GIT1_YEAST
ID GIT1_YEAST Reviewed; 518 AA.
AC P25346; D6VR99;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glycerophosphoinositol transporter 1 {ECO:0000303|PubMed:9691030};
GN Name=GIT1 {ECO:0000303|PubMed:9691030}; OrderedLocusNames=YCR098C;
GN ORFNames=YCR137, YCR98C;
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 [GENOMIC DNA].
RX PubMed=1574927; DOI=10.1002/yea.320080307;
RA Sor F., Cheret G., Fabre F., Faye G., Fukuhara H.;
RT "Sequence of the HMR region on chromosome III of Saccharomyces
RT cerevisiae.";
RL Yeast 8:215-222(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9691030; DOI=10.1093/genetics/149.4.1707;
RA Patton-Vogt J.L., Henry S.A.;
RT "GIT1, a gene encoding a novel transporter for glycerophosphoinositol in
RT Saccharomyces cerevisiae.";
RL Genetics 149:1707-1715(1998).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=12912892; DOI=10.1128/ec.2.4.729-736.2003;
RA Almaguer C., Mantella D., Perez E., Patton-Vogt J.;
RT "Inositol and phosphate regulate GIT1 transcription and
RT glycerophosphoinositol incorporation in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:729-736(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16141200; DOI=10.1074/jbc.m507051200;
RA Fisher E., Almaguer C., Holic R., Griac P., Patton-Vogt J.;
RT "Glycerophosphocholine-dependent growth requires Gde1p (YPL110c) and Git1p
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:36110-36117(2005).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Glycerophosphodiester transporter that mediates uptake of
CC both glycerophosphoinositol (GroPIns) and glycerophosphocholine
CC (GroPCho) as sources of the nutrients inositol and phosphate
CC (PubMed:9691030, PubMed:12912892, PubMed:16141200).
CC {ECO:0000269|PubMed:12912892, ECO:0000269|PubMed:16141200,
CC ECO:0000269|PubMed:9691030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sn-glycerol 3-phosphocholine(out) = sn-glycerol 3-
CC phosphocholine(in); Xref=Rhea:RHEA:32911, ChEBI:CHEBI:16870;
CC Evidence={ECO:0000269|PubMed:16141200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32912;
CC Evidence={ECO:0000269|PubMed:16141200};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sn-glycero-3-phospho-1D-myo-inositol(out) = sn-glycero-3-
CC phospho-1D-myo-inositol(in); Xref=Rhea:RHEA:32915, ChEBI:CHEBI:58444;
CC Evidence={ECO:0000269|PubMed:16141200};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32916;
CC Evidence={ECO:0000269|PubMed:16141200};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12912892,
CC ECO:0000305|PubMed:16141200, ECO:0000305|PubMed:9691030}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Both inositol and phosphate regulate GIT1 transcription and
CC expression is positively regulated by the transcription factor PHO4
CC (PubMed:12912892). {ECO:0000269|PubMed:12912892}.
CC -!- DISRUPTION PHENOTYPE: Impairs the uptake of glycerophosphoinositol
CC (GroPIns) (PubMed:9691030). Impairs also the uptake of
CC glycerophosphocholine (GroPCho) (PubMed:9691030).
CC {ECO:0000269|PubMed:16141200, ECO:0000269|PubMed:9691030}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X59720; CAA42240.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07568.1; -; Genomic_DNA.
DR PIR; S19514; S19514.
DR RefSeq; NP_010022.1; NM_001178805.1.
DR AlphaFoldDB; P25346; -.
DR SMR; P25346; -.
DR BioGRID; 31071; 28.
DR DIP; DIP-4626N; -.
DR IntAct; P25346; 3.
DR MINT; P25346; -.
DR STRING; 4932.YCR098C; -.
DR SwissLipids; SLP:000000076; -.
DR TCDB; 2.A.1.9.7; the major facilitator superfamily (mfs).
DR iPTMnet; P25346; -.
DR PaxDb; P25346; -.
DR PRIDE; P25346; -.
DR TopDownProteomics; P25346; -.
DR EnsemblFungi; YCR098C_mRNA; YCR098C; YCR098C.
DR GeneID; 850462; -.
DR KEGG; sce:YCR098C; -.
DR SGD; S000000695; GIT1.
DR VEuPathDB; FungiDB:YCR098C; -.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_12_1; -.
DR InParanoid; P25346; -.
DR OMA; IDGMFWM; -.
DR BioCyc; YEAST:G3O-29392-MON; -.
DR PRO; PR:P25346; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25346; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IMP:SGD.
DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IMP:SGD.
DR GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Glycerophosphoinositol transporter 1"
FT /id="PRO_0000050459"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 57322 MW; D173B1B0096F4D0D CRC64;
MEDKDITSVN EKEVNENTNP RIIKYDAERR ATRTETSKKD KWKNIVTIIA SGFALISDGY
VNGSMSMLNK VFVMEYGKKN YSSKVSTRVS NAALVGIIFG QFFMGIAADY YSRKSCILVA
TAILVIGSAL CAASHGTTVP GMFWMLTVMR GLVGIGVGAE YPTSTLSANE SANEYTTTKR
GGILVMVTNL PLAFGGPFAT IIFLIVYKIC SGTKHLEAIW RTVFAIGCFW PLSVFYFRWK
TATTEVYEKG RIKRNIPYFL ALKFYWKRLL GTCGTWFMYD FVTFPNGIFS STIISSVIKD
QNDLVKVAEW NLLLGVLAVL GVPIGAYLSD RIGRKYTLMF GFSGYIIFGL IIGCAYDQLK
KITPLFIIFY AFMNMLGNAG PGDMLGVISS EASATAVRGV FYGLSAVTGK IGSVVGVECF
QPIRDNLGAR WTFIIAAICG LIGIIITYFF VPHSLESDLM KQDVEFHNYL VSNGWTGKMG
FDETDEESMV RTIEVEENGT NCSKKNAEII SVRQVDQS
