S38A2_DANRE
ID S38A2_DANRE Reviewed; 504 AA.
AC Q5SPB1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sodium-coupled neutral amino acid transporter 2;
DE AltName: Full=Amino acid transporter A2;
DE AltName: Full=Solute carrier family 38 member 2;
DE AltName: Full=System A amino acid transporter 2;
DE AltName: Full=System A transporter 1;
DE AltName: Full=System N amino acid transporter 2;
GN Name=slc38a2; Synonyms=snat2; ORFNames=si:ch211-132p20.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
CC Mediates the saturable, pH-sensitive and electrogenic cotransport of
CC neutral amino acids and sodium ions with a stoichiometry of 1:1 (By
CC similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Inhibited by N-methyl-D-glucamine and choline.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AL929171; CAI11588.1; -; Genomic_DNA.
DR RefSeq; NP_001038569.1; NM_001045104.1.
DR AlphaFoldDB; Q5SPB1; -.
DR SMR; Q5SPB1; -.
DR STRING; 7955.ENSDARP00000118404; -.
DR PaxDb; Q5SPB1; -.
DR Ensembl; ENSDART00000146779; ENSDARP00000118404; ENSDARG00000045886.
DR GeneID; 566537; -.
DR KEGG; dre:566537; -.
DR CTD; 54407; -.
DR ZFIN; ZDB-GENE-030131-9659; slc38a2.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000155486; -.
DR HOGENOM; CLU_009020_0_1_1; -.
DR InParanoid; Q5SPB1; -.
DR OMA; QFWITAF; -.
DR OrthoDB; 1109791at2759; -.
DR PhylomeDB; Q5SPB1; -.
DR TreeFam; TF328787; -.
DR Reactome; R-DRE-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-DRE-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:Q5SPB1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045886; Expressed in muscle tissue and 30 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IBA:GO_Central.
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:0006868; P:glutamine transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="Sodium-coupled neutral amino acid transporter 2"
FT /id="PRO_0000311374"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..99
FT /note="Regulates protein turnover upon amino acid
FT deprivation"
FT /evidence="ECO:0000250"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 504 AA; 55832 MW; DF6EE0FA9189D20D CRC64;
MNKAPAQMSR FNIAPDMDSS STNSNEYTNY QDHASKVPLN GIQYSDVEAE SQNFLSDHHL
GKKKYEAEYS PGSASFGMSV FNLGNAIMGS GILGLSYAMA NTGIAMFVIL LVAVAIFSLY
SVHLLLKTAN EGGSLVYEQL GYKAFGIPGK LAASCSITMQ NFGAMASYLY IVKYELPIVI
RAFLDSNDNA WYTNGDYLVL IVTMSIILPL SLLKNLGYLG YTSGFSLLCM VFFLIVVIYK
KFQIPCPLPE NFINITVNVS QPPQTNNSTD EECCKPKYFI FNSQTVYAVP ILTFAFVCHP
AILPMYEELK DRSRRKMQNV ANVSFLGMFI MYLLAALFGY LTFNEAVEPE LLHTYSKVYN
FDVVLLIVRL AVLTAVTLTV PVVLFPIRTS VNHLLGASKE FSWPRHICIT VALLVCVNIL
VIFVPTIRDI FGFIGASAAA MLIFILPSAF YIKLVKKESM KSVQKIGATL FLIMGFLVMT
GSMALIIMDW IHNALSSEEH TGGH
