S38A5_RAT
ID S38A5_RAT Reviewed; 479 AA.
AC A2VCW5; Q91XR7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 5;
DE AltName: Full=Solute carrier family 38 member 5;
DE AltName: Full=System N transporter 2;
GN Name=Slc38a5; Synonyms=Sn2, Snat5;
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] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11698233; DOI=10.1152/ajpcell.2001.281.6.c1757;
RA Nakanishi T., Kekuda R., Fei Y.J., Hatanaka T., Sugawara M.,
RA Martindale R.G., Leibach F.H., Prasad P.D., Ganapathy V.;
RT "Cloning and functional characterization of a new subtype of the amino acid
RT transport system N.";
RL Am. J. Physiol. 281:C1757-C1768(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 TOPOLOGY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15390093; DOI=10.1002/glia.20106;
RA Cubelos B., Gonzalez-Gonzalez I.M., Gimenez C., Zafra F.;
RT "Amino acid transporter SNAT5 localizes to glial cells in the rat brain.";
RL Glia 49:230-244(2005).
RN [4]
RP FUNCTION, MUTAGENESIS OF HIS-479, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16629640; DOI=10.1042/bj20060026;
RA Baird F.E., Pinilla-Tenas J.J., Ogilvie W.L.J., Ganapathy V., Hundal H.S.,
RA Taylor P.M.;
RT "Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and
RT System N (SNAT5) amino acid transporter activity involving a conserved
RT histidine residue.";
RL Biochem. J. 397:369-375(2006).
CC -!- FUNCTION: Functions as a sodium-dependent amino acid transporter which
CC countertransport protons. Mediates the saturable, pH-sensitive, and
CC electrogenic cotransport of several neutral amino acids including
CC glycine, asparagine, alanine, serine, glutamine and histidine with
CC sodium. {ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:16629640}.
CC -!- ACTIVITY REGULATION: Not inhibited by lithium. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.92 mM for serine (at pH 8.0) {ECO:0000269|PubMed:16629640};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15390093};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15390093}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2VCW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2VCW5-2; Sequence=VSP_029704;
CC -!- TISSUE SPECIFICITY: Highly expressed in neocortex, hippocampus,
CC striatum and spinal cord by astrocytes (at protein level). Expressed in
CC brain, lung, stomach, liver, kidney, spleen and testis.
CC {ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15390093}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF276870; AAK69075.1; -; mRNA.
DR EMBL; BC128725; AAI28726.1; -; mRNA.
DR RefSeq; NP_620209.1; NM_138854.1. [A2VCW5-2]
DR RefSeq; XP_008771290.1; XM_008773068.2. [A2VCW5-1]
DR AlphaFoldDB; A2VCW5; -.
DR SMR; A2VCW5; -.
DR STRING; 10116.ENSRNOP00000038781; -.
DR TCDB; 2.A.18.6.8; the amino acid/auxin permease (aaap) family.
DR GlyGen; A2VCW5; 1 site.
DR iPTMnet; A2VCW5; -.
DR PhosphoSitePlus; A2VCW5; -.
DR PaxDb; A2VCW5; -.
DR PeptideAtlas; A2VCW5; -.
DR Ensembl; ENSRNOT00000038068; ENSRNOP00000038781; ENSRNOG00000027767. [A2VCW5-1]
DR Ensembl; ENSRNOT00000079664; ENSRNOP00000073818; ENSRNOG00000027767. [A2VCW5-2]
DR GeneID; 192208; -.
DR KEGG; rno:192208; -.
DR UCSC; RGD:620702; rat. [A2VCW5-1]
DR CTD; 92745; -.
DR RGD; 620702; Slc38a5.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000161233; -.
DR InParanoid; A2VCW5; -.
DR PhylomeDB; A2VCW5; -.
DR TreeFam; TF328787; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR SABIO-RK; A2VCW5; -.
DR PRO; PR:A2VCW5; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000027767; Expressed in pancreas and 15 other tissues.
DR ExpressionAtlas; A2VCW5; baseline and differential.
DR Genevisible; A2VCW5; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IDA: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; ISO:RGD.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0022889; F:serine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:1903713; P:asparagine transmembrane transport; ISO:RGD.
DR GO; GO:0006868; P:glutamine transport; IDA:ARUK-UCL.
DR GO; GO:0015816; P:glycine transport; IDA:RGD.
DR GO; GO:1904557; P:L-alanine transmembrane transport; ISO:RGD.
DR GO; GO:0089709; P:L-histidine transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0015825; P:L-serine transport; IDA:ARUK-UCL.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:RGD.
DR GO; GO:0032329; P:serine transport; ISO:RGD.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..479
FT /note="Sodium-coupled neutral amino acid transporter 5"
FT /id="PRO_0000312117"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 231..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11698233"
FT /id="VSP_029704"
FT MUTAGEN 479
FT /note="H->A: Modifies the transporter pH-sensitivity."
FT /evidence="ECO:0000269|PubMed:16629640"
FT CONFLICT 392
FT /note="I -> N (in Ref. 1; AAK69075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52436 MW; DC172C28CB7F5EDC CRC64;
MAISCAVGME MQEPKMNGTL STGAAAGYRQ EREGFLPTTH GPAPGRKPVQ FLDFEGKTSF
GMSVFNLSNA IMGSGILGLA YAMAHTGVIF FLALLLCIAL LSSYSIHLLL TCASVVGIRA
YEQLGQRAFG PAGKVVVAII ICLHNVGAMS SYLFIIKSEL PLVIGTFLHM DPEGDWFLKG
NLLIILVSLL IILPLALMKH LGYLGYTSSL SLTCMLFFLI SVIYKKFQLG CVVSHNDTVV
ESEPAPLQAF NSSCEAKLFT VDSQMSYTVP IMAFAFVCHP EVLPIYTELC CPTQRRMQAV
ANMSIGAMFI MYGLTATFGY LTFYSTVKAE MLEMYTQEDL LILCVRLAVL LAVTLTVPVV
LFPIRRALQQ LLFPSKAFSW PRHVAIALIL LILVNILVIC VPTIRDIFGF IGSTSAPSLI
FILPSVFYLR IVPADMEPLF SWPKIQALCF GVLGVLFMAI SLGFMFANWA TGQSRMSGH
