GAP3_CANAL
ID GAP3_CANAL Reviewed; 599 AA.
AC A0A1D8PN88;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Amino-acid permease GAP3;
GN Name=HIP1; Synonyms=GAP3 {ECO:0000303|PubMed:28028545};
GN OrderedLocusNames=CAALFM_C501800CA;
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 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 [7]
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 [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 that is able to transport phenylalanine
CC (PubMed:21764911, PubMed:28028545). {ECO:0000269|PubMed:21764911,
CC 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 also regulated by PLC1 and GCN4
CC (PubMed:16207920, PubMed:16215176). Expression is induced during
CC development of biofilm (PubMed:22265407). {ECO:0000269|PubMed:16207920,
CC ECO:0000269|PubMed:16215176, ECO:0000269|PubMed:22265407,
CC 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; AOW29610.1; -; Genomic_DNA.
DR RefSeq; XP_714611.2; XM_709518.2.
DR AlphaFoldDB; A0A1D8PN88; -.
DR SMR; A0A1D8PN88; -.
DR STRING; 237561.A0A1D8PN88; -.
DR GeneID; 3643761; -.
DR KEGG; cal:CAALFM_C501800CA; -.
DR CGD; CAL0000181363; HIP1.
DR VEuPathDB; FungiDB:C5_01800C_A; -.
DR eggNOG; KOG1286; Eukaryota.
DR OrthoDB; 612873at2759; -.
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 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; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..599
FT /note="Amino-acid permease GAP3"
FT /id="PRO_0000439808"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65578 MW; 628AED1D58B9A268 CRC64;
MTTKEKDEFN IGSLQNSPES STNMSPDVIT TPISKWQAFK DSFKPPEQKP LASSSSSTSS
LSASSPHHND VANNYDIEKS LRPDQQGELK RELKNRHVQM IALGGSVGTG LLIGSGGALH
QGGPAALLIA WGITGTMVFC IIHSLGELCV AFPVNGAFST YANMFVDSSW AFAVGWNYAI
MWLIVLPLEL VAAAMCITYW NDEINPASWV AIFYVLIVVI NIFGVKYYGD AEMYLTIFKI
IAIVGFIILG VVLVCGGGPT HEFIGNKYWK QDGAFANGFK GVATTFVTAS YSMAGSEMVG
LASAEVANPQ KSLPKAIRQV FWRIFLFYFL SLTFIGLLVP SNSPQLLGAS GTSASPFVIA
IKNGGIYALP SIFNACILLS VLSVGNSAVY GCSRTIQSLG AQGLGPKIFA YVDRKGRPLG
GLVMSAIFGL LCFLSAYHDE ATIFNWLLSV AGLATIFSWF NIGLCHVRFR LALRKQGRSL
QELTFTALTG VWGSVYSMIF LCVVLVIQFW TALFPLGSKG KANAENFFQN YLGAVVILIF
YVGHKLYTRN WKLCVKLEDI DLDSGRRSFD LDLIRAEIEE EKAANKAKPL YKRLWNYWC
