AAAT_RABIT
ID AAAT_RABIT Reviewed; 541 AA.
AC O19105;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Neutral amino acid transporter B(0) {ECO:0000303|PubMed:9227483};
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Intestine;
RX PubMed=9227483; DOI=10.1152/ajpgi.1997.272.6.g1463;
RA Kekuda R., Torres-Zamorano V., Fei Y.-J., Prasad P.D., Li H.W., Mader L.D.,
RA Leibach F.H., Ganapathy V.;
RT "Molecular and functional characterization of intestinal Na(+)-dependent
RT neutral amino acid transporter B0.";
RL Am. J. Physiol. 272:G1463-G1472(1997).
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:9227483}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15758}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9227483};
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}.
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DR EMBL; U75284; AAB66298.1; -; mRNA.
DR RefSeq; NP_001075847.1; NM_001082378.1.
DR AlphaFoldDB; O19105; -.
DR SMR; O19105; -.
DR PRIDE; O19105; -.
DR GeneID; 100009234; -.
DR KEGG; ocu:100009234; -.
DR CTD; 6510; -.
DR InParanoid; O19105; -.
DR OrthoDB; 1184392at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0015172; F:acidic amino acid transmembrane transporter activity; IEA:UniProt.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006835; P:dicarboxylic acid transport; IEA:UniProt.
DR GO; GO:0006868; P:glutamine transport; ISS:UniProtKB.
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..541
FT /note="Neutral amino acid transporter B(0)"
FT /id="PRO_0000202084"
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..225
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 226..249
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 250..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..286
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 287..307
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..329
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 330..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 335..365
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 366..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..401
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 402..414
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 415..448
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 449..461
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 462..483
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 484..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 385
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 387
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 472
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 476
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 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51912"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 541 AA; 56658 MW; 039FAD095091AD15 CRC64;
MVADPPKGDP KGLAAVEPTA NGAPAQDPLE DSGAAVGRCC SSRDQVRRCL RANLLVLLTV
VAVVAGVALG LAVSGAGGAL ALGPARLIAF AFPGELLLRL LKMIILPLVV CSLVGGAASL
DPSALGRLGA WALLFFLVTT LLASALGVGL ALALQPGAAF AAMNASLSST GAVEQTPSKQ
VLDSFLDLLR NIFPSNLVSA AFRSYSTSYE EKNFNGTLVK VPVAHEEEGM NILGLVVFAI
VFGVALRKLG PEGEPLIRFF NSFNDATMVL VSWIMWYAPV GILFLVASKI VEMDDVGVLF
ASLGKYILCC LLGHAIHGLL VLPLIYFLFT RKNPYRFLWG ILTPLAMAFG TSSSSATLPL
MMKCVEERNG VAKHISRFVL PIGATVNMDG AALFQCVAAV FIAQLNRQSL DFVKIITILV
TATASSVGAA GIPAGGVLTL AIILEAVSLP VSEISLILAV DWLVDRSCTI INVEGDAFGA
GLLQHYVDRT EQRGSEPELT QVKSEVPLGS LPAPNEEGNP LLRHSPGAAG DAGACEKESV
M
