S38A1_RAT
ID S38A1_RAT Reviewed; 485 AA.
AC Q9JM15;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 1;
DE AltName: Full=Amino acid transporter A1;
DE Short=rATA1;
DE AltName: Full=Glutamine transporter;
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 A transporter 2;
DE AltName: Full=System N amino acid transporter 1;
GN Name=Slc38a1; Synonyms=Ata1, Glnt, Sa2, Sat1, Snat1;
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, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Neuron;
RX PubMed=10660562; DOI=10.1074/jbc.275.6.4049;
RA Varoqui H., Zhu H., Yao D., Ming H., Erickson J.D.;
RT "Cloning and functional identification of a neuronal glutamine
RT transporter.";
RL J. Biol. Chem. 275:4049-4054(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 FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11692272; DOI=10.1007/s004240100663;
RA Albers A., Broeer A., Wagner C.A., Setiawan I., Lang P.A., Kranz E.U.,
RA Lang F., Broeer S.;
RT "Na+ transport by the neural glutamine transporter ATA1.";
RL Pflugers Arch. 443:92-101(2001).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11756489; DOI=10.1523/jneurosci.22-01-00062.2002;
RA Chaudhry F.A., Schmitz D., Reimer R.J., Larsson P., Gray A.T., Nicoll R.,
RA Kavanaugh M., Edwards R.H.;
RT "Glutamine uptake by neurons: interaction of protons with system a
RT transporters.";
RL J. Neurosci. 22:62-72(2002).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12855186; DOI=10.1016/s0165-3806(03)00107-x;
RA Weiss M.D., Derazi S., Rossignol C., Varoqui H., Erickson J.D.,
RA Kilberg M.S., Anderson K.J.;
RT "Ontogeny of the neutral amino acid transporter SAT1/ATA1 in rat brain.";
RL Brain Res. Dev. Brain Res. 143:151-159(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12684517; DOI=10.1074/jbc.m212718200;
RA Mackenzie B., Schaefer M.K.-H., Erickson J.D., Hediger M.A., Weihe E.,
RA Varoqui H.;
RT "Functional properties and cellular distribution of the system A glutamine
RT transporter SNAT1 support specialized roles in central neurons.";
RL J. Biol. Chem. 278:23720-23730(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15054072; DOI=10.1093/cercor/bhh018;
RA Melone M., Quagliano F., Barbaresi P., Varoqui H., Erickson J.D., Conti F.;
RT "Localization of the glutamine transporter SNAT1 in rat cerebral cortex and
RT neighboring structures, with a note on its localization in human cortex.";
RL Cereb. Cortex 14:562-574(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16023720; DOI=10.1016/j.placenta.2005.05.002;
RA Novak D., Lehman M., Bernstein H., Beveridge M., Cramer S.;
RT "SNAT expression in rat placenta.";
RL Placenta 27:510-516(2006).
RN [9]
RP INDUCTION BY FORSKOLIN.
RX PubMed=17323379; DOI=10.1002/jcp.21031;
RA Ogura M., Taniura H., Nakamichi N., Yoneda Y.;
RT "Upregulation of the glutamine transporter through transactivation mediated
RT by cAMP/protein kinase A signals toward exacerbation of vulnerability to
RT oxidative stress in rat neocortical astrocytes.";
RL J. Cell. Physiol. 212:375-385(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-54 AND SER-56, AND
RP IDENTIFICATION BY 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: 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. {ECO:0000269|PubMed:10660562, ECO:0000269|PubMed:11692272,
CC ECO:0000269|PubMed:11756489, ECO:0000269|PubMed:12684517}.
CC -!- ACTIVITY REGULATION: Inhibited by lithium, potassium, choline ions, N-
CC methyl-D-glucamine and 2-methylamino-isobutyric acid (MeAIB).
CC {ECO:0000269|PubMed:10660562, ECO:0000269|PubMed:11692272}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=489 uM for L-glutamine (at pH 7.4) {ECO:0000269|PubMed:10660562};
CC KM=582 uM for L-glutamine (at pH 8.2) {ECO:0000269|PubMed:10660562};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10660562,
CC ECO:0000269|PubMed:12684517, ECO:0000269|PubMed:15054072}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10660562,
CC ECO:0000269|PubMed:12684517, ECO:0000269|PubMed:15054072}.
CC Note=Restricted to the somatodendritic compartment of neurons. Found in
CC the cellular processes of neurons in the developing brain.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain with the highest
CC levels in cerebellum and thalamus (at protein level). Expressed in
CC glutamatergic, GABAergic and a subset of dopaminergic neurons of the
CC substantia nigra and cholinergic motoneurons (at protein level). Also
CC expressed by ependymal cells lining the ventricle (at protein level).
CC Expression is also detected in spinal cord, heart, colon and placenta.
CC {ECO:0000269|PubMed:10660562, ECO:0000269|PubMed:11756489,
CC ECO:0000269|PubMed:12684517, ECO:0000269|PubMed:12855186,
CC ECO:0000269|PubMed:15054072, ECO:0000269|PubMed:16023720}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages examined including E17,
CC E19, P2, P10 and P14. Expressed in neocortex, hippocampus and
CC neuroepithelium at E17 and more prominently expressed in striatum,
CC hippocampus and cortex at postnatal days (at protein level).
CC {ECO:0000269|PubMed:12855186}.
CC -!- INDUCTION: Up-regulated by forskolin in astrocytes.
CC {ECO:0000269|PubMed:17323379}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF075704; AAF34240.1; -; mRNA.
DR EMBL; BC097283; AAH97283.1; -; mRNA.
DR RefSeq; NP_620187.1; NM_138832.1.
DR RefSeq; XP_006242339.1; XM_006242277.3.
DR RefSeq; XP_006242340.1; XM_006242278.3.
DR RefSeq; XP_006242341.1; XM_006242279.3.
DR RefSeq; XP_006242342.1; XM_006242280.3.
DR RefSeq; XP_006242343.1; XM_006242281.3.
DR RefSeq; XP_017450126.1; XM_017594637.1.
DR AlphaFoldDB; Q9JM15; -.
DR SMR; Q9JM15; -.
DR STRING; 10116.ENSRNOP00000008138; -.
DR TCDB; 2.A.18.6.1; the amino acid/auxin permease (aaap) family.
DR GlyGen; Q9JM15; 2 sites.
DR iPTMnet; Q9JM15; -.
DR PhosphoSitePlus; Q9JM15; -.
DR PaxDb; Q9JM15; -.
DR PRIDE; Q9JM15; -.
DR ABCD; Q9JM15; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000008138; ENSRNOP00000008138; ENSRNOG00000005291.
DR GeneID; 170567; -.
DR KEGG; rno:170567; -.
DR UCSC; RGD:69645; rat.
DR CTD; 81539; -.
DR RGD; 69645; Slc38a1.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000160716; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q9JM15; -.
DR OMA; LTQRIWA; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q9JM15; -.
DR TreeFam; TF328787; -.
DR Reactome; R-RNO-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:Q9JM15; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005291; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q9JM15; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0098591; C:external side of apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005295; F:neutral amino acid:sodium symporter activity; IDA:ARUK-UCL.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006868; P:glutamine transport; ISO:RGD.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:ARUK-UCL.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
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..485
FT /note="Sodium-coupled neutral amino acid transporter 1"
FT /id="PRO_0000310478"
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..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..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..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..485
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:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 485 AA; 53846 MW; 0CDAD864513FC186 CRC64;
MMHFKSGLEL TELQNMTVPE DDNVSNDSND FTEVENGQIN SKFISDRESR RSLTNSHLEK
RKCDEYIPGT TSLGMSVFNL SNAIMGSGIL GLAFALANTG ILLFLILLTS VTLLSIYSIN
LLLICSKETG CMVYEKLGEQ VFGTTGKLVI FGATSLQNTG AMLSYLFIVK NELPSAIKSL
MGEEETFSAW YVDGRVLVVM VTFGIILPLC LLKNLGYLGY TSGFSLSCMV FFLIVVIYKK
FQIPCMNGEQ NSTVSANVTD ACTPKYVTFN SKTVYALPTI AFAFVCHPSV LPIYSELKDR
SQKKMQMVSN ISFFAMFVMY FLTAIFGYLT FYEKVQSDLL HKYQSTGDIL ILTVRLAVIV
AVILTVPVLF FTVRSSLFEL AKKTKFHLCR HVLVTIILLV IINLLVIFIP SMKDIFGVVG
VTSANMLIFI LPSSLYLKIT NQDGDKNTQR IWAALFLALG VLFSLISIPL VIYDWACSSS
NGEGH
