GUP1_MILFA
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