ID A0A2N1JH95_9BASI Unreviewed; 172 AA.
AC A0A2N1JH95;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Phosphatidylglycerol/phosphatidylinositol transfer protein {ECO:0000256|ARBA:ARBA00016056};
GN Name=NPC2 {ECO:0000313|EMBL:PKI85905.1};
GN ORFNames=MVES_000506 {ECO:0000313|EMBL:PKI85905.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI85905.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI85905.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI85905.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol
CC and phosphatidylinositol. {ECO:0000256|ARBA:ARBA00002053}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the NPC2 family.
CC {ECO:0000256|ARBA:ARBA00006370}.
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DR EMBL; KZ454987; PKI85905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1JH95; -.
DR OrthoDB; 5472305at2759; -.
DR Proteomes; UP000232875; Unassembled WGS sequence.
DR GO; GO:0032934; F:sterol binding; IEA:InterPro.
DR GO; GO:0032366; P:intracellular sterol transport; IEA:InterPro.
DR CDD; cd00917; PG-PI_TP; 1.
DR Gene3D; 2.70.220.10; Ganglioside GM2 activator; 1.
DR InterPro; IPR036846; GM2-AP_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR003172; ML_dom.
DR InterPro; IPR033917; ML_PG-PI_TP.
DR InterPro; IPR039670; NPC2-like.
DR PANTHER; PTHR11306; NIEMANN PICK TYPE C2 PROTEIN NPC2-RELATED; 1.
DR PANTHER; PTHR11306:SF0; PHOSPHATIDYLGLYCEROL_PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; 1.
DR Pfam; PF02221; E1_DerP2_DerF2; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..172
FT /note="Phosphatidylglycerol/phosphatidylinositol transfer
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014793767"
FT DOMAIN 73..172
FT /note="MD-2-related lipid-recognition"
FT /evidence="ECO:0000259|SMART:SM00737"
SQ SEQUENCE 172 AA; 19113 MW; 6AD972BBA557DB21 CRC64;
MSPRLLLFWL ALLACVIALA PQRQAAFQAQ EHVALPDIVD IMEKEAHAQH IALDSMLRPV
ASRVKPKSER WWWNTCGDDG VVVHAREIEL NPDPPVKGQN LTVHAVGTVD SAVEQGSYID
INVHVGFVRV LSRRFDLCDA LVDNNVEVQC PIKPGKYNFS HTVALPREIP PG
//
