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Database: UniProt
Entry: A0A1A6HCD9_NEOLE
LinkDB: A0A1A6HCD9_NEOLE
Original site: A0A1A6HCD9_NEOLE 
ID   A0A1A6HCD9_NEOLE        Unreviewed;       561 AA.
AC   A0A1A6HCD9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
DE   Flags: Fragment;
GN   ORFNames=A6R68_17312 {ECO:0000313|EMBL:OBS76238.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS76238.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS76238.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS76238.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS76238.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBS76238.1}.
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DR   EMBL; LZPO01034952; OBS76238.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6HCD9; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015172; F:acidic amino acid transmembrane transporter activity; IEA:UniProt.
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   GO; GO:0006835; P:dicarboxylic acid 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   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:UP000092124};
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..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        130..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        249..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        326..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        355..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        398..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   TRANSMEM        435..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361216"
FT   REGION          534..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         561
FT                   /evidence="ECO:0000313|EMBL:OBS76238.1"
SQ   SEQUENCE   561 AA;  59135 MW;  5FB06E640C88B4C6 CRC64;
     MAVDPPKTDP KXVVAVNPTA NGGPALDSRE DQGAKAGGCC GSWDQVRRCL RANLLVLFTV
     AAVVAGVVIG LGVSSAGGAE ALGPARLTAF AFPGELLLRL LKMIILPLVV CSLIGGAASL
     DPSALGRVGA WALLFFLVTT LLASALGVGL ALALKPGAAF TAINGSVGDT CVDNAPTKEV
     LDSFLDLARN IFPSNLVSAA FRSVSLLGYA KGLGVRWGWA EKRKMQQPAT CTTRVINGTM
     VQLGCEVEGM NILGLVVFAI VFGVALRKLG PDGELLIRFF NSFNDATMVL VSWIMWYAPV
     GILFLVASKI VEMKDVRQLF ISLGKYILCC LLGHAIHGLL VLPLIYFIFT RRNPYRFLWG
     IMTPLATAFG TSSSSATLPL MMKCVEEKNG VAKHISRFIL PIGATVNMDG AALFQCVAAV
     FIAQLNGVSL DFVKIITILV TATASSVGAA GIPAGGVLTL AIILEAISLP VKDISLILAV
     DWLVDRSCTI LNVEGDAFGA GLLQSYVDRT KMPPSSEPEL IQVKNDVPLN PLPLTTEEGN
     PLLKQYRGPA GDAATCEKES V
//
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