GAP4_CANAL
ID GAP4_CANAL Reviewed; 607 AA.
AC Q59WB3;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=S-adenosylmethionine permease GAP4 {ECO:0000303|PubMed:28028545};
DE Short=SAM permease {ECO:0000303|PubMed:28028545};
DE AltName: Full=Amino-acid permease GAP4 {ECO:0000305};
GN Name=GAP4 {ECO:0000303|PubMed:28028545};
GN OrderedLocusNames=CAALFM_C107120WA;
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=15814841; DOI=10.1091/mbc.e05-01-0071;
RA Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
RA Enjalbert B., Brown A.J.;
RT "Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the
RT fungal pathogen, Candida albicans.";
RL Mol. Biol. Cell 16:2913-2925(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=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [8]
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 [9]
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 involved in S-adenosylmethionine (SAM)
CC transport and required for SAM-induced morphogenesis (PubMed:28028545).
CC GAP4 is also able to transport arginine and thialysine, and thus
CC probably also lysine (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 also regulated by HAP43, GCN2, GCN4
CC and SSN6 (PubMed:16215176, PubMed:15814841, PubMed:21592964). Induced
CC during biofilm development (PubMed:22265407).
CC {ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:16215176,
CC ECO:0000269|PubMed:21592964, 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; CP017623; AOW26364.1; -; Genomic_DNA.
DR RefSeq; XP_713900.1; XM_708807.2.
DR AlphaFoldDB; Q59WB3; -.
DR SMR; Q59WB3; -.
DR STRING; 237561.Q59WB3; -.
DR TCDB; 2.A.3.10.25; the amino acid-polyamine-organocation (apc) family.
DR PRIDE; Q59WB3; -.
DR EnsemblFungi; KHC83473; KHC83473; W5Q_00691.
DR EnsemblFungi; KHC89509; KHC89509; I503_00695.
DR GeneID; 3644463; -.
DR KEGG; cal:CAALFM_C107120WA; -.
DR CGD; CAL0000198089; GAP4.
DR VEuPathDB; FungiDB:C1_07120W_A; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q59WB3; -.
DR OMA; TFWRIAI; -.
DR OrthoDB; 600052at2759; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:EnsemblFungi.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005771; C:multivesicular body; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:CGD.
DR GO; GO:0001761; F:beta-alanine transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0005291; F:high-affinity L-histidine transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0003333; P:amino acid transmembrane transport; IMP:CGD.
DR GO; GO:0015817; P:histidine transport; IEA:EnsemblFungi.
DR GO; GO:0006828; P:manganese ion transport; IEA:EnsemblFungi.
DR GO; GO:0015805; P:S-adenosyl-L-methionine 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; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..607
FT /note="S-adenosylmethionine permease GAP4"
FT /id="PRO_0000439809"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 607 AA; 66478 MW; 88A2E3251053A030 CRC64;
MSYKGNDIEK QQSASTATGF NDKQIASTSE DATDRSHNIH GDTSSLDSRY TYETVDQEKN
YFKRVYNSFK PMNLEEQGID TSQLTPVERT IIASAKHPLA RRLKARHLQM IAIGGSIGTG
LFVGSGYALA NGGPGAVLIG YVIVGYALLT VVNALGELSV QFPVSGSFNA FFSRFLEPSF
GGTFGILYAA SWCISLPSEL IAAAMTIQYW NTEVNPAVWV AVFWVVIVVI NLFGVKGYGE
MEYFLSIIKV LAVVGFIILG ICITCGVGDQ GYIGGKYWHN PGAFNHGLKG VTSVFISAAF
SFGGIELVAL AASETANPRI SLPAAVKSTF WRIFIFYILT AIIIGCLVPY TNDDLLNGTG
IAASPFVIAV SQGGIRVVPH IMNAVVVIAV ISVGNSSVYG CSRTLASLAV QGLLPKSMGY
IDRGGRPLIA ILFTSAIGLL GFLVVVDNEG DVFTWFFSIC SLSSFFTWGA INVVHLRWRF
ALAAQGRSTD EIIFRSPLGT FGSWTGILVL ILIVIGEVWV SIWPIGSPAD VQQFWKNCLS
LPLMIVMWAG FKTYHRSWNM LWVKLEDIDL DTGRREIDVE LLKQELAEER QIIKSKPFVY
RIYKFFF
