ID J9VVG9_CRYNH Unreviewed; 297 AA.
AC J9VVG9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 42.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5 {ECO:0000256|RuleBase:RU367059};
DE Short=PITP SFH5 {ECO:0000256|RuleBase:RU367059};
GN ORFNames=CNAG_02104 {ECO:0000313|EMBL:AFR95715.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR95715.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR95715.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
CC -!- FUNCTION: Non-classical phosphatidylinositol (PtdIns) transfer protein
CC (PITP), which exhibits PtdIns-binding/transfer activity in the absence
CC of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2
CC homeostasis at the plasma membrane. Heme-binding protein that may play
CC a role in organic oxidant-induced stress responses.
CC {ECO:0000256|ARBA:ARBA00024180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000256|ARBA:ARBA00024146};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000256|ARBA:ARBA00024146};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367059}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406,
CC ECO:0000256|RuleBase:RU367059}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU367059}.
CC Microsome membrane {ECO:0000256|RuleBase:RU367059}; Peripheral membrane
CC protein {ECO:0000256|RuleBase:RU367059}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the SFH5 family. {ECO:0000256|ARBA:ARBA00006667,
CC ECO:0000256|RuleBase:RU367059}.
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DR EMBL; CP003825; AFR95715.1; -; Genomic_DNA.
DR RefSeq; XP_012049947.1; XM_012194557.1.
DR AlphaFoldDB; J9VVG9; -.
DR GeneID; 23885761; -.
DR KEGG; cng:CNAG_02104; -.
DR VEuPathDB; FungiDB:CNAG_02104; -.
DR HOGENOM; CLU_045138_0_1_1; -.
DR OrthoDB; 53323at2759; -.
DR Proteomes; UP000010091; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:UniProtKB-UniRule.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR042938; Sfh5.
DR PANTHER; PTHR47669; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR PANTHER; PTHR47669:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367059};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367059}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU367059};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367059};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU367059};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367059}.
FT DOMAIN 145..282
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
SQ SEQUENCE 297 AA; 33021 MW; F15ED27B70796C10 CRC64;
MSVVEASSAA QATWPELTED HPLSQLNSRL PKILSEAGHS QIWGVTLIYS TPPVFSTLII
LQKFLRSVDN SVDEAATALG KTLKWRKDWG LDAPADQKEK ENFGPDFEGL GYVTKIKKNN
GGDEIVTWNV YGAVKDLKST FGDLDRFLRW RVNLMEEAIA HLHLATTSTP IPDFNAGIDP
HRMAQVHLYE GVSFLRMDPH VKAASKATIE LMAANYPELL SRKFFVGVPL IMSWMFQAVR
MFVSAETAKK FVVISYKENL ANELGELEGV PKEYGGKGLS LGELQNQLRG KDPVTSL
//
