GAP6_CANAL
ID GAP6_CANAL Reviewed; 568 AA.
AC A0A1D8PNP3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Amino-acid permease GAP6;
GN Name=GAP6; OrderedLocusNames=CAALFM_C503500WA;
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=16215176; DOI=10.1128/ec.4.10.1687-1696.2005;
RA Tournu H., Tripathi G., Bertram G., Macaskill S., Mavor A., Walker L.,
RA Odds F.C., Gow N.A., Brown A.J.;
RT "Global role of the protein kinase Gcn2 in the human pathogen Candida
RT albicans.";
RL Eukaryot. Cell 4:1687-1696(2005).
RN [5]
RP INDUCTION.
RX PubMed=16207920; DOI=10.1099/mic.0.28353-0;
RA Kunze D., Melzer I., Bennett D., Sanglard D., MacCallum D., Norskau J.,
RA Coleman D.C., Odds F.C., Schafer W., Hube B.;
RT "Functional analysis of the phospholipase C gene CaPLC1 and two unusual
RT phospholipase C genes, CaPLC2 and CaPLC3, of Candida albicans.";
RL Microbiology 151:3381-3394(2005).
RN [6]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [7]
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 [8]
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 with rather broad substrate specificity
CC (PubMed:21764911). Transports many amino acids including proline,
CC methionine, leucine, valine, isoleucine, phenylalanine, tryptophan,
CC threonine and tyrosine, but not basic ones (arginine) and citrulline
CC (PubMed:21764911, PubMed:28028545). Functions as a sensor via detection
CC of some amino acids including methionine, leading to a rapid activation
CC of trehalase, a downstream target of PKA (PubMed:21764911).
CC {ECO:0000269|PubMed:21764911, ECO:0000269|PubMed:28028545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28028545};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is under control of the CSY1 amino-acid sensor
CC (PubMed:28028545). Expression is also regulated by PLC1 and GCN4
CC (PubMed:16207920, PubMed:16215176). Expression is induced during
CC development of rat catheter biofilm (PubMed:19527170).
CC {ECO:0000269|PubMed:16207920, ECO:0000269|PubMed:16215176,
CC ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:28028545}.
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; AOW29762.1; -; Genomic_DNA.
DR RefSeq; XP_711412.2; XM_706320.2.
DR AlphaFoldDB; A0A1D8PNP3; -.
DR SMR; A0A1D8PNP3; -.
DR STRING; 237561.A0A1D8PNP3; -.
DR GeneID; 3646968; -.
DR KEGG; cal:CAALFM_C503500WA; -.
DR CGD; CAL0000192270; GAP6.
DR VEuPathDB; FungiDB:C5_03500W_A; -.
DR OMA; NYALFWV; -.
DR OrthoDB; 600052at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
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; IMP:CGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR Pfam; PF00324; AA_permease; 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..568
FT /note="Amino-acid permease GAP6"
FT /id="PRO_0000439811"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 568 AA; 61796 MW; 160B0073536B227F CRC64;
MPKEASSPEC YTTSTSSNEI SEKPGMWRNF KDSFKPPVPI DDIENGSISS TQLKGGQNVP
LQQSLKKRQL QMIALGGCVG SGLLVASGAA LRNGPASLLI AWFIVSTFLY CTMQCLAELS
STFPVSGSFA VYSIKFIDPS WGTAMGYNYA LFWVVVMPLE LVASSMTIKF WPSNINTSVW
VAVFYVLIIG TNLFGGTRAF GETEFVASVI KLLGIVGFNI LAIVLICGGG DQGYIGGKNW
HPPFTTGVKG VISVLLTATY SLAGTELVGL TSAEAAGDAR KVLPKAIKQV LWRILIFYLL
TLTLVGFLVP ASDPQLIGGG SGASASPFVI AIREGGIKGL PSVFNVVVLV ALLAIANSAV
YGFSRTILAL AEQGVAPSIF KYVDRQGRPL AGIATSAIVG LLSFVSASKQ QEQVFDWLVA
LSGLSTFFTW GSINAAHIRF RIAMKVQGRS LDELPYKANT GVLGAYYGLI MNVAVLALQF
WLAVWPIGGK PDATYFFKQY LAAVLVLAVY VIHKVATRNW KFMVDYKDMD LDSGRSDIDI
DILKQELEEE REAYKRQPWY YKFYQFWC
