S6A19_RAT
ID S6A19_RAT Reviewed; 634 AA.
AC Q2A865; A4ZVM8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 {ECO:0000312|RGD:1594328};
GN Synonyms=B0at1 {ECO:0000312|EMBL:CAI64591.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:CAI64591.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAI64591.1};
RA Volk C., Koepsell H., Arndt P.;
RT "Cloning and characterization of the rat B0 amino acid transporter 1.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar Kyoto;
RX PubMed=17646927; DOI=10.1007/s11010-007-9548-9;
RA Pinho M.J., Serrao M.P., Jose P.A., Soares-da-Silva P.;
RT "Organ specific underexpression renal of Na+-dependent B0AT1 in the SHR
RT correlates positively with overexpression of NHE3 and salt intake.";
RL Mol. Cell. Biochem. 306:9-18(2007).
RN [3] {ECO:0000305}
RP INDUCTION BY HIGH SALT INTAKE.
RX PubMed=17264310; DOI=10.1152/ajprenal.00465.2006;
RA Pinho M.J., Serrao M.P., Soares-da-Silva P.;
RT "High-salt intake and the renal expression of amino acid transporters in
RT spontaneously hypertensive rats.";
RL Am. J. Physiol. 292:F1452-F1463(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- INDUCTION: By high salt intake in SHR rats. Reduced level upon high
CC salt intake in Wistar Kyoto rats. {ECO:0000269|PubMed:17264310}.
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; AJ890206; CAI64591.1; -; mRNA.
DR EMBL; EF474455; ABP63542.1; -; mRNA.
DR RefSeq; NP_001034811.1; NM_001039722.2.
DR AlphaFoldDB; Q2A865; -.
DR SMR; Q2A865; -.
DR STRING; 10116.ENSRNOP00000028917; -.
DR DrugCentral; Q2A865; -.
DR GuidetoPHARMACOLOGY; 939; -.
DR GlyGen; Q2A865; 5 sites.
DR iPTMnet; Q2A865; -.
DR PhosphoSitePlus; Q2A865; -.
DR PaxDb; Q2A865; -.
DR PRIDE; Q2A865; -.
DR Ensembl; ENSRNOT00000036714; ENSRNOP00000028917; ENSRNOG00000026501.
DR GeneID; 664630; -.
DR KEGG; rno:664630; -.
DR UCSC; RGD:1594328; rat.
DR CTD; 340024; -.
DR RGD; 1594328; Slc6a19.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000154896; -.
DR HOGENOM; CLU_006855_7_2_1; -.
DR InParanoid; Q2A865; -.
DR OMA; SAKIQMS; -.
DR OrthoDB; 547281at2759; -.
DR PhylomeDB; Q2A865; -.
DR TreeFam; TF343812; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-RNO-442660; Na+/Cl- dependent neurotransmitter transporters.
DR PRO; PR:Q2A865; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000026501; Expressed in jejunum and 8 other tissues.
DR Genevisible; Q2A865; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015804; P:neutral amino acid transport; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein 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_0000299498"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
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:0007744|PubMed:22673903"
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"
FT CONFLICT 32
FT /note="R -> K (in Ref. 1; CAI64591)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> P (in Ref. 1; CAI64591)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="F -> Y (in Ref. 1; CAI64591)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="F -> L (in Ref. 2; ABP63542)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="L -> F (in Ref. 2; ABP63542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 71232 MW; 005015BEAF876CE4 CRC64;
MVRLVLPNPG LEDRIPSLDE LEVIEKEEAS SRPKWDNKAQ YMLTCVGFCV GLGNVWRFPY
LCQSHGGGAF MIPFLILLVL EGIPLLHLEF AIGQRLRKGS VGVWSSIHPA LKGVGIASMF
VSFMVGLYYN TIIAWVMWYF FNSFQEPLPW SECPLNQNQT GYVEECAKSS SVDYFWYRET
LNISTSISDS GSIQWWILLC LTCAWSVLYV CTIRGIETTG KAVYITSTLP YVVLTIFLIR
GLTLKGATNG IVFLFTPNIT ELSNPNTWLD AGAQVFYSFS LAFGGLISFS SYNSVHNNCE
MDSVIVSIIN GFTSVYAATV VYSIIGFRAT ERFDDCVNTN ILTLINGFDL PEGNVTAENF
EAYQHWCNAT NPEAYAQLTF QTCDINTFLS EGVEGTGLAF IVFTEAITKM PVSPLWSVLF
FIMLFCLGLS SMFGNMEGVV VPLQDLNITP KKWPKELLTG LICLGTYLIA FIFTLNSGQY
WLSLLDSYAG SIPLLIIAFC EMFAVVYVYG VDRFNKDIEF MIGHKPNIFW QVTWRVVSPL
IMLVIFLFFF VIEVNKQLMY SVWDPDYEEF PKSQKVPYPD WVYAVVVIVA GVPCLTIPCF
AIYKLIRNYC QKSGDQHGLV NALSTASVNG DLKN
