GIT3_CANAL
ID GIT3_CANAL Reviewed; 535 AA.
AC Q5A1L6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Major glycerophosphoinositol permease GIT3 {ECO:0000303|PubMed:24114876};
DE Short=GroPCho permease GIT3 {ECO:0000303|PubMed:24114876};
DE AltName: Full=Glycerophosphodiester transporter GIT3 {ECO:0000305};
GN Name=GIT3 {ECO:0000303|PubMed:24114876};
GN OrderedLocusNames=CAALFM_C500880CA;
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, DISRUPTION PHENOTYPE, INDUCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 glycerophosphocholine (GroPCho) with GIT4 (PubMed:24114876). GIT3 acts
CC as the major GroPCho permease (PubMed:24114876). Does not possess
CC detectable glycerophosphoinositol (GroPIns) transport activity
CC (PubMed:24114876). The expanded ability to utilize GroPIns and GroPCho
CC results from the organism's pathogenic nature and its need to occupy a
CC variety of environments within its host organism (PubMed:24114876).
CC This possibility is buttressed by the fact that GroPIns and GroPCho are
CC present and abundant in human fluids (PubMed:24114876).
CC {ECO:0000269|PubMed:24114876}.
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:24114876};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32912;
CC Evidence={ECO:0000269|PubMed:24114876};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for glycerophosphocholine transport
CC {ECO:0000269|PubMed:24114876};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24114876};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the transcription
CC factor PHO4 (PubMed:24114876).
CC -!- DISRUPTION PHENOTYPE: Triple deletion of GIT2, GIT3 and GIT4 impairs
CC the uptake of glycerophosphocholine (GroPCho) and reduces virulence in
CC a mouse model of blood stream infection (PubMed:24114876).
CC {ECO:0000269|PubMed:24114876}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017627; AOW29530.1; -; Genomic_DNA.
DR RefSeq; XP_715741.1; XM_710648.2.
DR AlphaFoldDB; Q5A1L6; -.
DR SMR; Q5A1L6; -.
DR STRING; 237561.Q5A1L6; -.
DR PRIDE; Q5A1L6; -.
DR EnsemblFungi; KHC74999; KHC74999; W5Q_04123.
DR EnsemblFungi; KHC86151; KHC86151; I503_04124.
DR GeneID; 3642634; -.
DR KEGG; cal:CAALFM_C500880CA; -.
DR CGD; CAL0000176352; GIT3.
DR VEuPathDB; FungiDB:C5_00880C_A; -.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_12_1; -.
DR InParanoid; Q5A1L6; -.
DR OMA; IMFTNFQ; -.
DR OrthoDB; 419975at2759; -.
DR PHI-base; PHI:3822; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IMP:CGD.
DR GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IMP:CGD.
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 Pfam; PF00083; Sugar_tr; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..535
FT /note="Major glycerophosphoinositol permease GIT3"
FT /id="PRO_0000439800"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 535 AA; 59400 MW; 47CC2BEA8C2AA213 CRC64;
MSTRDLPHSF SELSYGWVKR IRAEFTVGKS KEQLLAEDYH STTDEDSEVV TSVKANSLWP
AFASGAGLFS DGYVNNSIST VLFCLKKIYP DEITKSNAIN NIASIAFVGT VVGQLGFGYI
SDRIARKGGM MAANVMLIFF TLMCAVGSWG VTVQGFFACL TVWRFFLGVA IGAEYPTSSV
IASEFANQLP PGKRNRYFSW FTNAMIDSGF VVSAFVPFVL IWIFTEKHLR ALWRVAIGLG
VIPPLSLFFM RLKMKNSSSF QKLHMKNVKY RDYPWWLIVK FYWFRLTIVS LIWFIYDFSA
YSFGNFNTII IGEIIPEAPI WKQWGWSIVF NLFYIPGAFL GAISADYIGP RLTLALGVGI
QGVIGIAMSA CLNSLKKHIA GFVVVFGIFT TFGEFGPGDN IGLLASKTSA TAIRGQYYGI
AAAIGKIGAF VGTWVFPAIQ SKYANNANPD LQLQVPFYIS SALCLFSACL AIFFCPQVGQ
DAIYKEDHDF VQYLSNNGFD INMLGEGGDV REVCRESDSL EKGKRDDFQV DNNSL
