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