GAP1_CANAL
ID GAP1_CANAL Reviewed; 582 AA.
AC Q5AG77; Q8TGV8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Amino-acid permease GAP1;
GN Name=GAP1; OrderedLocusNames=CAALFM_C502790CA;
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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12949183; DOI=10.1099/mic.0.26215-0;
RA Biswas S., Roy M., Datta A.;
RT "N-acetylglucosamine-inducible CaGAP1 encodes a general amino acid permease
RT which co-ordinates external nitrogen source response and morphogenesis in
RT Candida albicans.";
RL Microbiology 149:2597-2608(2003).
RN [5]
RP INDUCTION.
RX PubMed=14617156; DOI=10.1046/j.1365-2958.2003.03747.x;
RA Limjindaporn T., Khalaf R.A., Fonzi W.A.;
RT "Nitrogen metabolism and virulence of Candida albicans require the GATA-
RT type transcriptional activator encoded by GAT1.";
RL Mol. Microbiol. 50:993-1004(2003).
RN [6]
RP INDUCTION.
RX PubMed=15470236; DOI=10.1128/ec.3.5.1076-1087.2004;
RA Lorenz M.C., Bender J.A., Fink G.R.;
RT "Transcriptional response of Candida albicans upon internalization by
RT macrophages.";
RL Eukaryot. Cell 3:1076-1087(2004).
RN [7]
RP INDUCTION.
RX PubMed=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
RA Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
RT "Transcriptional profiling in Candida albicans reveals new adaptive
RT responses to extracellular pH and functions for Rim101p.";
RL Mol. Microbiol. 54:1335-1351(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21764911; DOI=10.1128/ec.05026-11;
RA Kraidlova L., Van Zeebroeck G., Van Dijck P., Sychrova H.;
RT "The Candida albicans GAP gene family encodes permeases involved in general
RT and specific amino acid uptake and sensing.";
RL Eukaryot. Cell 10:1219-1229(2011).
RN [9]
RP INDUCTION.
RX PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT biofilm formation by Candida albicans.";
RL Mol. Microbiol. 80:995-1013(2011).
RN [10]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
RN [11]
RP INDUCTION.
RX PubMed=23572557; DOI=10.1128/mbio.00637-12;
RA Desai J.V., Bruno V.M., Ganguly S., Stamper R.J., Mitchell K.F., Solis N.,
RA Hill E.M., Xu W., Filler S.G., Andes D.R., Fanning S., Lanni F.,
RA Mitchell A.P.;
RT "Regulatory role of glycerol in Candida albicans biofilm formation.";
RL MBio 4:E00637-E00637(2013).
RN [12]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28028545; DOI=10.1128/msphere.00284-16;
RA Kraidlova L., Schrevens S., Tournu H., Van Zeebroeck G., Sychrova H.,
RA Van Dijck P.;
RT "Characterization of the Candida albicans amino acid permease family: Gap2
RT is the only general amino acid permease and Gap4 is an S-adenosylmethionine
RT (SAM) transporter required for SAM-induced morphogenesis.";
RL MSphere 1:0-0(2016).
CC -!- FUNCTION: Amino-acid permease that coordinates external nitrogen source
CC response and morphogenesis (PubMed:12949183, PubMed:21764911,
CC PubMed:28028545). Is capable of transporting several structurally
CC unrelated amino acids such as leucine and phenylalanine, though with a
CC lower capacity than the GAP2 and GAP6 permeases (PubMed:21764911). Has
CC citrulline import activity (PubMed:12949183). GAP1 is also able to
CC transport thialysine, and thus probably also lysine (PubMed:21764911).
CC Functions as a sensor via detection of some amino acids including
CC methionine, leading to a rapid activation of trehalase, a downstream
CC target of PKA (PubMed:21764911). {ECO:0000269|PubMed:12949183,
CC ECO:0000269|PubMed:21764911, ECO:0000269|PubMed:28028545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21764911,
CC ECO:0000269|PubMed:28028545}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is under control of the CSY1 amino-acid sensor
CC (PubMed:28028545). Expression is induced by N-acetylglucosamine
CC (PubMed:12949183). Expression is also regulated by CPH1-mediated RAS1
CC signaling but is independent of EFG1 (PubMed:12949183). Induced during
CC biofilm development (PubMed:21414038, PubMed:22265407,
CC PubMed:23572557). Induced upon internalization by host macrophages
CC (PubMed:15470236). Expression is down-regulated by growth in alkaline
CC conditions (PubMed:15554973). Expression is also controlled by the
CC nitrogen-dependent GATA-type transcriptional activator GAT1
CC (PubMed:14617156). {ECO:0000269|PubMed:12949183,
CC ECO:0000269|PubMed:14617156, ECO:0000269|PubMed:15470236,
CC ECO:0000269|PubMed:15554973, ECO:0000269|PubMed:21414038,
CC ECO:0000269|PubMed:22265407, ECO:0000269|PubMed:23572557,
CC ECO:0000269|PubMed:28028545}.
CC -!- DISRUPTION PHENOTYPE: Decreases two fold the citrulline uptake
CC (PubMed:12949183). Leads to defective hyphal formation in solid hyphal-
CC inducing media and exhibits less hyphal clumps when induced by N-
CC acetylglucosamine (PubMed:12949183). {ECO:0000269|PubMed:12949183}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29704.1; -; Genomic_DNA.
DR RefSeq; XP_720611.1; XM_715518.2.
DR AlphaFoldDB; Q5AG77; -.
DR SMR; Q5AG77; -.
DR STRING; 237561.Q5AG77; -.
DR TCDB; 2.A.3.10.23; the amino acid-polyamine-organocation (apc) family.
DR PRIDE; Q5AG77; -.
DR EnsemblFungi; KHC75179; KHC75179; W5Q_04306.
DR EnsemblFungi; KHC85938; KHC85938; I503_04306.
DR GeneID; 3637806; -.
DR KEGG; cal:CAALFM_C502790CA; -.
DR CGD; CAL0000177621; GAP1.
DR VEuPathDB; FungiDB:C5_02790C_A; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q5AG77; -.
DR OMA; VSQCGVW; -.
DR OrthoDB; 600052at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:CGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:CGD.
DR GO; GO:0006865; P:amino acid transport; IGI:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Amino-acid permease GAP1"
FT /id="PRO_0000439806"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 582 AA; 63951 MW; 72CC98F97D0E4053 CRC64;
MLHKKETNDT FVQLNRSPST GEQKSSGIWS SIKDSFKPAL PQDKLTGVDD IPDRELTDIE
RININAANSN LQRKLKTRHL QMIAIGSSIG TGLFVGTGGA LSTGGPAAIV LAWAISAISV
FMTMQGLGEL AVAFPVSGGF NLYASKFLEP GIGFAVGWNY FLQFFVLLPL ELVAGAITIK
YWNASINSDV FVIIFWFVVL VITMLGVRWY GEAELVFCTI KVIAVIGFII LGIVLICGGG
PNHEFIGGKY WREPGPFANS FKGFASSLIT AAFSFGGTEM IALTASESSN VRHALPKAIK
QVFWRIVIFY LGSIIMIATL VPYNDKRLLG SSSVDVTASP FTIAIVNGGI KGLPSVINAV
ILISVLSVGN ASVYATSRTL NSLAEQGMAP KWTGYIDRAG RPLFAILITN VFGLFALIAA
DNEKQVVAFN WLLALSGLSS IFTWMSINLS HIRFRRAMKV QNRSLTELPF VAQSGVWGSY
FGLTLNILYL IAQFYIGLFP VGGKPNAYDF FLAYLGVPVI LASWIGYKIW KRDWTLFIRA
KDIDLDTGRI NVDLDLLQQE IAEEKAQLAE KPFYIRIYRF WC
