ID A0A2I2Z9U1_GORGO Unreviewed; 339 AA.
AC A0A2I2Z9U1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=SLC1A5 {ECO:0000313|Ensembl:ENSGGOP00000043937.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000043937.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000043937.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000043937.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000043937.1}
RP IDENTIFICATION.
RG Ensembl;
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; CABD030114056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2Z9U1; -.
DR Ensembl; ENSGGOT00000064242.1; ENSGGOP00000043937.1; ENSGGOG00000008792.3.
DR GeneTree; ENSGT00940000159485; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000008792; Expressed in testis and 5 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: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:UP000001519};
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 303..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 36608 MW; DD79D2673EDD4FC9 CRC64;
MYSTTYEERN ITGTRVKVPV GQEVEGMNIL GLVVFAIVFG VALRKLGPEG ELLIRFFNSF
NEATMVLVSW IMWYAPVGIM FLVAGKIVEM EDVGLLFARL GKYILCCLLG HAIHGLLVLP
LIYFLFTRKN PYRFLWGIVT PLATAFGTSS SSATLPLMMK CVEENNGVAK HISRFILPIG
ATVNMDGAAL FQCVAAVFIA QLSQQSLDFV KIITILVTAT ASSVGAAGIP AGGVLTLAII
LEAVNLPVDH ISLILAVDWL VDRSCTVLNV EGDALGAGLL QNYVDRTESR STEPELIQVK
SELPLDPLPV PTEEGNPLLK HYRGPAGDAT AASEKESVM
//
