SATT_MOUSE
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 03-AUG-2022, entry version 156.
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; 3.
DR IntAct; O35874; 1.
DR MINT; O35874; -.
DR STRING; 10090.ENSMUSP00000105223; -.
DR GlyGen; O35874; 2 sites.
DR iPTMnet; O35874; -.
DR PhosphoSitePlus; O35874; -.
DR SwissPalm; O35874; -.
DR EPD; O35874; -.
DR PaxDb; O35874; -.
DR PeptideAtlas; O35874; -.
DR PRIDE; O35874; -.
DR ProteomicsDB; 256922; -.
DR Antibodypedia; 30840; 256 antibodies from 33 providers.
DR DNASU; 55963; -.
DR Ensembl; ENSMUST00000109594; ENSMUSP00000105223; ENSMUSG00000020142.
DR GeneID; 55963; -.
DR KEGG; mmu:55963; -.
DR UCSC; uc007idb.2; mouse.
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; ICSFVVP; -.
DR OrthoDB; 1184392at2759; -.
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 75 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 249 other tissues.
DR ExpressionAtlas; O35874; baseline and differential.
DR Genevisible; O35874; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; -; 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; 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
