMed:28082413}.
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DR EMBL; KI669674; ETM98685.1; -; Genomic_DNA.
DR RefSeq; XP_008916025.1; XM_008917777.1.
DR AlphaFoldDB; W2PDG1; -.
DR SMR; W2PDG1; -.
DR EnsemblProtists; ETM98685; ETM98685; PPTG_19378.
DR GeneID; 20188153; -.
DR VEuPathDB; FungiDB:PPTG_19378; -.
DR OMA; WAGGNIH; -.
DR Proteomes; UP000018817; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..238
FT /note="Inactive glycoside hydrolase XLP1"
FT /id="PRO_5004821942"
FT ACT_SITE 133
FT /evidence="ECO:0000250|UniProtKB:G4ZHR2"
FT ACT_SITE 219
FT /evidence="ECO:0000250|UniProtKB:G4ZHR2"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 25
FT /note="W->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-39, A-41, A-42, A-43, A-44, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 38
FT /note="N->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-41, A-42, A-43, A-44, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 40
FT /note="W->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A42, A-43, A-44, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 41
FT /note="N->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A-41, A-43, A-44, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 42
FT /note="Q->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A-41, A-42, A-44, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 43
FT /note="N->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A-41, A-42, A-43, A-77 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 75
FT /note="T->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A-41, A-42, A-43, A-44 and A-
FT 78."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 76
FT /note="Q->A: Affects the binding to host GIP2 and relieves
FT GIP2 inhibition of XEG1-induced sugar elevation; when
FT associated with A-26, A-39, A-41, A-42, A-43, A-44 and A-
FT 77."
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 238 AA; 25545 MW; 65F8BA5CC9C5A2D8 CRC64;
MKSFLIAIVI AVLLPVSAAD FCAQWRLSKA GKYIIYNNLW NQNTATSGSQ CTGVDKVSGS
TVAWHTSYSW AGAPTQVKSY SNAALVFTKK QIKNIKTIPT TMKYSYSYSG TLIADVAYDL
FTSSTASGSN EYEIMIWLAA YGGAGPISST GKAIATVTIN SNSFKLYKGP NGSTTVYSFV
ATKTITNFSA DLLDFFTYLV KTQAFPSSQY LTTLEAGTEP FTGSNAKMTV SSYSAAVN
