ID Q6GM93_XENLA Unreviewed; 527 AA.
AC Q6GM93;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=slc1a5.S {ECO:0000313|RefSeq:NP_001086093.1,
GN ECO:0000313|Xenbase:XB-GENE-6077517};
GN Synonyms=aaat {ECO:0000313|RefSeq:NP_001086093.1}, asct2
GN {ECO:0000313|RefSeq:NP_001086093.1}, atbo
GN {ECO:0000313|RefSeq:NP_001086093.1}, m7v1
GN {ECO:0000313|RefSeq:NP_001086093.1}, m7vs1
GN {ECO:0000313|RefSeq:NP_001086093.1}, MGC82017
GN {ECO:0000313|EMBL:AAH74180.1}, r16
GN {ECO:0000313|RefSeq:NP_001086093.1}, rdrc
GN {ECO:0000313|RefSeq:NP_001086093.1}, slc1a5
GN {ECO:0000313|RefSeq:NP_001086093.1,
GN ECO:0000313|Xenbase:XB-GENE-6077517};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH74180.1};
RN [1] {ECO:0000313|RefSeq:NP_001086093.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH74180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH74180.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001086093.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 EMBL; BC074180; AAH74180.1; -; mRNA.
DR RefSeq; NP_001086093.1; NM_001092624.1.
DR STRING; 8355.Q6GM93; -.
DR PaxDb; 8355-Q6GM93; -.
DR GeneID; 444522; -.
DR KEGG; xla:444522; -.
DR AGR; Xenbase:XB-GENE-6077517; -.
DR CTD; 444522; -.
DR Xenbase; XB-GENE-6077517; slc1a5.S.
DR OMA; VGTFYAT; -.
DR OrthoDB; 49426at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 444522; Expressed in kidney and 19 other cell types or tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IEA:UniProt.
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 2: Evidence at transcript level;
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:UP000186698};
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 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 293..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 368..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 405..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 55860 MW; C0B9BF73A1A03126 CRC64;
MKESECNGTS SPGEHPVPLA LYRPGDSAPS PGCGPRCRRF LRGNVLVLLT VMGVILGAGL
GMAVRPLNLS KAHIASFSFP GELLLRLLKM IILPLVVCSL VSGAASLQPS ALGKLGGWAM
LFFLITTLLA SSLGVCLALL IRPGVGALVE SGQGDGVPEG KDVVDSFLDL IRNIFPSNLV
SAAFQSYATS YKLEHVNSSV LGDMNSTWVK VPYGQEVEGM NILGLVVFAI VFGIALRKLG
PEGEILIRFF NSFNEATMVL VTWIMWYAPL GIMFLVAGKI VEMEDVVQLF TSLGKYISCC
IVGHIIHGLL VLPLIYFAFT RKNPYRFLWG IVSALATAFG TSSSSATLPL MMKCVEEKNG
VSKQISRFIL PIGATVNMDG AALFQCVAAV FIAQLNNVSL DFIQVITILV TATASSVGAA
GIPAGGVLTL AIILEAVGLP TNDISLILAV DWLVDRTCTV LNVEGDAFGA GLLQVYSDRT
SSSNDGAELS AVQVEIPGDH PEGDPLLQKH TQLKSDGASA LEKESTM
//
