GUP2_YEAST
ID GUP2_YEAST Reviewed; 609 AA.
AC Q08929; D6W3I0;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Membrane-bound O-acyltransferase GUP2 {ECO:0000305};
DE AltName: Full=Glycerol uptake protein 2;
DE Flags: Precursor;
GN Name=GUP2; OrderedLocusNames=YPL189W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=10931309; DOI=10.1046/j.1365-2958.2000.01968.x;
RA Holst B., Lunde C., Lages F., Oliveira R., Lucas C., Kielland-Brandt M.C.;
RT "GUP1 and its close homologue GUP2, encoding multimembrane-spanning
RT proteins involved in active glycerol uptake in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 37:108-124(2000).
RN [4]
RP INDUCTION.
RX PubMed=15278288; DOI=10.1007/s00294-004-0519-3;
RA Oliveira R., Lucas C.;
RT "Expression studies of GUP1 and GUP2, genes involved in glycerol active
RT transport in Saccharomyces cerevisiae, using semi-quantitative RT-PCR.";
RL Curr. Genet. 46:140-146(2004).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=25589358; DOI=10.1002/jobm.201400781;
RA Faria-Oliveira F., Carvalho J., Belmiro C.L., Ramalho G., Pavao M.,
RA Lucas C., Ferreira C.;
RT "Elemental biochemical analysis of the polysaccharides in the extracellular
RT matrix of the yeast Saccharomyces cerevisiae.";
RL J. Basic Microbiol. 55:685-694(2015).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
CC -!- FUNCTION: Probable membrane-bound O-acyltransferase (By similarity).
CC Together with GUP1, has an influence on the chemical composition of the
CC yeast extracellular matrix (yECM) in yeast multicellular aggregates,
CC such as biofilms and colonies (PubMed:25589358).
CC {ECO:0000250|UniProtKB:P53154, ECO:0000269|PubMed:25589358}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26928762}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:15278288}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originaly thought to be involved in active uptake of
CC glycerol driven by electrogenic proton symport (PubMed:10931309), but
CC has later been shown to be an acyltransferase and that effects on
CC glycerol transport may be indirect (PubMed:15381122).
CC {ECO:0000305|PubMed:10931309, ECO:0000305|PubMed:15381122}.
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DR EMBL; Z73545; CAA97902.1; -; Genomic_DNA.
DR EMBL; Z73544; CAA97901.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11246.1; -; Genomic_DNA.
DR PIR; S65208; S65208.
DR RefSeq; NP_015135.1; NM_001184003.1.
DR AlphaFoldDB; Q08929; -.
DR SMR; Q08929; -.
DR BioGRID; 35994; 72.
DR DIP; DIP-8868N; -.
DR IntAct; Q08929; 4.
DR MINT; Q08929; -.
DR STRING; 4932.YPL189W; -.
DR PaxDb; Q08929; -.
DR PRIDE; Q08929; -.
DR EnsemblFungi; YPL189W_mRNA; YPL189W; YPL189W.
DR GeneID; 855912; -.
DR KEGG; sce:YPL189W; -.
DR SGD; S000006110; GUP2.
DR VEuPathDB; FungiDB:YPL189W; -.
DR eggNOG; KOG3860; Eukaryota.
DR GeneTree; ENSGT00530000063629; -.
DR HOGENOM; CLU_021430_1_1_1; -.
DR InParanoid; Q08929; -.
DR OMA; GWHASYN; -.
DR BioCyc; YEAST:G3O-34082-MON; -.
DR PRO; PR:Q08929; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08929; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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:0016020; C:membrane; ISM:SGD.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; ISA:SGD.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015793; P:glycerol transmembrane transport; IGI:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..609
FT /note="Membrane-bound O-acyltransferase GUP2"
FT /id="PRO_0000213133"
FT TOPO_DOM 19..75
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..169
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..324
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..406
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..502
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..575
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT ACT_SITE 496
FT /evidence="ECO:0000250|UniProtKB:P53154"
SQ SEQUENCE 609 AA; 71289 MW; 346B7B9D7E3E5830 CRC64;
MSMLRIWSCI VHFFSVQALD SRIKPDIEFK RRQRIFINSS KEENGSSSSA VTVTRNPVLS
SNSPSPPLWN TWEFRLYYLA FTVVVPFMIK AALATSSESN PNYYKFSGLL AHGWILGRKV
DNSDPQYRFF RSNFFLLAIL ILLQIILKKV FVKFSKIPKT KFDFACGLVF VCFMYGINSV
KLFTHAFIFF TLAHSLKRKR LIAAFAIWSY GIFTLFINQK MKNLPFNNIA IILSPMDQWY
KGIVPRWDFF FNFTLLRLLS YSMDFLERWH EQLSRQPSID YDDRRPEFRK SLSGSTLQTI
YESGKNVLEE KERLVAEHHI QDYNFINFIA YITYAPLFLV GPIITFNDYL YQSENKLPSL
TKKNIGFYAL KVFSSLLLME IILHYIYVGA IARTKAWNND TPLQQAMIAL FNLNIMYLKL
LIPWRLFRLW AMVDGIDAPE NMLRCVDNNY STVGFWRAWH TSFNKWVIRY IYVPFGGSNN
KILTSFAVFS FVAIWHDIQL RVLFWGWLTV LLLLGETYIT NCFSRYRFRS WYRFVCGIGA
AINICMMMII NVYGFCLGAE GTKLLLKGIF NNSHSPEFLT AVMVSLFIAV QVMFEIREEE
KRHGINLKC
