S6A19_PONAB
ID S6A19_PONAB Reviewed; 634 AA.
AC Q5R6J1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT1;
DE AltName: Full=Solute carrier family 6 member 19;
DE AltName: Full=System B(0) neutral amino acid transporter AT1;
GN Name=SLC6A19; Synonyms=B0AT1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transporter that mediates resorption of neutral amino acids
CC across the apical membrane of renal and intestinal epithelial cells.
CC This uptake is sodium-dependent and chloride-independent. Requires
CC CLTRN in kidney or ACE2 in intestine for cell surface expression and
CC amino acid transporter activity. {ECO:0000250|UniProtKB:Q9D687}.
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:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) + Na(+)(in) = L-cysteine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68232, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-isoleucine(in) + Na(+)(in) = L-isoleucine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29275, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
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:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan(in) + Na(+)(in) = L-tryptophan(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68252, ChEBI:CHEBI:29101, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine(in) + Na(+)(in) = L-tyrosine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:68248, ChEBI:CHEBI:29101, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-valine(in) + Na(+)(in) = L-valine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:29267, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762;
CC Evidence={ECO:0000250|UniProtKB:Q695T7};
CC -!- SUBUNIT: Interacts in a tissue-specific manner with ACE2 in small
CC intestine and with CLTRN in the kidney. Interacts with CLTRN; this
CC interaction is required for trafficking of SLC6A19 to the plasma
CC membrane and for its catalytic activation in kidneys. Interacts with
CC ACE2; this interaction is required for trafficking of SLC6A19 to the
CC plasma membrane and for its catalytic activation in intestine.
CC Interacts with ANPEP; the interaction positively regulates its amino
CC acid transporter activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9D687}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q695T7}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A19 subfamily. {ECO:0000305}.
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DR EMBL; CR860498; CAH92619.1; -; mRNA.
DR RefSeq; NP_001126535.1; NM_001133063.1.
DR AlphaFoldDB; Q5R6J1; -.
DR SMR; Q5R6J1; -.
DR GeneID; 100173524; -.
DR KEGG; pon:100173524; -.
DR CTD; 340024; -.
DR InParanoid; Q5R6J1; -.
DR OrthoDB; 547281at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002438; Neutral_aa_SLC6.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01206; ORPHTRNSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..634
FT /note="Sodium-dependent neutral amino acid transporter
FT B(0)AT1"
FT /id="PRO_0000214811"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D687"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D687"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 71102 MW; EF3F0D20162B8E4C CRC64;
MVRLVLPNPG LDTRILSLAE LETIEQEEAS SRPKWDNKAQ YLLTCVGFCV GLGNVWRFPY
LCQSHGGGAF MIPFLILLVL EGIPLLHLEF AIGQRLRRGS LGVWSSIHPA LKGVGLTSML
VSFVVGLYYN TIISWIMWYL FNSFQEPLPW SECPLNENQT GYVDECARSS PVDYFWYRET
LNISTSISDS GSIQWRMLLC LACAWSVLYM CTIRGIETTG KVVYITSTLP YVVLTIFLIR
GLTLKGATKG IIYLFTPNVT ELANPVTWLD AGAQVFFSFS LAFGGLISFS SYNSVHNNCE
RDSVIVSIIN GFTSVYVAIV IYSIIGFRAT QRYDDCFSTN ILTLINGFDL PEGNVTQENF
VEMQRQCNAS NPAAYAQLVF QTCDINSFLS EGVEGTGLAF IVFTEAITKM PVSPLWSVLF
FIMLFCLGLS SMFGNMEGVV VPLQDLKVIP PKWPKELLTG LICLGTFLIG FIFTLNSGQY
WLSLLDSYAV SIPLLIIAFC EMFSVVYVYG VDRFNKDIEF MIGHKPNIFW QVTWRVVSPL
LMLIILVFFF VVQVSQELTY SIWNPGYEEF PKSQKISHPN WVYAVVVIVA GVPSLTIPSY
AIYKLIRNCC QKPGDRQGLV STLSTASMNG DLKY
