S38A3_RAT
ID S38A3_RAT Reviewed; 504 AA.
AC Q9JHZ9; Q66HS0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 3;
DE AltName: Full=N-system amino acid transporter 1;
DE AltName: Full=Na(+)-coupled neutral amino acid transporter 3;
DE AltName: Full=Solute carrier family 38 member 3;
DE AltName: Full=System N amino acid transporter 1;
GN Name=Slc38a3 {ECO:0000312|RGD:628620}; Synonyms=Snat3;
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] {ECO:0000305, ECO:0000312|EMBL:AAF81797.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:10619430};
RX PubMed=10619430; DOI=10.1016/s0092-8674(00)81674-8;
RA Chaudhry F.A., Reimer R.J., Krizaj D., Barber D., Storm-Mathisen J.,
RA Copenhagen D.R., Edwards R.H.;
RT "Molecular analysis of system N suggests novel physiological roles in
RT nitrogen metabolism and synaptic transmission.";
RL Cell 99:769-780(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle {ECO:0000269|PubMed:10823827};
RX PubMed=10823827; DOI=10.1074/jbc.m002282200;
RA Fei Y.-J., Sugawara M., Nakanishi T., Huang W., Wang H., Prasad P.D.,
RA Leibach F.H., Ganapathy V.;
RT "Primary structure, genomic organization, and functional and electrogenic
RT characteristics of human system N 1, a Na+- and H+-coupled glutamine
RT transporter.";
RL J. Biol. Chem. 275:23707-23717(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Sodium-dependent amino acid/proton antiporter. Mediates
CC electrogenic cotransport of glutamine and sodium ions in exchange for
CC protons. Also recognizes histidine and asparagine. May mediate amino
CC acid transport in either direction under physiological conditions. May
CC play a role in nitrogen metabolism and synaptic transmission.
CC {ECO:0000269|PubMed:10619430, ECO:0000269|PubMed:10823827,
CC ECO:0000303|PubMed:10619430}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10619430};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10619430}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, liver, kidney, heart
CC and brain. Not detected in gut, lung or spleen. Expressed ubiquitously
CC in hepatocytes in liver whereas in kidney expression is restricted to
CC the medulla. Within brain, expressed in glial cells. In the cerebellum,
CC expressed on Bergmann glial fibers in the molecular layer and
CC astrocytes in the granule layer. {ECO:0000269|PubMed:10619430,
CC ECO:0000269|PubMed:10823827}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF273025; AAF81797.1; -; mRNA.
DR EMBL; BC081717; AAH81717.1; -; mRNA.
DR RefSeq; NP_665719.1; NM_145776.1.
DR AlphaFoldDB; Q9JHZ9; -.
DR SMR; Q9JHZ9; -.
DR BioGRID; 251668; 1.
DR STRING; 10116.ENSRNOP00000023623; -.
DR GlyGen; Q9JHZ9; 4 sites.
DR iPTMnet; Q9JHZ9; -.
DR PhosphoSitePlus; Q9JHZ9; -.
DR PaxDb; Q9JHZ9; -.
DR PRIDE; Q9JHZ9; -.
DR Ensembl; ENSRNOT00000023623; ENSRNOP00000023623; ENSRNOG00000016827.
DR GeneID; 252919; -.
DR KEGG; rno:252919; -.
DR UCSC; RGD:628620; rat.
DR CTD; 10991; -.
DR RGD; 628620; Slc38a3.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000157127; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q9JHZ9; -.
DR OMA; CWGVAVM; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q9JHZ9; -.
DR TreeFam; TF328787; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:Q9JHZ9; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000016827; Expressed in liver and 18 other tissues.
DR Genevisible; Q9JHZ9; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:UniProtKB.
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:0006867; P:asparagine transport; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006868; P:glutamine transport; IDA:UniProtKB.
DR GO; GO:0015817; P:histidine transport; IDA:UniProtKB.
DR GO; GO:0015808; P:L-alanine transport; ISO:RGD.
DR GO; GO:2000487; P:positive regulation of glutamine transport; IDA:RGD.
DR GO; GO:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; ISO:RGD.
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; Antiport; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="Sodium-coupled neutral amino acid transporter 3"
FT /id="PRO_0000093830"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 239..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 504 AA; 55637 MW; D8C19AED34A791DD CRC64;
MEIPRQTEMV ELVPNGKHLE GLLPVGMPTA DTQRAEDAQH CGEGKGFLQQ SSSKEPHFTD
FEGKTSFGMS VFNLSNAIMG SGILGLAYAM ANTGIILFLF LLTAVALLSS YSIHLLLKSS
GIVGIRAYEQ LGYRAFGTPG KLAAALAITL QNIGAMSSYL YIIKSELPLV IQTFLNLEKP
TPVWYMDGNY LVILVSVIII LPLALMRQLG YLGYSSGFSL SCMVFFLIAV IYKKFQVPCP
LAHNLVNATG NFSHMVVVEE KSQLQSEPDT AEAFCTPSYF TLNSQTAYTI PIMAFAFVCH
PEVLPIYTEL KDPSKRKMQH ISNLSIAVMY VMYFLAALFG YLTFYDGVES ELLHTYSKVD
PFDVLILCVR VAVLIAVTLT VPIVLFPVRR AIQQMLFQNQ EFSWLRHVLI ATGLLTCINL
LVIFAPNILG IFGIIGATSA PCLIFIFPAI FYFRIMPTEK EPVRSTPKIL ALCFAAVGFL
LMTMSLSFII TDWVSGTSQH GGNH
