S38A5_MOUSE
ID S38A5_MOUSE Reviewed; 479 AA.
AC Q3U1J0; Q3TZ39; Q8BJZ6; Q8BW30;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=Jm24, Sn2, Snat5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Inner ear, Ovary, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP INDUCTION.
RX PubMed=17032746; DOI=10.1677/jme.1.02096;
RA Petri A., Ahnfelt-Roenne J., Frederiksen K.S., Edwards D.G., Madsen D.,
RA Serup P., Fleckner J., Heller R.S.;
RT "The effect of neurogenin3 deficiency on pancreatic gene expression in
RT embryonic mice.";
RL J. Mol. Endocrinol. 37:301-316(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Not inhibited by lithium. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U1J0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1J0-2; Sequence=VSP_029703;
CC -!- INDUCTION: Down-regulated in Dgn3 deficient mice.
CC {ECO:0000269|PubMed:17032746}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35799.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK054485; BAC35799.1; ALT_INIT; mRNA.
DR EMBL; AK077667; BAC36941.1; -; mRNA.
DR EMBL; AK155928; BAE33507.1; -; mRNA.
DR EMBL; AK158125; BAE34371.1; -; mRNA.
DR EMBL; AL805902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC152401; AAI52402.1; -; mRNA.
DR CCDS; CCDS52990.1; -. [Q3U1J0-1]
DR RefSeq; NP_766067.2; NM_172479.3. [Q3U1J0-1]
DR AlphaFoldDB; Q3U1J0; -.
DR SMR; Q3U1J0; -.
DR STRING; 10090.ENSMUSP00000033512; -.
DR GlyGen; Q3U1J0; 1 site.
DR iPTMnet; Q3U1J0; -.
DR PhosphoSitePlus; Q3U1J0; -.
DR PaxDb; Q3U1J0; -.
DR PRIDE; Q3U1J0; -.
DR ProteomicsDB; 260778; -. [Q3U1J0-1]
DR ProteomicsDB; 260779; -. [Q3U1J0-2]
DR Antibodypedia; 43079; 103 antibodies from 17 providers.
DR DNASU; 209837; -.
DR Ensembl; ENSMUST00000033512; ENSMUSP00000033512; ENSMUSG00000031170. [Q3U1J0-1]
DR Ensembl; ENSMUST00000115590; ENSMUSP00000111253; ENSMUSG00000031170. [Q3U1J0-2]
DR Ensembl; ENSMUST00000115591; ENSMUSP00000111254; ENSMUSG00000031170. [Q3U1J0-2]
DR GeneID; 209837; -.
DR KEGG; mmu:209837; -.
DR UCSC; uc009sos.2; mouse. [Q3U1J0-1]
DR CTD; 92745; -.
DR MGI; MGI:2148066; Slc38a5.
DR VEuPathDB; HostDB:ENSMUSG00000031170; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000161233; -.
DR HOGENOM; CLU_009020_0_2_1; -.
DR InParanoid; Q3U1J0; -.
DR OMA; DSQMAYT; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q3U1J0; -.
DR TreeFam; TF328787; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 209837; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Slc38a5; mouse.
DR PRO; PR:Q3U1J0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q3U1J0; protein.
DR Bgee; ENSMUSG00000031170; Expressed in fetal liver hematopoietic progenitor cell and 110 other tissues.
DR ExpressionAtlas; Q3U1J0; baseline and differential.
DR Genevisible; Q3U1J0; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022858; F:alanine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISO:MGI.
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:MGI.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022889; F:serine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:1903713; P:asparagine transmembrane transport; ISO:MGI.
DR GO; GO:0006868; P:glutamine transport; ISO:MGI.
DR GO; GO:0015816; P:glycine transport; ISO:MGI.
DR GO; GO:1904557; P:L-alanine transmembrane transport; ISO:MGI.
DR GO; GO:0089709; P:L-histidine transmembrane transport; ISO:MGI.
DR GO; GO:0015825; P:L-serine transport; ISO:MGI.
DR GO; GO:0015804; P:neutral amino acid transport; ISO:MGI.
DR GO; GO:0032329; P:serine transport; ISO:MGI.
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_0000312116"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..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:16141072"
FT /id="VSP_029703"
FT CONFLICT 35
FT /note="F -> L (in Ref. 1; BAC36941)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="S -> G (in Ref. 1; BAC35799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52617 MW; 3B740701BB709ED9 CRC64;
MAISCAVGME MQEPKMNGTL SAGAAAGYRQ EREGFLPTTR NPATGRKPVQ FLDFEGKTSF
GMSVFNLSNA IMGSGILGLA YAMAHTGVIF FLALLLCIAL LSSYSIHLLL TCASVVGIRA
YEQLGQRAFG PAGKVVVAII ICLHNVGAMS SYLFIIKSEL PLVIGTFLHM DPEGDWFLKG
NLLIILVSLL IILPLALMKH LGYLGYTSSL SLTCMLFFLI SVIYKKFQIG CDVSHNDTVV
EAEQAPLQAF NSSCEAELFT VDSQMSYTVP IMAFAFVCHP EVLPIYTELC RPTQRRMQAV
ANMSIGAMFI MYGLTATFGY LTFYSTVKAE MLEMYTQEDM LILCVRLAVL LAVTLTVPVV
LFPIRRALQQ LLFPSKAFSW LRHVAIALIL LILVNILVIC VPTIRDIFGF IGSTSAPSLI
FILPSVFYLR IVPTEVEPLF SWPKIQALCF GVLGVLFMAI SLGFMFANWA TGQSRMSGH
