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S38A1_PONAB
ID   S38A1_PONAB             Reviewed;         487 AA.
AC   Q5R443;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 1;
DE   AltName: Full=Amino acid transporter A1;
DE   AltName: Full=N-system amino acid transporter 2;
DE   AltName: Full=Solute carrier family 38 member 1;
DE   AltName: Full=System A amino acid transporter 1;
DE   AltName: Full=System N amino acid transporter 1;
GN   Name=SLC38A1; Synonyms=SNAT1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
CC       Mediates the saturable, pH-sensitive and electrogenic cotransport of
CC       glutamine and sodium ions with a stoichiometry of 1:1. May also
CC       transport small zwitterionic and aliphatic amino acids with a lower
CC       affinity. May supply glutamatergic and GABAergic neurons with glutamine
CC       which is required for the synthesis of the neurotransmitters glutamate
CC       and GABA (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Inhibited by lithium, potassium, choline ions, N-
CC       methyl-D-glucamine and 2-methylamino-isobutyric acid (MeAIB).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Restricted to the somatodendritic
CC       compartment of neurons. Found in the cellular processes of neurons in
CC       the developing brain. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
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DR   EMBL; CR861417; CAH93473.1; -; mRNA.
DR   RefSeq; NP_001127036.1; NM_001133564.1.
DR   AlphaFoldDB; Q5R443; -.
DR   SMR; Q5R443; -.
DR   STRING; 9601.ENSPPYP00000005062; -.
DR   GeneID; 100174062; -.
DR   KEGG; pon:100174062; -.
DR   CTD; 81539; -.
DR   eggNOG; KOG1305; Eukaryota.
DR   InParanoid; Q5R443; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   2: Evidence at transcript 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..487
FT                   /note="Sodium-coupled neutral amino acid transporter 1"
FT                   /id="PRO_0000310477"
FT   TOPO_DOM        1..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..350
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..416
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        438..452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        453..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        474..487
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2P7"
FT   MOD_RES         11
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2P7"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   MOD_RES         54
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2H9"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        245..264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   487 AA;  53923 MW;  ADE2330886511406 CRC64;
     MMHFKSGLEL TELQNMTVPE DDNISNDSND FTEVENGQIN SKFISDRESR RSLTNSHLEK
     KKCDEYIPGT TSLGMSVFNL SNAIMGSGIL GLAFALANTG ILLFLVLLTS VTLLSIYSIN
     LLLICSKETG CMVYEKLGEQ VFGTTGKFVI FGATSLQNTG AMLSYLFIVK NELPSAIKFL
     MGKEETFSAW YVDGRVLVVI VTFGIILPLC LLKNLGYLGY TSGFSLSCMV FFLIVVIYKK
     FQIPCIVPEL NSTISANSTN ADTCTPKYVT LNSKTVYALP TIAFAFVCHP SVLPIYSELK
     DRSQKKMQMV SNISFFAMFV MYFLTAIFGY LTFYDNVQSD LLHKYQGKDD ILILTVRLAV
     IVAVILTVPV LFFTVRSSLF ELAKKTKFNL CRHTVVTCIL LVVINLLVIS IPSMKDIFGV
     VGVTSANMLI FILPSSLYLK ITDQDGDKGT QRIWAALFLG LGVLFSLVSI PLVIYDWACS
     SSSDEGH
 
 
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