AAAT_MOUSE
ID AAAT_MOUSE Reviewed; 553 AA.
AC P51912; Q61326;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neutral amino acid transporter B(0);
DE Short=ATB(0);
DE AltName: Full=ASC-like Na(+)-dependent neutral amino acid transporter ASCT2;
DE AltName: Full=Insulin-activated amino acid transporter {ECO:0000303|PubMed:7702599};
DE AltName: Full=Sodium-dependent neutral amino acid transporter type 2;
DE AltName: Full=Solute carrier family 1 member 5;
GN Name=Slc1a5; Synonyms=Aaat, Asct2, Slc1a7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Adipose tissue;
RX PubMed=7702599; DOI=10.1006/bbrc.1995.1434;
RA Liao K., Lane M.D.;
RT "Expression of a novel insulin-activated amino acid transporter gene during
RT differentiation of 3T3-L1 preadipocytes into adipocytes.";
RL Biochem. Biophys. Res. Commun. 208:1008-1015(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=JCL:ICR; TISSUE=Testis;
RX PubMed=8662767; DOI=10.1074/jbc.271.25.14883;
RA Utsunomiya-Tate N., Endou H., Kanai Y.;
RT "Cloning and functional characterization of a system ASC-like Na+-dependent
RT neutral amino acid transporter.";
RL J. Biol. Chem. 271:14883-14890(1996).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506 AND SER-518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-518 AND SER-543, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:7702599, ECO:0000269|PubMed:8662767}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q15758}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7702599,
CC ECO:0000269|PubMed:8662767}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q15758}. Melanosome
CC {ECO:0000250|UniProtKB:Q15758}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adipose tissue, lower levels
CC seen in lung. Not expressed in brain, kidney, liver or heart and only
CC traces are detected in spleen, thymus and skeletal muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed is induced during differentiation of
CC preadipocytes into adipocytes.
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; L42115; AAA66264.1; -; mRNA.
DR EMBL; D85044; BAA12716.1; -; mRNA.
DR PIR; JC4149; JC4149.
DR AlphaFoldDB; P51912; -.
DR SMR; P51912; -.
DR IntAct; P51912; 1.
DR STRING; 10090.ENSMUSP00000104136; -.
DR TCDB; 2.A.23.3.2; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR GlyGen; P51912; 2 sites.
DR iPTMnet; P51912; -.
DR PhosphoSitePlus; P51912; -.
DR SwissPalm; P51912; -.
DR EPD; P51912; -.
DR jPOST; P51912; -.
DR MaxQB; P51912; -.
DR PaxDb; P51912; -.
DR PeptideAtlas; P51912; -.
DR PRIDE; P51912; -.
DR ProteomicsDB; 286038; -.
DR MGI; MGI:105305; Slc1a5.
DR eggNOG; KOG3787; Eukaryota.
DR InParanoid; P51912; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR ChiTaRS; Slc1a5; mouse.
DR PRO; PR:P51912; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P51912; protein.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
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; IDA:ARUK-UCL.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:ARUK-UCL.
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; IDA:MGI.
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; IDA:ARUK-UCL.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0150104; P:transport across blood-brain barrier; IDA:ARUK-UCL.
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 1: Evidence at protein 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..553
FT /note="Neutral amino acid transporter B(0)"
FT /id="PRO_0000202083"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 81..93
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 116..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 153..236
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 261..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 298..318
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..340
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 341..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 346..376
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 377..385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..412
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 413..425
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 426..459
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 460..472
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..494
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 495..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 531..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 396
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT BINDING 398
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 483
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O59010"
FT BINDING 487
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 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15758"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 13..21
FT /note="VAVDSSRRC -> SSGGFHRNGG (in Ref. 1; AAA66264)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..154
FT /note="LLFFLVTTLLASALGVGLALALKP -> ALFPGHHTARVGARRGFGPGAEA
FT (in Ref. 1; AAA66264)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> V (in Ref. 1; AAA66264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 58483 MW; D25EBC982FBDE158 CRC64;
MAVDPPKADP KGVAVDSSRR CPALGSREDQ SAKAGGCCGS RDRVRRCIRA NLLVLLTVAA
VVAGVGLGLG VSAAGGADAL GPARLTRFAF PGELLLRLLK MIILPLVVCS LIGGAASLDP
SALGRVGAWA LLFFLVTTLL ASALGVGLAL ALKPGAAVTA ITSINDSVVD PCARSAPTKE
ALDSFLDLVR NIFPSNLVSA AFRSFATSYE PKDNSCKIPQ SCIQREINST MVQLLCEVEG
MNILGLVVFA IVFGVALRKL GPEGELLIRF FNSFNDATMV LVSWIMWYAP VGILFLVASK
IVEMKDVRQL FISLGKYILC CLLGHAIHGL LVLPLIYFLF TRKNPYRFLW GIMTPLATAF
GTSSSSATLP LMMKCVEEKN GVAKHISRFI LPIGATVNMD GAALFQCVAA VFIAQLNGVS
LDFVKIITIL VTATASSVGA AGIPAGGVLT LAIILEAVSL PVKDISLILA VDWLVDRSCT
VLNVEGDAFG AGLLQSYVDR TKMPSSEPEL IQVKNEVSLN PLPLATEEGN PLLKQYQGPT
GDSSATFEKE SVM
