ID A0A1V4K5C1_PATFA Unreviewed; 527 AA.
AC A0A1V4K5C1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=SLC1A1 {ECO:0000313|EMBL:OPJ79594.1};
GN ORFNames=AV530_004098 {ECO:0000313|EMBL:OPJ79594.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ79594.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ79594.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ79594.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ79594.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-
CC aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29990;
CC Evidence={ECO:0000256|ARBA:ARBA00036068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000256|ARBA:ARBA00037017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000256|ARBA:ARBA00036463};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004146}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004414}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361216}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004565}. Synapse, synaptosome
CC {ECO:0000256|ARBA:ARBA00034102}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A1 subfamily.
CC {ECO:0000256|ARBA:ARBA00037996}.
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:OPJ79594.1}.
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DR EMBL; LSYS01004381; OPJ79594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4K5C1; -.
DR STRING; 372326.A0A1V4K5C1; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015813; P:L-glutamate 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:SF110; EXCITATORY AMINO ACID TRANSPORTER 3; 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 Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
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 Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Symport {ECO:0000256|ARBA:ARBA00022847, ECO:0000256|RuleBase:RU361216};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599};
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 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 58..82
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
SQ SEQUENCE 527 AA; 57204 MW; A3D8906418482729 CRC64;
MAKAGRKGCS CPVFLKKNCL LLSTVAAVLL GIGVGVLVRE YAKLSNLDKF YFSFPGEVLM
RMLKLIILPL IISSMITGVA ALDSSISGKI GLRAVVYYFC TTVIAVILGI VLVVTIKPGV
TQTTNDIYRV GSTPDVSTVD ALLDLIRNMF PENLVQACFQ QYKTKREKVE AETSVDKNSS
TFAEEPVTTA TTFKASENKT QEYKVVGSYS DGINVLGLIV FCLVFGMVIG KMGEKGQVLV
DFFNALNEAT MRIVHIIMWY MPIGIVFLIA GKIIEVEDWE IFRKLGLYMA TVISGLAIHS
VIILPLIYLI IVRKNPFRFA MGMAQALLTA LMISSSSATL PVTFRCAEEK NLIDKRITRF
VLPVGATINM DGTALYEAVA AVFIAQLNDL QLDVGKIVTI SVTATAASIG AAGVPQAGLV
TMVIVLTAVG LPAEDVTLII AVDWLLDRFR TMVNVLGDAF GTGIVEKLSK KELEQMDVNS
EVNIVNPFAL ETAVLENDEA ETKKSYVNGG FAVDKSDTIS FTQTSQF
//
