ID   GUP1_CANAL              Reviewed;         584 AA.
AC   Q5AKZ2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Membrane-bound O-acyltransferase GUP1;
DE   AltName: Full=Glycerol uptake protein 1;
GN   Name=GUP1; OrderedLocusNames=CAALFM_C113540WA; ORFNames=orf19.4985;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION.
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).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20843317; DOI=10.1186/1471-2180-10-238;
RA   Ferreira C., Silva S., Faria-Oliveira F., Pinho E., Henriques M., Lucas C.;
RT   "Candida albicans virulence and drug-resistance requires the O-
RT   acyltransferase Gup1p.";
RL   BMC Microbiol. 10:238-238(2010).
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 (By similarity). Plays a role in virulence and antifungal
CC       resistance (PubMed:20843317). {ECO:0000250|UniProtKB:P53154,
CC       ECO:0000269|PubMed:20843317, 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   -!- DISRUPTION PHENOTYPE: Changes ergosterol plasma membrane constitution
CC       and distribution and presents an increased resistance to azoles.
CC       Impairs the development of hyphae, adhesion, to invasion, and formation
CC       of biofilms, all of which are significant virulence factors.
CC       {ECO:0000269|PubMed:20843317}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP017623; AOW26956.1; -; Genomic_DNA.
DR   RefSeq; XP_722191.1; XM_717098.2.
DR   AlphaFoldDB; Q5AKZ2; -.
DR   SMR; Q5AKZ2; -.
DR   STRING; 237561.Q5AKZ2; -.
DR   GeneID; 3636171; -.
DR   KEGG; cal:CAALFM_C113540WA; -.
DR   CGD; CAL0000180356; GUP1.
DR   VEuPathDB; FungiDB:C1_13540W_A; -.
DR   eggNOG; KOG3860; Eukaryota.
DR   HOGENOM; CLU_021430_1_1_1; -.
DR   InParanoid; Q5AKZ2; -.
DR   OrthoDB; 392243at2759; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Endoplasmic reticulum; Membrane;
KW   Mitochondrion; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..584
FT                   /note="Membrane-bound O-acyltransferase GUP1"
FT                   /id="PRO_0000451585"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..109
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..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..456
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        499..509
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        531..550
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        572..584
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
FT   ACT_SITE        471
FT                   /evidence="ECO:0000250|UniProtKB:P53154"
SQ   SEQUENCE   584 AA;  68733 MW;  D636040B1B4C245F CRC64;
     MNYLSQLGKL FSLETLDTRL NPTTNPIKRQ SIIKKANPTS RWSTLEFKIY LTILIIVVPL
     MIKAAMESSN ETNPNYPRFQ HLLSDGWILG RKVDNSDQQY RFFRNNFPLL CGLIFIHVTL
     RKLINTFIII PNGRYNNNFK RTYFDLIFGI IFLIGAHGIN VFKISFHLFI NYLIGKYIKN
     YKLAIWCTWI YGIFSLFFNE WFGDSSFGLS IFVNGSGYYT GIIPRWDVFY NFTLLRMLSF
     NLDYIERERK LGNNDGQLNL NKQENINGAD NPPTLLNLDD RQRLSAPLPL DDYNVSNYIA
     YISYTPLFIA GPIITFNDYV YQSNYQQSST TQNYQRIFMY AIRFLFCLLV MEFLLHFMYV
     VAVSKTKAWD GDTPFQISML GMFNLNLIWL KLLIPWRLFR LWALLDGIDP PENMIRCMDN
     NFSALAFWRA WHRSYNRWVI RYIYIPMGGS GTGKYRIINS LLVFSFVAIW HDIELKLLMW
     GWLVVIFLIP EISATLIFSK YNKNWWYRYL CGIGAVINIW MMMIANLVGF CLGTDGMWKL
     LHDLFQTFEG GRFFIISSIC LFVGAQIMFE LRESELRRAI DVRC