ENPL_LEIDO
ID ENPL_LEIDO Reviewed; 771 AA.
AC Q8T7E0;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Endoplasmin homolog {ECO:0000305};
DE AltName: Full=Glucose-regulated protein 94 {ECO:0000303|PubMed:12198148};
DE AltName: Full=Lipophosphoglycan biosynthetic protein 3 {ECO:0000303|PubMed:12198148};
DE Flags: Precursor;
GN Name=LPG3 {ECO:0000303|PubMed:12198148};
GN Synonyms=GRP94 {ECO:0000303|PubMed:12198148};
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661 {ECO:0000312|EMBL:AAM00390.1};
RN [1] {ECO:0000312|EMBL:AAM00390.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-159.
RC STRAIN=MHOM/SD/62/1S {ECO:0000303|PubMed:12198148};
RX PubMed=12198148; DOI=10.1093/emboj/cdf447;
RA Descoteaux A., Avila H.A., Zhang K., Turco S.J., Beverley S.M.;
RT "Leishmania LPG3 encodes a GRP94 homolog required for phosphoglycan
RT synthesis implicated in parasite virulence but not viability.";
RL EMBO J. 21:4458-4469(2002).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins (By similarity). Required for the
CC synthesis of lipophosphoglycan (LPG), a cell surface glycoconjugate
CC (PubMed:12198148). Necessary for the attachment of the galactosyl
CC residue to the mannose within the phosphoglycan repeats of the nascent
CC LPG chain (PubMed:12198148). Also required for addition of
CC phosphoglycan to acid phosphatase (PubMed:12198148). Not required for
CC normal growth (PubMed:12198148). Has ATPase activity (By similarity).
CC Binds heparin with micromolar affinity which may facilitate infection
CC of host cells (By similarity). {ECO:0000250|UniProtKB:P08113,
CC ECO:0000250|UniProtKB:Q9NGD0, ECO:0000269|PubMed:12198148}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9NGD0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12198148}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle with lower
CC expression in stationary phase promastigotes and higher levels in
CC amastigotes. {ECO:0000269|PubMed:12198148}.
CC -!- INDUCTION: Not induced by stress conditions such as heat, glucose
CC deprivation or treatment with the glycosylation inhibitor tunicamycin.
CC {ECO:0000269|PubMed:12198148}.
CC -!- DISRUPTION PHENOTYPE: Defective lipophosphoglycan synthesis and reduced
CC levels of the surface glycoproteins gp46 and gp63.
CC {ECO:0000269|PubMed:12198148}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AF369892; AAM00390.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8T7E0; -.
DR SMR; Q8T7E0; -.
DR VEuPathDB; TriTrypDB:LdBPK_290790.1; -.
DR VEuPathDB; TriTrypDB:LdCL_290012700; -.
DR VEuPathDB; TriTrypDB:LDHU3_29.1080; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Heparin-binding; Nucleotide-binding; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..771
FT /note="Endoplasmin homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_5004316334"
FT REGION 254..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 768..771
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000305|PubMed:12198148"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 405
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 159
FT /note="G->D: In OB1; defective lipophosphoglycan (LPG)
FT synthesis with production of a truncated LPG form lacking
FT phosphoglycan repeats; defective addition of phosphoglycan
FT to acid phosphatase."
FT /evidence="ECO:0000269|PubMed:12198148"
SQ SEQUENCE 771 AA; 86938 MW; 48985705202B4297 CRC64;
MANSSLLRVV LVALLLLGSV TVSAGDGRGT PIAFQAEVSK MLDILVNSLY TNRAVFLREL
ISNGSDALDK IRVLYLTSPK EPLTKDGEAP TMDLRISFDK EKSELILRDG GVGMTKEELA
KHLGSLGTSG TKHFLEKLQE GVGAVGGDQN NLIGQFGVGF YSVFLVGDRV RVASKSDDSD
EQYVWESKGD GQYFLYPDPR GNTLGRGTEI TIELKPDAEQ FLSAETIKKT IHQYSEFINF
PIYVQEEVEV ASTAATPESA AEERSLDEGA VEEDPDKEGD TQGVVKEKRW TLVNENRPIW
TRPIGNVTEE EYHKFYKAFS GDYRDPLYFN HFKVEGEVDF DSILFVPTTV DPASFSDDNA
VPNTNIKLYV RRVFITDEFR DLLPRYLNFV KGIVDSNDLP LNVSREVLQE SRILRVIKKK
LVRKTLSMFA DIAAQDEAIA NGKQVENPAP SGHTHLKKPA YTKFWELYGK HLRLGVMLDS
NNRNRLTKLF RYKSSRSESE YISLQTYVDR MKKGQKGIYY LSGDSVARIK KSPVLEDAVN
HDVEVIFMTD AIDEYVVSQL TDFAGKKLIN LAKEGVQFEE SDARQRVVDR KRKEKYDSFF
THLRALFGYS EVRKVILTKR MTNEAFIVSS SENQITARLA SIMRGQSMSL ANQQLTAERV
LEVNYRHPLV DEMFKRFTVD EDDEVATDIA WVLYDTANLQ AEFPVADVAA YSKRINRLLR
SSVDLSADDS LLPPDDAEYT VSDTETEEEE EQPKVDTNAH EEAETDGEGD L
