GUP1_CANTR
ID GUP1_CANTR Reviewed; 582 AA.
AC Q7Z877;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Membrane-bound O-acyltransferase GUP1;
DE AltName: Full=Glycerol uptake protein 1;
GN Name=GUP1;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IGC3097;
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; AY299512; AAQ16649.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7Z877; -.
DR SMR; Q7Z877; -.
DR VEuPathDB; FungiDB:CTMYA2_007890; -.
DR VEuPathDB; FungiDB:CTRG_03643; -.
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..582
FT /note="Membrane-bound O-acyltransferase GUP1"
FT /id="PRO_0000451586"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..158
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..373
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..548
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT ACT_SITE 469
FT /evidence="ECO:0000250|UniProtKB:P53154"
SQ SEQUENCE 582 AA; 68991 MW; 0B95BA3CA8FE3DAF CRC64;
MVIPRYHLIP TNCILSYHIK MSYLTDILKL FSLETLDTRL YPSSNTAKKQ SIIKQANPKS
RWSTIEFKFY YLVFLIIVPL MFKAGMESAN ENNPNYPKYE HLLSNGWIFG RKVDNSDQQY
RFFRNNFPLL CLLIIIHVGL RRVINRIIPL SSKRTYFDFI FGIIFLIGAH GVNVLKLSIH
LLINYLIGKY IKNYKLSLWI TWIYGISSLF FNEWYGNYTL GLSFLSTGYT GIIPRWDVFY
NFTLLRMISF NFDYLERQQK LNNMTLPKEE SNGSLLNLDD RERLTAPLPI EDYNIFNYIS
YLTYTPLFIA GPILTFNDYI YQSNYQQSSS TKDYHRIMMY LIRFIFCLLT LEFILHFMYV
VAASKTKSWE GNLPFQISML GMFNLNIIWL KLLIPWRLFR LWSLLDGIDP PENMIRCMDN
NFSALAFWRA WHRSYNRWII RYIYLPMGGG GKYRILNSLL VFSFVAIWHD IELKLLMWGW
LVVLFLIPEI SVTMIFKKYR NQWWYRHLCG VGAVINIWMM MIANLVGFCL GTDGMWKLLH
DLFKTFDGVR FLIISSGALF VGAQIMFEIR ESEMRKGINV RC
