ID   GUP1_MILFA              Reviewed;         505 AA.
AC   Q7Z888;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   10-FEB-2021, entry version 32.
DE   RecName: Full=Membrane-bound O-acyltransferase GUP1;
DE   AltName: Full=Glycerol uptake protein 1;
GN   Name=GUP1;
OS   Millerozyma farinosa (Yeast) (Pichia farinosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=4920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CBS 7064;
RX   PubMed=15381122; DOI=10.1016/j.femsyr.2004.06.012;
RA   Neves L., Oliveira R., Lucas C.;
RT   "Yeast orthologues associated with glycerol transport and metabolism.";
RL   FEMS Yeast Res. 5:51-62(2004).
CC   -!- FUNCTION: Membrane-bound O-acyltransferase involved in the remodeling
CC       of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-
CC       anchored proteins, but not on free GPI lipids. Also involved in lipid
CC       metabolism, having profound effects on sphingolipid-sterol-ordered
CC       domains integrity and assembly. Involved in cell integrity and
CC       apoptosis. {ECO:0000250|UniProtKB:P53154, ECO:0000305|PubMed:15381122}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P53154};
CC       Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:P53154}; Multi-pass membrane protein
CC       {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P53154};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY338363; AAQ01787.1; -; Genomic_DNA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Membrane-bound O-acyltransferase GUP1"
FT                   /id="PRO_0000451587"
FT   TOPO_DOM        1..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..464
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        486..505
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
SQ   SEQUENCE   505 AA;  59111 MW;  64A26FE11DB797D2 CRC64;
     MFKAAMDASN ETNPNYPKFA HLLSQGWMFG RKVDNSDQQY RFFRDNFPLL CGLVLLHTSL
     RRGVNLIAGN HKRTGFDFVF GXDIHLCSTR DEFLPYFDSL GYXIFPFLKY IKRNDVATXT
     YVDXTAILSL FLNDNYXSCT IWNRFYRSWI SEVSFQDGMC FSISHCXRML SYNLDYIEKR
     KSASEESNLE LKNSSSSLSE LDDRERLVAP IPLTDYNFVN YMAYITYAPL FIAGPIITFN
     DYIYQSDYKA MSSVKDYKRT FIYFLRFAFC ILVMEFLLHF MYVVAVSKTK AWEGDTPFQL
     SMLGLFNLNI IWLKLLIPWR LFRLWSLIDG IDPPENMIRC MDNNFSTLAF WRAWHRSYNR
     WIIRYIYIPL GGGGKYRILN SLCVFSFVAI WHDIELKLLM WGWLVVIFII PELAATAIFK
     NYQHEPWYRH VCALGAVINI WMMMLANLFG FCMGKDGTMS LIKTLFTTAV GLRFLFLSLG
     ALFVGSQVMF ELREAEKRRG VNVKC