ID   SATT_MOUSE              Reviewed;         532 AA.
AC   O35874;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Neutral amino acid transporter A;
DE   AltName: Full=Alanine/serine/cysteine/threonine transporter 1;
DE            Short=ASCT-1;
DE   AltName: Full=Solute carrier family 1 member 4;
GN   Name=Slc1a4; Synonyms=Asct1, Satt;
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].
RA   Peng J.-B., Guo L.-H.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201 AND ASN-206.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201 AND ASN-206.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-530, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, and Pancreas;
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 neutral amino-acid transporter that mediates
CC       transport of alanine, serine, cysteine, proline, hydroxyproline and
CC       threonine. {ECO:0000250|UniProtKB:P43007}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC         Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC         Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC         Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC         Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-L-proline(in) + Na(+)(in) = 4-hydroxy-L-proline(out)
CC         + Na(+)(out); Xref=Rhea:RHEA:70023, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:58419; Evidence={ECO:0000250|UniProtKB:P43007};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43007}; Multi-
CC       pass membrane protein {ECO:0000255}. Melanosome
CC       {ECO:0000250|UniProtKB:P43007}. Note=Identified by mass spectrometry in
CC       melanosome fractions from stage I to stage IV.
CC       {ECO:0000250|UniProtKB:P43007}.
CC   -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC       (DAACS) (TC 2.A.23) family. SLC1A4 subfamily. {ECO:0000305}.
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DR   EMBL; U75215; AAB71740.1; -; mRNA.
DR   EMBL; BC052733; AAH52733.1; -; mRNA.
DR   CCDS; CCDS24457.1; -.
DR   RefSeq; NP_061349.3; NM_018861.3.
DR   AlphaFoldDB; O35874; -.
DR   SMR; O35874; -.
DR   BioGRID; 207749; 5.
DR   IntAct; O35874; 1.
DR   MINT; O35874; -.
DR   STRING; 10090.ENSMUSP00000105223; -.
DR   GlyCosmos; O35874; 2 sites, No reported glycans.
DR   GlyGen; O35874; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; O35874; -.
DR   PhosphoSitePlus; O35874; -.
DR   SwissPalm; O35874; -.
DR   EPD; O35874; -.
DR   PaxDb; 10090-ENSMUSP00000105223; -.
DR   PeptideAtlas; O35874; -.
DR   ProteomicsDB; 256922; -.
DR   Pumba; O35874; -.
DR   Antibodypedia; 30840; 287 antibodies from 33 providers.
DR   DNASU; 55963; -.
DR   Ensembl; ENSMUST00000109594.8; ENSMUSP00000105223.2; ENSMUSG00000020142.13.
DR   GeneID; 55963; -.
DR   KEGG; mmu:55963; -.
DR   UCSC; uc007idb.2; mouse.
DR   AGR; MGI:2135601; -.
DR   CTD; 6509; -.
DR   MGI; MGI:2135601; Slc1a4.
DR   VEuPathDB; HostDB:ENSMUSG00000020142; -.
DR   eggNOG; KOG3787; Eukaryota.
DR   GeneTree; ENSGT00940000157081; -.
DR   HOGENOM; CLU_019375_3_3_1; -.
DR   InParanoid; O35874; -.
DR   OMA; GIMFVVH; -.
DR   OrthoDB; 49426at2759; -.
DR   PhylomeDB; O35874; -.
DR   TreeFam; TF315206; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 55963; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Slc1a4; mouse.
DR   PRO; PR:O35874; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O35874; Protein.
DR   Bgee; ENSMUSG00000020142; Expressed in supraoptic nucleus and 252 other cell types or tissues.
DR   ExpressionAtlas; O35874; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR   GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015184; F:L-cystine transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0034590; F:L-hydroxyproline transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015193; F:L-proline transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015195; F:L-threonine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; ISO:MGI.
DR   GO; GO:0034589; P:hydroxyproline transport; ISO:MGI.
DR   GO; GO:1904273; P:L-alanine import across plasma membrane; ISO:MGI.
DR   GO; GO:0015808; P:L-alanine transport; ISO:MGI.
DR   GO; GO:0140009; P:L-aspartate import across plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central.
DR   GO; GO:1903812; P:L-serine import across plasma membrane; ISO:MGI.
DR   GO; GO:0015825; P:L-serine transport; ISO:MGI.
DR   GO; GO:0015824; P:proline transport; ISO:MGI.
DR   GO; GO:0098718; P:serine import across plasma membrane; IDA:MGI.
DR   GO; GO:0015826; P:threonine transport; ISO:MGI.
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:SF20; NEUTRAL AMINO ACID TRANSPORTER A; 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.
DR   Genevisible; O35874; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..532
FT                   /note="Neutral amino acid transporter A"
FT                   /id="PRO_0000202080"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P43007"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43007"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
SQ   SEQUENCE   532 AA;  56062 MW;  99DD9E43C5DB55D7 CRC64;
     MEKSGETNGY LDGTQAEPAA GPRTPETAMG KSQRCASFFR RHALVLLTVS GVLVGAGMGA
     ALRGLQLTRT QITYLAFPGE MLLRMLRMII LPLVVCSLVS GAASLDASSL GRLGGIAVAY
     FGLTTLSASA LAVALAFIIK PGAGAQTLQS SSLGLENSGP PPVSKETVDS FLDLLRNLFP
     SNLVVAAFTT SATDYTVVTH NTSSGNVTKE KIPVVTDVEG MNILGLVLFA LVLGVALKKL
     GPEGEDLIRF FNSFNEATMV LVSWIMWYVP IGIMFLIGSK IVEMKDIVML VTSLGKYIFA
     SMLGHVIHGG IVLPLVYFAF TRKNPFTFLL GLLTPFATAF ATCSSSATLP SMMKCIEENN
     GVDKRISRFI LPIGATVNMD GAAIFQCVAA VFIAQLNNVD LNAGQIFTIL VTATASSVGA
     AGVPAGGVLT IAIILEAIGL PTHDLSLILA VDWIVDRTTT VVNVEGDALG AGILNHLNQK
     VVKKGEQELQ EVKVEAIPNS KSEEETSPLV THQNPAGPVA IAPELESKES VL
//