GUP1_SCHPO
ID GUP1_SCHPO Reviewed; 583 AA.
AC Q09758; Q9C0Z5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 4.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Membrane-bound O-acyltransferase gup1;
DE AltName: Full=Glycerol uptake protein 1;
GN Name=gup1; ORFNames=SPAC24H6.01c, SPAPB21F2.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
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; CU329670; CAA90845.4; -; Genomic_DNA.
DR PIR; S62402; S62402.
DR RefSeq; NP_592951.3; NM_001018352.3.
DR AlphaFoldDB; Q09758; -.
DR SMR; Q09758; -.
DR BioGRID; 278010; 2.
DR STRING; 4896.SPAC24H6.01c.1; -.
DR MaxQB; Q09758; -.
DR PaxDb; Q09758; -.
DR EnsemblFungi; SPAC24H6.01c.1; SPAC24H6.01c.1:pep; SPAC24H6.01c.
DR GeneID; 2541508; -.
DR KEGG; spo:SPAC24H6.01c; -.
DR PomBase; SPAC24H6.01c; gup1.
DR VEuPathDB; FungiDB:SPAC24H6.01c; -.
DR eggNOG; KOG3860; Eukaryota.
DR HOGENOM; CLU_021430_1_1_1; -.
DR InParanoid; Q09758; -.
DR OMA; ATWIFNI; -.
DR PhylomeDB; Q09758; -.
DR PRO; PR:Q09758; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; ISO:PomBase.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
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..583
FT /note="Membrane-bound O-acyltransferase gup1"
FT /id="PRO_0000213141"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..159
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..298
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..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..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..549
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P53154"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
FT /evidence="ECO:0000250|UniProtKB:P53154"
SQ SEQUENCE 583 AA; 68234 MW; 1D6BA8A07F17FBFB CRC64;
MLRLFRFDVL ETSTKDTERP NSKSSRLSST SGSSHPSSSS RLTVRSAVPE KSAFGSIEFI
FYFSVILSIL TIACFKIHYV SSPKHPNYKN IEKYLKPGWL FGQKVDSADF QYSAFRENMP
ILLLVIIVYN FLWRLVKLVF TKNTNDELAI KNNYRLCFSL LFALLVYGTG VIYVLTIALI
NYLISKSLKN SIFNPLLTWT LDISVVFFKE YFAYCKFSSL HPGLGFLDQY TGILERWYVL
FNITMLRLVS FNMDYYWSLK HNSEKLNTLI FDKDREPTTL TFRERVDYSC LDEDYNLKNF
LTYIFYAPLY LAGPIISFNN FMSQMKYPTV STLKYRNLLY AIRFLVCVLT MEFLLHYAYV
TAISKDGNWN QYSAVESAMI SFIVLFMTWL KLLIPWRLFR LWSLIDDIEP PENIVRCMCN
NYSAVGFWRA WHRSFNRWLI RYIYVPLGGS NHSILNLFII FTFVALWHDI SWELFAWGWL
IVLFILPERL CCFMSRRTGL TKHPYYRYIS GFGAALNIYF MIICNLIGFA VGIDGIKNVL
VSFFLTLKGA MSAIAAFIMF FSAVQIMFQI RVNEEEEGIN LRC
