ENPL_LEIIN
ID ENPL_LEIIN Reviewed; 771 AA.
AC Q9NGD0;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Endoplasmin homolog {ECO:0000305};
DE AltName: Full=Glucose-regulated protein 94 {ECO:0000303|PubMed:11052869};
DE AltName: Full=Lipophosphoglycan biosynthetic protein 3 {ECO:0000303|PubMed:29568220};
DE Flags: Precursor;
GN Name=LPG3 {ECO:0000303|PubMed:29568220};
GN Synonyms=GRP94 {ECO:0000303|PubMed:11052869};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000312|EMBL:AAF67727.1};
RN [1] {ECO:0000312|EMBL:AAF67727.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION AS AN ANTIGEN.
RC STRAIN=MHOM/FR/78/LEM75 {ECO:0000312|EMBL:AAF67727.1};
RX PubMed=11052869; DOI=10.1006/expr.2000.4553;
RA Larreta R., Soto M., Alonso C., Requena J.M.;
RT "Leishmania infantum: gene cloning of the GRP94 homologue, its expression
RT as recombinant protein, and analysis of antigenicity.";
RL Exp. Parasitol. 96:108-115(2000).
RN [2] {ECO:0000312|EMBL:ADP89477.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MCAN/IR/96/LON-49 {ECO:0000312|EMBL:ADP89477.1};
RA Pirdel L., Zavaran Hosseini A., Kazemi B., Rasouli M.;
RT "Molecular cloning of the LPG3 gene from Leishmania infantum.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP IDENTIFICATION AS AN ANTIGEN.
RC STRAIN=MCAN/ES/96/BCN150 {ECO:0000303|PubMed:11803053};
RX PubMed=11803053; DOI=10.1016/s0165-2478(01)00331-5;
RA Larreta R., Guzman F., Patarroyo M.E., Alonso C., Requena J.M.;
RT "Antigenic properties of the Leishmania infantum GRP94 and mapping of
RT linear B-cell epitopes.";
RL Immunol. Lett. 80:199-205(2002).
RN [4] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND SUBUNIT.
RC STRAIN=MHOM/BR/75/M2682;
RX PubMed=29568220; DOI=10.1177/1177932218763363;
RA Martins T.V.F., Zeraik A.E., Alves N.O., de Oliveira L.L.,
RA de Oliveira Mendes T.A., DeMarco R., de Almeida Marques-da-Silva E.;
RT "Lipophosphoglycan 3 from Leishmania infantum chagasi binds heparin with
RT micromolar affinity.";
RL Bioinf. Biol. Insights 12:1177932218763363-1177932218763363(2018).
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 (By
CC similarity). Necessary for the attachment of the galactosyl residue to
CC the mannose within the phosphoglycan repeats of the nascent LPG chain
CC (By similarity). Also required for addition of phosphoglycan to acid
CC phosphatase (By similarity). Not required for normal growth (By
CC similarity). Has ATPase activity (PubMed:29568220). Binds heparin with
CC micromolar affinity which may facilitate infection of host cells
CC (PubMed:29568220). {ECO:0000250|UniProtKB:P08113,
CC ECO:0000250|UniProtKB:Q8T7E0, ECO:0000269|PubMed:29568220}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29568220}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8T7E0}.
CC -!- MISCELLANEOUS: Prominent antigen during human and canine visceral
CC leishmaniasis. {ECO:0000269|PubMed:11052869,
CC ECO:0000269|PubMed:11803053}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AF253053; AAF67727.1; -; Genomic_DNA.
DR EMBL; HQ400675; ADP89477.1; -; mRNA.
DR AlphaFoldDB; Q9NGD0; -.
DR SMR; Q9NGD0; -.
DR STRING; 5671.XP_001466598.1; -.
DR VEuPathDB; TriTrypDB:LINF_290012700; -.
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_5010148570"
FT REGION 253..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:0000250|UniProtKB:Q8T7E0"
FT COMPBIAS 740..771
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 771 AA; 86652 MW; FAA3B8A1F3C08026 CRC64;
MANSSLLRVV LVALLLLGSV TVSAGDGRGT PIAFQAEVSK MLDILVNSLY TNRAVFLREL
ISNGSDALDK IRVLYLTSPK EPLTKDGEAP TMDLRISFDK EKSELILRDG GVGMTKEELA
KHLGSLGTSG TKHFLEKLQE GVGAGGGDQN NLIGQFGVGF YSVFLVGDRV RVASKSDDSD
EQYVWESKGD GQYFLYPDPR GNTLGRGTEI TIELKPDAEQ FLSAETIKKT IHQYSEFINF
PIYVQEEVEV ASTAATPEPA AEEGSLDEGA VEEDPDKEGD TQGVVKERRW TLVNENRPIW
TRPIGNVTEE EYHTFYKAFS GDYRDPLYFN HFKVEGEVDF DSILFVPTTV DPASFSDDNS
VPNTNIKLYV RRVFITDEFR DLLPRYLNFV KGIVDSNDLP LNVSREVLQE SRILRVIKKK
LVRKTLSMFA DIAAQDEAIA NGKQVESPAP SGHTHLKKPA YTKFWELYGK HLRLGVMLDS
NNRNRLTKLF RYKSSRSESE YISLQTYVDR MKKGQKGIYY LSGDSVARIK KSPVLEDAVN
HDVEVIFMTD AIDEYVVSQL TDFAGKKLIN LAKEGVQLEE SDARQRVADR KRKEKYDSFF
THLRALFGYS EVRKVILTKR MTNEAFLVSS GENQITARLA SIMRGQSMSL ANQQMTAERV
LEVNYRHPLV DEMFKRFTVD EDDEVATDIA WVLYDTANLQ AEFPVADVAA YSKRINRLLR
SSVDLSADDS LLPPDDAEYT VSDTEAEEEE EQPKVDANAD EEAEAVGEDD L
