ID W5KY52_ASTMX Unreviewed; 501 AA.
AC W5KY52;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012514.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000012514.1}
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 RefSeq; XP_007238008.1; XM_007237946.2.
DR AlphaFoldDB; W5KY52; -.
DR STRING; 7994.ENSAMXP00000012514; -.
DR Ensembl; ENSAMXT00000012514.2; ENSAMXP00000012514.1; ENSAMXG00000012158.2.
DR GeneID; 103028401; -.
DR KEGG; amex:103028401; -.
DR CTD; 54407; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000155486; -.
DR HOGENOM; CLU_009020_0_1_1; -.
DR InParanoid; W5KY52; -.
DR OMA; SHYADMD; -.
DR OrthoDB; 935269at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000012158; Expressed in zone of skin and 14 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:UP000018467};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 403..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..481
FT /note="Amino acid transporter transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01490"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 55093 MW; F7350D2E89512EBD CRC64;
MSKTPGQPEM SRFNISPDED SSCSSNSNDY QGYQDCTGKK GPIGSSQYAD MDAENQNFLP
HYAAKKKYEA EYHPGTASFG MSVFNLGNAI MGSGILGLSY AMANTGIALF VILLVAVSIF
SLYSVHLLLK TANEGGSLVY EQLGYKAFGM PGKLAASCSI TMQNIGAMSS YLYIVKYELP
IVIKAFVENS DGMWYTNGDY LVMLVSLIII LPLSLLKNLG YLGYTSGFSL LCMVFFVIVV
IYKTFQIPCP LPNDIINMTL NHTVAHNSSV CTPKYFVFNS QTVYAVPILT FAFVCHPAIL
PMYEELKDRS RKKMQGVANV SFLAMFIMYL LAALFGYLTF NDAVESELLH TYSKVYKFDV
VLLIVRLAVL TAVTLTVPVV LFPIRTSVNQ LLCASKEFSW IRHTIITVIL LACVNVLVIF
VPTIRDIFGF IGASAAAMLI FILPSAFYIK LVKKEPMMSV QKIGACVFLA SGFLVMFGSM
TLIVLDWIHN AGASEAHGDG H
//
