GIT1_CANAL
ID GIT1_CANAL Reviewed; 519 AA.
AC Q59Q30;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glycerophosphoinositol permease 1 {ECO:0000303|PubMed:21984707};
DE AltName: Full=Glycerophosphodiester transporter GIT1 {ECO:0000305};
GN Name=GIT1 {ECO:0000303|PubMed:21984707}; Synonyms=GIT99;
GN OrderedLocusNames=CAALFM_C206590CA;
GN ORFNames=orf19.34 {ECO:0000303|PubMed:19151328};
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 INDUCTION.
RX PubMed=19151328; DOI=10.1128/ec.00387-08;
RA MacCallum D.M., Castillo L., Nather K., Munro C.A., Brown A.J., Gow N.A.,
RA Odds F.C.;
RT "Property differences among the four major Candida albicans strain
RT clades.";
RL Eukaryot. Cell 8:373-387(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RX PubMed=21984707; DOI=10.1128/ec.05160-11;
RA Bishop A.C., Sun T., Johnson M.E., Bruno V.M., Patton-Vogt J.;
RT "Robust utilization of phospholipase-generated metabolites,
RT glycerophosphodiesters, by Candida albicans: role of the CaGit1 permease.";
RL Eukaryot. Cell 10:1618-1627(2011).
RN [6]
RP FUNCTION.
RX PubMed=24114876; DOI=10.1074/jbc.m113.505735;
RA Bishop A.C., Ganguly S., Solis N.V., Cooley B.M., Jensen-Seaman M.I.,
RA Filler S.G., Mitchell A.P., Patton-Vogt J.;
RT "Glycerophosphocholine utilization by Candida albicans: role of the Git3
RT transporter in virulence.";
RL J. Biol. Chem. 288:33939-33952(2013).
CC -!- FUNCTION: Glycerophosphodiester transporter that mediates uptake of
CC glycerophosphoinositol (GroPIns) as a source of inositol and phosphate
CC (PubMed:21984707, PubMed:24114876). Does not possess detectable
CC glycerophosphocholine (GroPCho) transport activity (PubMed:21984707).
CC Although no glycerophosphoinositol transport activity occurs in the
CC absence of GIT1, C.albicans is still able to use glycerophosphoinositol
CC as a phosphate source at pH 7.5, albeit slowly (PubMed:21984707). Thus,
CC a second, GIT1-independent, mechanism must exist for utilizing
CC glycerophosphoinositol as a phosphate source at physiological pH
CC (PubMed:21984707, PubMed:24114876). The expanded ability to utilize
CC GroPIns and GroPCho results from the organism's pathogenic nature and
CC its need to occupy a variety of environments within its host organism
CC (PubMed:21984707). This possibility is buttressed by the fact that
CC GroPIns and GroPCho are present and abundant in human fluids
CC (PubMed:21984707, PubMed:24114876). {ECO:0000269|PubMed:21984707,
CC ECO:0000269|PubMed:24114876}.
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:21984707};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32916;
CC Evidence={ECO:0000269|PubMed:21984707};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for glycerophosphoinositol transport
CC {ECO:0000269|PubMed:21984707};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21984707};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Phosphate levels regulate glycerophosphoinositol transport
CC activity and transcription factor PHO4 is required for GIT1 expression
CC (PubMed:21984707). Expression profile differs significantly in isolates
CC of high, medium, and low virulence, being the highest in the most
CC virulent strains (PubMed:19151328). {ECO:0000269|PubMed:19151328,
CC ECO:0000269|PubMed:21984707}.
CC -!- DISRUPTION PHENOTYPE: Abolished the utilization of
CC glycerophosphoinositol(GroPIns) as a phosphate source
CC (PubMed:21984707). {ECO:0000269|PubMed:21984707}.
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; CP017624; AOW27660.1; -; Genomic_DNA.
DR RefSeq; XP_711841.1; XM_706749.1.
DR AlphaFoldDB; Q59Q30; -.
DR SMR; Q59Q30; -.
DR STRING; 237561.Q59Q30; -.
DR EnsemblFungi; KHC81693; KHC81693; W5Q_02082.
DR EnsemblFungi; KHC88024; KHC88024; I503_02096.
DR GeneID; 3646562; -.
DR KEGG; cal:CAALFM_C206590CA; -.
DR CGD; CAL0000193792; GIT1.
DR VEuPathDB; FungiDB:C2_06590C_A; -.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_12_1; -.
DR OMA; IDGMFWM; -.
DR OrthoDB; 824050at2759; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IDA:CGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IDA:CGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..519
FT /note="Glycerophosphoinositol permease 1"
FT /id="PRO_0000439798"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 519 AA; 57163 MW; 896615C246109D9D CRC64;
MSDLVKSSEV IETTEVPPHN NNNNKRHFKY DSEQRKQRLA GGVKLKDALM ILCAGFALIS
DGYQNNVMSM MNKVFALEYP KEYTASLSTQ VSNASLVGTI FGQVIIGLTA DYIGRKWSIV
TATCFLIFGT MMCAASHGKT VNGMFWMLTI FRGVTGFGIG AEYPSSSVTA SEAANESVKR
RGGAFILATN LPLSFGGPFA LCIFLIVRRI CGNHLDAIWR TMFAIGCFWP LSVFYFRLKM
VTSELYTKSA IKQRAPYWLA LKYYWPRLIG TCVAWFLYDF VTFPNGIFSA GIISNVIPKS
EKNNLEKIAE WNLLLGAIAL PGVFVGAYVV DILGRKYTMM IGFCGYIVFG LIVGCGYHQI
KPITGLFIVF YGLMMSCGNF GPGNNMGLTS SESFATPIRG TAYGISAAIG KVGAVVGTKT
FSPIQKNLGD KWTFIIAAIC GLAGVLVTFI FIPHLKDEDL LEEDVKFKNY LIDNGWKGKF
GIQEYDEEED LEGSSEDSSD GEIVKNNTKN DVEKVDALK
