ID A0A2K6QKQ3_RHIRO Unreviewed; 537 AA.
AC A0A2K6QKQ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=SLC1A5 {ECO:0000313|Ensembl:ENSRROP00000029363.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000029363.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000029363.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6QKQ3; -.
DR Ensembl; ENSRROT00000053763.1; ENSRROP00000029363.1; ENSRROG00000038480.1.
DR GeneTree; ENSGT00940000159485; -.
DR OMA; VGTFYAT; -.
DR Proteomes; UP000233200; 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; PS00713; NA_DICARBOXYL_SYMP_1; 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:UP000233200};
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 54..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 224..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 262..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 298..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 373..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 410..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT REGION 501..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 55693 MW; C0F420E321DF0596 CRC64;
MVADPPRGDS KGLAAAEPTA IGGLALASIE DQGAAAGGCC GSRDRVRRCL RANLLVLLTV
VAVVVGVALG LGISGAGGAL ALGPQRLSAF LFPGELLLRL LRMIILPLVV CSLIGGAASL
DPGALGRLGA WALLFFLVTT LLASALGVGL ALALQPGAAS AAINASVAAA GSAENAPNKE
VLDSFLDLAR NIFPSNLVSA AFRSVSPQGC PEGSGVPVGQ EVEGMNILGL VVFAIVFGVA
LRKLGPEGEL LICFFNSFNE ATMVLVSWIM WYAPVGIMFL VAGKIVEMED VGLLFARLGK
YILCCLLGHA IHGLLVLPLI YFLFTRKNPY RFLWGIVTPL ATAFGTSSSS ATLPLMMKCV
EENNGVAKHI SRFILPIGAT VNMDGAALFQ CVAAVFIAQL SEQSLDFVKI ITILVTATAS
SVGAAGIPAG GVLTLAIILE AVNLPADHIS LILAVDWLVD RSCTVLNVEG DALGAGLLQN
YVDRTEVRST EPELIQVKSE LPLDPLPAPT EEGNPLLQHY RGPAGDATAA SEKESVM
//
