ID G1P5Y4_MYOLU Unreviewed; 495 AA.
AC G1P5Y4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Sodium-coupled neutral amino acid symporter 2 {ECO:0000256|ARBA:ARBA00039205};
DE AltName: Full=Amino acid transporter A2 {ECO:0000256|ARBA:ARBA00042516};
DE AltName: Full=Solute carrier family 38 member 2 {ECO:0000256|ARBA:ARBA00042868};
DE AltName: Full=System A amino acid transporter 2 {ECO:0000256|ARBA:ARBA00041859};
DE AltName: Full=System A transporter 1 {ECO:0000256|ARBA:ARBA00041916};
DE AltName: Full=System N amino acid transporter 2 {ECO:0000256|ARBA:ARBA00041835};
GN Name=SLC38A2 {ECO:0000313|Ensembl:ENSMLUP00000005444.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005444.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005444.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005444.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000256|ARBA:ARBA00035911};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285;
CC Evidence={ECO:0000256|ARBA:ARBA00035911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine(in) + Na(+)(in) = L-asparagine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:71383, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000256|ARBA:ARBA00036092};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71385;
CC Evidence={ECO:0000256|ARBA:ARBA00036092};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035969};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68238;
CC Evidence={ECO:0000256|ARBA:ARBA00035969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine(in) + Na(+)(in) = L-histidine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:71583, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595;
CC Evidence={ECO:0000256|ARBA:ARBA00036231};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71585;
CC Evidence={ECO:0000256|ARBA:ARBA00036231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine(in) + Na(+)(in) = L-leucine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29263, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427;
CC Evidence={ECO:0000256|ARBA:ARBA00036115};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29265;
CC Evidence={ECO:0000256|ARBA:ARBA00036115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine(in) + Na(+)(in) = L-methionine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68240, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844;
CC Evidence={ECO:0000256|ARBA:ARBA00036104};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68242;
CC Evidence={ECO:0000256|ARBA:ARBA00036104};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(in) + Na(+)(in) = L-phenylalanine(out) +
CC Na(+)(out); Xref=Rhea:RHEA:68244, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000256|ARBA:ARBA00036194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68246;
CC Evidence={ECO:0000256|ARBA:ARBA00036194};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000256|ARBA:ARBA00036201};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28969;
CC Evidence={ECO:0000256|ARBA:ARBA00036201};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000256|ARBA:ARBA00036787};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577;
CC Evidence={ECO:0000256|ARBA:ARBA00036787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926;
CC Evidence={ECO:0000256|ARBA:ARBA00035810};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001;
CC Evidence={ECO:0000256|ARBA:ARBA00035810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000256|ARBA:ARBA00036564};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68230;
CC Evidence={ECO:0000256|ARBA:ARBA00036564};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AAPE02023417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006091520.1; XM_006091458.2.
DR RefSeq; XP_014313658.1; XM_014458172.1.
DR RefSeq; XP_014313659.1; XM_014458173.1.
DR AlphaFoldDB; G1P5Y4; -.
DR STRING; 59463.ENSMLUP00000005444; -.
DR Ensembl; ENSMLUT00000005958.2; ENSMLUP00000005444.2; ENSMLUG00000005954.2.
DR GeneID; 102421580; -.
DR KEGG; mlf:102421580; -.
DR CTD; 54407; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000155486; -.
DR HOGENOM; CLU_009020_0_1_1; -.
DR InParanoid; G1P5Y4; -.
DR OMA; SHYADMD; -.
DR OrthoDB; 935269at2759; -.
DR TreeFam; TF328787; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0005295; F:neutral L-amino acid:sodium symporter activity; IEA:Ensembl.
DR GO; GO:1903841; P:cellular response to arsenite(3-); IEA:Ensembl.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IEA:Ensembl.
DR GO; GO:0015824; P:proline transport; IEA:Ensembl.
DR GO; GO:0080135; P:regulation of cellular response to stress; IEA:Ensembl.
DR InterPro; IPR013057; AA_transpt_TM.
DR PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR PANTHER; PTHR22950:SF207; SODIUM-COUPLED NEUTRAL AMINO ACID TRANSPORTER 2; 1.
DR Pfam; PF01490; Aa_trans; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..487
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55101 MW; 2F891D3F5BA0B16E CRC64;
MKKAEVGRFS ISPDEDSSSY SSNSDFNYSY PTKQAALKSH YADVDPENQN FLLESNLGKK
KYETDFHPGT TSFGMSVFNL SNAIVGSGIL GLSYAMANTG IALFIILLTF VSIFSLYSVH
LLLKTANEGG SLSYEQLGHK AFGMVGKLAA SGSITMQNIG AMSSYLFIVK YELPLVIKAL
MNIEDTTGLW YLNGDYLVLL VSLLLILPLS LLKNLGYLGY TSGLSLLCML FFLIVVICKK
FEIACPFEDA VNSTFIEPTA SLPYMAFNTT DDSCKPHYFF FNSQTVYAVP ILTFSFVCHP
AILPIYEELK DRSRRRMMNV SKISFFAMFL MYLFAALFGY LTFFEKVESE LLHTYSKVLG
ADILLLIVRL AVLMAVTLTV PVVIFPIRSS ITQLFCPTKD FTWWRHGLIT ISILAFTNVL
VIFVPTIRDI FGFIGASAAA MLIFILPSAF YIKLVKKESM KSVQKIGALL FLLSGVVVMI
GSMVLIILDW VHNAH
//
