GIT4_CANAL
ID GIT4_CANAL Reviewed; 532 AA.
AC A0A1D8PN14;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Glycerophosphocholine permease GIT4 {ECO:0000303|PubMed:24114876};
DE Short=GroPCho permease GIT4 {ECO:0000303|PubMed:24114876};
DE AltName: Full=Glycerophosphodiester transporter GIT4 {ECO:0000305};
GN Name=GIT4 {ECO:0000303|PubMed:24114876};
GN OrderedLocusNames=CAALFM_C500870CA;
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 GIT3 (PubMed:24114876). Does not
CC possess 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=16 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}.
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DR EMBL; CP017627; AOW29529.1; -; Genomic_DNA.
DR RefSeq; XP_715742.2; XM_710649.2.
DR AlphaFoldDB; A0A1D8PN14; -.
DR SMR; A0A1D8PN14; -.
DR STRING; 237561.A0A1D8PN14; -.
DR GeneID; 3642635; -.
DR KEGG; cal:CAALFM_C500870CA; -.
DR CGD; CAL0000176164; GIT4.
DR VEuPathDB; FungiDB:C5_00870C_A; -.
DR eggNOG; KOG0252; Eukaryota.
DR OrthoDB; 419975at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IMP:CGD.
DR GO; GO:0046942; P:carboxylic acid transport; IBA:GO_Central.
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..532
FT /note="Glycerophosphocholine permease GIT4"
FT /id="PRO_0000439801"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 532 AA; 59246 MW; B7D55072FBB9D024 CRC64;
MATRDLPHSV GDFCFGWVDQ IRSEITLGKS QDQLIKEDVL EDDETVETKV EIKNLWPAFA
SGAGLFSDGY VNAGISTVLS CLKKIYGDEF TKSNAMNNIG SIGFVGTVVG QLSFGYISDN
FDRKTGMLTA NVMLIFFTLM CAVASWGTTV QGFFACLTVW RFFLGIAIGA EYPTSSVIAS
EFANQLPSGH RNRYFSWFTN AMIDFGFVVS SFVPLVLLWI FTPRHLRAVW RLSIGLGVIP
PLILFFIRLK MDNSKSFKKM NMKRVNYSKY PWWLIIKFYW FRLTVVSLIW FIYDFSVYSF
GTFNTIIIGE VIPNGTLYEN WGWSVVFNLF YMPGAFLGAF IGDYLGPRLT LAIGVGAQGI
IGIAMSACLK SLKKHVAGFV VVFGIFSTFG EFGPGNNTGL LASKTCASSI RGQYYGIAAA
IGKIGAFVGT WVFPAIQKHY AYSEDLSLQV PFYVSSALCL FSAFLTIFFV PPVGQDAINK
EDRLFKEYLE ENGVDIRLLG DSGVVTQYQE DEDIGVISDE KDDTVKVQQK NV
