ID K0KFS5_WICCF Unreviewed; 444 AA.
AC K0KFS5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE SubName: Full=Phosphatidylinositol:ceramide phosphoinositol transferase (IPC synthase) {ECO:0000313|EMBL:CCH44010.1};
DE EC=2.-.-.- {ECO:0000313|EMBL:CCH44010.1};
GN Name=AUR1 {ECO:0000313|EMBL:CCH44010.1};
GN ORFNames=BN7_3567 {ECO:0000313|EMBL:CCH44010.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH44010.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH44010.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:CCH44010.1}.
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DR EMBL; CAIF01000101; CCH44010.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KFS5; -.
DR STRING; 1206466.K0KFS5; -.
DR eggNOG; ENOG502QPQM; Eukaryota.
DR HOGENOM; CLU_030747_2_0_1; -.
DR InParanoid; K0KFS5; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProt.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF11; INOSITOL PHOSPHORYLCERAMIDE SYNTHASE CATALYTIC SUBUNIT AUR1; 1.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW Transferase {ECO:0000313|EMBL:CCH44010.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..318
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 406..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 50099 MW; B8DB383C1E25000B CRC64;
MSFLIKLFQS YFLDERPNGA VIADIDLNLN PKITVERLKN HKFTKYEVLN YSTLAFFFTI
SFFLNQLNIF IKLGIVSLYI TSLLIPFTSQ FFIYGSPVLA WVAFLFNSKN LDAAFRPPIS
VKVLPAIETI LYGDNLSQLL ATSTAPILDI LAWLPYGLIH FSFPFVTAAL IFLWGPPTAL
RSFGFAFGYM NLIGVVTQVL FPAAAPWYKI LHGLDPANYS MLGSPGGLAR IDEILGFDMY
TTAFSKTSPV VFGAFPSLHS GSASMDALFL FWLFPKASPI ILLYVIWLWW STMYLTHHYF
FDLIAGSFLS FVVFQFTKYN YLPVINYNYK NRWSYGSIIK PNIWNSDPLS LSPEIDVENQ
VFSSQRAINN VELNVIQRQS RSNIFDDSEI TSPALSVFEN DSEVPRSFSR ASNNSQTSIE
SQFDMSIPVS ASSNLQPGGK SRLD
//
