ID A0A0F4YED0_TALEM Unreviewed; 482 AA.
AC A0A0F4YED0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5 {ECO:0000256|ARBA:ARBA00018320, ECO:0000256|RuleBase:RU367059};
DE Short=PITP SFH5 {ECO:0000256|RuleBase:RU367059};
GN ORFNames=T310_9811 {ECO:0000313|EMBL:KKA16544.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA16544.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA16544.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA16544.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA16544.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LASV01000752; KKA16544.1; -; Genomic_DNA.
DR RefSeq; XP_013323156.1; XM_013467702.1.
DR AlphaFoldDB; A0A0F4YED0; -.
DR STRING; 1408163.A0A0F4YED0; -.
DR GeneID; 25321733; -.
DR OrthoDB; 53323at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
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; IPR011074; CRAL/TRIO_N_dom.
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 Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 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 Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367059}.
FT DOMAIN 214..349
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 53463 MW; D8ABD089691CBCB6 CRC64;
MSAEPAAQET PQAVPEAQTA EKTVASVSEV KPEEKPEEKP EEKPEEKPAE TTQEQPAEAT
TTANGSETAP KDEPAPKKDE SAATAKPEFL TKNPALSQFF DRLPAILEKT GHTEMWGVPL
KDFNDPPTAN VLIKFLRANE GNVKQAEEQL TKALEWRKKL NPLDLVENAR FSAKKFGGLG
YITTYNDPKH GKVIINWNIY GAVKDINKTF GDFDSFLKWR VALMELAVKE LKLEEATSVI
DYNGEDPYQM IQVHDYQNLS FLRLNPTIRN ASKQTIDIFS TAYPELLREK FFVNVPAIMG
WMFAAMKVFL SKNTIRKFHP ITNGANLARE FSFGDELPKT YGGKAPELKE SGRTVPLEDD
TAEPAKEEEP AKESTKEEAK EETPKEETSK EEAPKEEAAK EEPAKAEPAK EEPAPATEAK
DGPAKEEPSK EEPVKEEPAK EEPAKEEPAK DEPAKDESAK EPAKEEPAQT ESAAAEAAPE
TK
//
