AAAT_BOVIN
ID AAAT_BOVIN Reviewed; 539 AA.
AC Q95JC7; Q08DD9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Neutral amino acid transporter B(0);
DE Short=ATB(0);
DE AltName: Full=Sodium-dependent neutral amino acid transporter type 2;
DE AltName: Full=Solute carrier family 1 member 5;
GN Name=SLC1A5; Synonyms=ASCT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=11997120; DOI=10.1016/s0005-2736(02)00346-2;
RA Pollard M., Meredith D., McGivan J.D.;
RT "Characterisation and cloning of a Na(+)-dependent broad-specificity
RT neutral amino acid transporter from NBL-1 cells: a novel member of the
RT ASC/B(0) transporter family.";
RL Biochim. Biophys. Acta 1561:202-208(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sodium-dependent amino acids transporter that has a broad
CC substrate specificity, with a preference for zwitterionic amino acids.
CC It accepts as substrates all neutral amino acids, including glutamine,
CC asparagine, and branched-chain and aromatic amino acids, and excludes
CC methylated, anionic, and cationic amino acids.
CC {ECO:0000269|PubMed:11997120}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15758}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11997120};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome
CC {ECO:0000250|UniProtKB:Q15758}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A5 subfamily. {ECO:0000305}.
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 EMBL; AY039236; AAK83490.1; -; mRNA.
DR EMBL; BC123803; AAI23804.1; -; mRNA.
DR RefSeq; NP_777026.1; NM_174601.2.
DR AlphaFoldDB; Q95JC7; -.
DR SMR; Q95JC7; -.
DR STRING; 9913.ENSBTAP00000018050; -.
DR PaxDb; Q95JC7; -.
DR PeptideAtlas; Q95JC7; -.
DR PRIDE; Q95JC7; -.
DR Ensembl; ENSBTAT00000018050; ENSBTAP00000018050; ENSBTAG00000013577.
DR Ensembl; ENSBTAT00000079696; ENSBTAP00000064727; ENSBTAG00000013577.
DR GeneID; 282355; -.
DR KEGG; bta:282355; -.
DR CTD; 6510; -.
DR VEuPathDB; HostDB:ENSBTAG00000013577; -.
DR VGNC; VGNC:34715; SLC1A5.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000159485; -.
DR InParanoid; Q95JC7; -.
DR OMA; QATNTPM; -.
DR OrthoDB; 1184392at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013577; Expressed in caput epididymis and 104 other tissues.
DR ExpressionAtlas; Q95JC7; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006868; P:glutamine transport; ISS:UniProtKB.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 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; Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..539
FT /note="Neutral amino acid transporter B(0)"
FT /id="PRO_0000202081"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 83..95
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 118..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 155..223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..247
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 248..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 257..284
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 285..305
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..327
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 328..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 333..363
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 364..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..399
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 400..412
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 413..446
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 447..459
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 460..481
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 482..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 518..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 381
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 383
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 385
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 470
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 474
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51912"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 56448 MW; 1C09257A639F51A4 CRC64;
MVADPPKGDP KGYAAAEPTA NGVSMLVPIE DVGSLKGGRC GSGDQVRRCL RANLLVLLTV
VAVVAGVALG LGVSGAGGAF ALGPARLEAF SFPGELLLRL LKMIILPLVV CSLIGGAASL
DPSALGRLGA WALLFFLVTT LLASALGVGL ALALQPGAAF AAINTSVGAP VEEAPSKEVL
DSFLDLVRNI FPSNLVSAAF RSYTTSYKER LFNGTLVKVP TGGEVEGMNI LGLVVFAIIF
GVALRKLGPE GELLIRFFNS FNDATMVLVS WIMWYAPVGI LFLVAGKIVE MENVGLLFAS
LGKYILCCLL GHAIHGLLTL PLIYFLFARK NPYRFLWGIM TPLATAFGTS SSSATLPLMM
KCVEEKNGVA RHISRFILPI GATVNMDGAA LFQCVAAVFI AQLNHRSLDF VKIITILVTA
TASSVGAAGI PSGGVLTLAI ILEAVNLPVH DISLILAVDW LVDRSCTVLN VEGDAFGAGL
LQSYLDRTEN CNSVPELIQV KSEMPLAALP VPGEEGNPLL KGCPGPAGDA DTCEKESVM
