ID A0A2K5ZTS6_MANLE Unreviewed; 339 AA.
AC A0A2K5ZTS6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=SLC1A5 {ECO:0000313|Ensembl:ENSMLEP00000031220.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000031220.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000031220.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(in) + L-alanine(out) + Na(+)(out) = D-serine(out) +
CC L-alanine(in) + Na(+)(in); Xref=Rhea:RHEA:75311, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:35247, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000256|ARBA:ARBA00035832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(in) + L-glutamine(out) + Na(+)(out) = D-serine(out) +
CC L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:75307, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:35247, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036702};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-glutamate(out) + L-glutamine(in) + Na(+)(out) =
CC H(+)(in) + L-glutamate(in) + L-glutamine(out) + Na(+)(in);
CC Xref=Rhea:RHEA:70883, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(out) + L-glutamine(in) + Na(+)(out) = L-alanine(in)
CC + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70867,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57972, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine(in) + L-glutamine(out) + Na(+)(out) = L-
CC asparagine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70859,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine(out) + L-glutamine(in) + Na(+)(out) = L-
CC asparagine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70891,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-methionine(out) + Na(+)(out) = L-
CC glutamine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70875,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57844, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-
CC glutamine(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:70887,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035896};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-threonine(out) + Na(+)(out) = L-
CC glutamine(out) + L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:70879,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00037007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-valine(out) + Na(+)(out) = L-
CC glutamine(out) + L-valine(in) + Na(+)(in); Xref=Rhea:RHEA:70871,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57762, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in)
CC + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036385};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(out) + L-threonine(in) + Na(+)(out) = L-
CC glutamine(in) + L-threonine(out) + Na(+)(in); Xref=Rhea:RHEA:70863,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036690};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC ChEBI:CHEBI:16382; Evidence={ECO:0000256|ARBA:ARBA00024145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nitrate(in) = nitrate(out); Xref=Rhea:RHEA:34923,
CC ChEBI:CHEBI:17632; Evidence={ECO:0000256|ARBA:ARBA00035073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiocyanate(in) = thiocyanate(out); Xref=Rhea:RHEA:75347,
CC ChEBI:CHEBI:18022; Evidence={ECO:0000256|ARBA:ARBA00036895};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361216}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000256|RuleBase:RU361216}.
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DR RefSeq; XP_011825055.1; XM_011969665.1.
DR AlphaFoldDB; A0A2K5ZTS6; -.
DR Ensembl; ENSMLET00000054788.1; ENSMLEP00000031220.1; ENSMLEG00000039768.1.
DR GeneID; 105531675; -.
DR CTD; 6510; -.
DR GeneTree; ENSGT00940000159485; -.
DR OrthoDB; 49426at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR11958:SF19; NEUTRAL AMINO ACID TRANSPORTER B(0); 1.
DR PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR SUPFAM; SSF118215; Proton glutamate symport protein; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361216};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Symport {ECO:0000256|ARBA:ARBA00022847, ECO:0000256|RuleBase:RU361216};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361216};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361216};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361216}.
FT TRANSMEM 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 64..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 100..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 175..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 212..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT REGION 306..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 36635 MW; 8737D29E6DC2B95F CRC64;
MYSTSYEERN ITGTRVKVPV GQEVEGMNIL GLVVFAIVFG VALRKLGPEG ELLIRFFNSF
NEATMVLVSW IMWYAPVGIM FLVAGKIVEM EDVGLLFARL GKYILCCLLG HAIHGLLVLP
LIYFLFTRKN PYRFLWGIVT PLATAFGTSS SSATLPLMMK CVEENNGVAK HISRFILPIG
ATVNMDGAAL FQCVAAVFIA QLSEQSLDFV KIITILVTAT ASSVGAAGIP AGGVLTLAII
LEAVNLPVDH ISLILAVDWL VDRSCTVLNV EGDALGAGLL QNYVDRTEVR STEPELIQVK
SELPLDPLPA PTEEGNPLLR HYRGPAGDAT VASEKESVM
//
