NPC2_ASPOR
ID NPC2_ASPOR Reviewed; 175 AA.
AC O94183; Q2UER2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Phosphatidylglycerol/phosphatidylinositol transfer protein;
DE Short=PG/PI-TP;
DE Flags: Precursor;
GN Name=pltp; Synonyms=pg/pi-tp; ORFNames=AO090026000516;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=LMTC 2.14;
RX PubMed=10023082; DOI=10.1016/s0167-4781(98)00272-3;
RA Record E., Moukha S., Asther M.;
RT "Characterization and expression of the cDNA encoding a new kind of
RT phospholipid transfer protein, the
RT phosphatidylglycerol/phosphatidylinositol transfer protein from Aspergillus
RT oryzae: evidence of a putative membrane targeted phospholipid transfer
RT protein in fungi.";
RL Biochim. Biophys. Acta 1444:276-282(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LMTC 2.14;
RX PubMed=11179668; DOI=10.1016/s0378-1119(00)00514-x;
RA Record E., Moukha S., Asther M., Asther M.;
RT "Cloning and expression in phospholipid containing cultures of the gene
RT encoding the specific phosphatidylglycerol/phosphatidylinositol transfer
RT protein from Aspergillus oryzae: evidence that the pg/pi-tp is tandemly
RT arranged with the putative 3-ketoacyl-CoA thiolase gene.";
RL Gene 262:61-72(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [4]
RP PROTEIN SEQUENCE OF 38-65, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=7742351; DOI=10.1016/0005-2760(94)00252-t;
RA Record E., Asther M., Marion D., Asther M.;
RT "Purification and characterization of a novel specific
RT phosphatidylglycerol-phosphatidylinositol transfer protein with high
RT activity from Aspergillus oryzae.";
RL Biochim. Biophys. Acta 1256:18-24(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9933913; DOI=10.1139/w98-092;
RA Record E., Asther M., Moukha S., Marion D., Burlat V., Ruel K., Asther M.;
RT "Localization of a phosphatidylglycerol/phosphatidylinositol transfer
RT protein in Aspergillus oryzae.";
RL Can. J. Microbiol. 44:945-953(1998).
CC -!- FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol
CC and phosphatidylinositol. {ECO:0000269|PubMed:10023082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-7. {ECO:0000269|PubMed:7742351};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:7742351};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7742351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9933913}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:9933913}. Golgi apparatus
CC {ECO:0000269|PubMed:9933913}. Note=Also associated with Golgi-like
CC vesicles.
CC -!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000305}.
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DR EMBL; AF089838; AAD16095.1; -; mRNA.
DR EMBL; AF154412; AAG13652.1; -; Genomic_DNA.
DR EMBL; AP007159; BAE59953.1; -; Genomic_DNA.
DR RefSeq; XP_001821955.1; XM_001821903.2.
DR AlphaFoldDB; O94183; -.
DR SMR; O94183; -.
DR STRING; 510516.O94183; -.
DR EnsemblFungi; BAE59953; BAE59953; AO090026000516.
DR GeneID; 5993983; -.
DR KEGG; aor:AO090026000516; -.
DR VEuPathDB; FungiDB:AO090026000516; -.
DR HOGENOM; CLU_097982_0_0_1; -.
DR OMA; QTYDLCE; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0032934; F:sterol binding; IEA:EnsemblFungi.
DR GO; GO:0032366; P:intracellular sterol transport; IEA:EnsemblFungi.
DR CDD; cd00917; PG-PI_TP; 1.
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; PTHR11306; 1.
DR Pfam; PF02221; E1_DerP2_DerF2; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Golgi apparatus;
KW Lipid transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..37
FT /evidence="ECO:0000269|PubMed:7742351"
FT /id="PRO_0000019869"
FT CHAIN 38..175
FT /note="Phosphatidylglycerol/phosphatidylinositol transfer
FT protein"
FT /id="PRO_0000019870"
SQ SEQUENCE 175 AA; 18845 MW; A302CEDAF55D3274 CRC64;
MKFLSTAAAL LVCLAPVSTT ARSLDFFKSS QSPIQAQAKS VPGNNPLEYC NDPSGDILDI
KQVDLSPNPP LPGKTLAITA SGTLREKIED GAYVLLEVKY GLITLVRQTA DLCEQLVNVE
LKCPLGPGDM TLTKQVDLPK QIPPGKYTVQ ADVFNSDGEH ITCLKALNIE FKGPF
