S38A4_RAT
ID S38A4_RAT Reviewed; 547 AA.
AC Q9EQ25;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 4;
DE AltName: Full=Amino acid transporter A3;
DE AltName: Full=Na(+)-coupled neutral amino acid transporter 4;
DE AltName: Full=Solute carrier family 38 member 4;
DE AltName: Full=System A amino acid transporter 3;
GN Name=Slc38a4; Synonyms=Ata3, Snat4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=11118514; DOI=10.1016/s0005-2736(00)00349-7;
RA Sugawara M., Nakanishi T., Fei Y.-J., Martindale R.G., Ganapathy M.E.,
RA Leibach F.H., Ganapathy V.;
RT "Structure and function of ATA3, a new subtype of amino acid transport
RT system A, primarily expressed in the liver and skeletal muscle.";
RL Biochim. Biophys. Acta 1509:7-13(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sodium-dependent amino acid transporter. Mediates
CC electrogenic symport of neutral amino acids and sodium ions. Has a
CC broad specificity, with a preference for Ala, followed by Ser, Gly,
CC Cys, Asn, Thr, Pro and Met. May mediate sodium-independent transport of
CC cationic amino acids, such as Arg and Lys. Amino acid uptake is pH-
CC dependent, with lower transport activities at pH 6.5, intermediate at
CC pH 7.0 and highest between pH 7.5 and 8.5.
CC {ECO:0000269|PubMed:11118514}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver, and at lower
CC level in skeletal muscle. {ECO:0000269|PubMed:11118514}.
CC -!- PTM: The disulfide bond plays an important role in substrate transport,
CC but has no effect on trafficking to the cell surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF295535; AAG45335.1; -; mRNA.
DR EMBL; BC097292; AAH97292.1; -; mRNA.
DR RefSeq; NP_570104.1; NM_130748.1.
DR RefSeq; XP_008763885.1; XM_008765663.2.
DR AlphaFoldDB; Q9EQ25; -.
DR SMR; Q9EQ25; -.
DR STRING; 10116.ENSRNOP00000009187; -.
DR TCDB; 2.A.18.6.7; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q9EQ25; 3 sites.
DR iPTMnet; Q9EQ25; -.
DR PhosphoSitePlus; Q9EQ25; -.
DR jPOST; Q9EQ25; -.
DR PaxDb; Q9EQ25; -.
DR PRIDE; Q9EQ25; -.
DR Ensembl; ENSRNOT00000009187; ENSRNOP00000009187; ENSRNOG00000006653.
DR GeneID; 170573; -.
DR KEGG; rno:170573; -.
DR UCSC; RGD:621836; rat.
DR CTD; 55089; -.
DR RGD; 621836; Slc38a4.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000158917; -.
DR InParanoid; Q9EQ25; -.
DR OMA; IRTFMGL; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q9EQ25; -.
DR TreeFam; TF328787; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:Q9EQ25; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006653; Expressed in liver and 18 other tissues.
DR Genevisible; Q9EQ25; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 2.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="Sodium-coupled neutral amino acid transporter 4"
FT /id="PRO_0000247863"
FT TOPO_DOM 1..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..476
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 60613 MW; 28BFF2C0F2B74BF0 CRC64;
MDPIELRSVN IEPYEDSCSV DSIQSCYTGM GNSEKGAMDS QFANEDAESQ KFLTNGFLGK
KTLTDYADEH HPGTTSFGMS SFNLSNAIMG SGILGLSYAM ANTGIVLFVI MLLTVAILSL
YSVHLLLKTA KEGGSLIYEK LGEKAFGWPG KIGAFISITM QNIGAMSSYL FIIKYELPEV
IRVFMGLEEN TGEWYLNGNY LVLFVSVGII LPLSLLKNLG YLGYTSGFSL TCMVFFVSVV
IYKKFQIPCP LPVLDHNNGN LTFNNTLPMH VIMLPNNSES TGMNFMVDYT HRDPEGLDEK
PAAGPLHGSG VEYEAHSGDK CQPKYFVFNS RTAYAIPILA FAFVCHPEVL PIYSELKDRS
RRKMQTVSNI SITGMLVMYL LAALFGYLSF YGEVEDELLH AYSKVYTFDT ALLMVRLAVL
VAVTLTVPIV LFPIRTSVIT LLFPRRPFSW VKHFGIAAII IALNNVLVIL VPTIKYIFGF
IGASSATMLI FILPAAFYLK LVKKEPLRSP QKIGALVFLV TGIIFMMGSM ALIIIDWIYN
PPNPDHH
