SC6A6_BOVIN
ID SC6A6_BOVIN Reviewed; 620 AA.
AC Q9MZ34;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sodium- and chloride-dependent taurine transporter;
DE AltName: Full=Solute carrier family 6 member 6;
GN Name=SLC6A6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11118543; DOI=10.1016/s0005-2736(00)00315-1;
RA Qian X., Vinnakota S., Edwards C., Sarkar H.K.;
RT "Molecular characterization of taurine transport in bovine aortic
RT endothelial cells.";
RL Biochim. Biophys. Acta 1509:324-334(2000).
CC -!- FUNCTION: Mediates sodium- and chloride-dependent transport of taurine
CC (PubMed:11118543). Can also mediate transport of beta-alanine,
CC hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).
CC {ECO:0000250|UniProtKB:O35316, ECO:0000269|PubMed:11118543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:O35316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + 2 Na(+)(out) + taurine(out) = chloride(in) + 2
CC Na(+)(in) + taurine(in); Xref=Rhea:RHEA:71223, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:11118543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71224;
CC Evidence={ECO:0000269|PubMed:11118543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(out) + chloride(out) + 2 Na(+)(out) = beta-
CC alanine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71247,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71248;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC Evidence={ECO:0000250|UniProtKB:O35316};
CC -!- ACTIVITY REGULATION: Taurine transport activity is inhibited by L-
CC alanine, guanidinoethane sulfonate, homotaurine and phorbol 12-
CC myristate 13-acetate (PubMed:11118543). Taurine transport activity is
CC stimulated by hypertonic stress (PubMed:11118543).
CC {ECO:0000269|PubMed:11118543}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for taurine {ECO:0000269|PubMed:11118543};
CC Vmax=24.9 pmol/min/mg enzyme for taurine
CC {ECO:0000269|PubMed:11118543};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31641};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Taurine transport activity is down-regulated upon Ser-322
CC phosphorylation. {ECO:0000250|UniProtKB:Q00589}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A6 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF260239; AAF76147.1; -; mRNA.
DR RefSeq; NP_777035.1; NM_174610.2.
DR AlphaFoldDB; Q9MZ34; -.
DR SMR; Q9MZ34; -.
DR STRING; 9913.ENSBTAP00000014720; -.
DR PaxDb; Q9MZ34; -.
DR PRIDE; Q9MZ34; -.
DR GeneID; 282366; -.
DR KEGG; bta:282366; -.
DR CTD; 6533; -.
DR eggNOG; KOG3660; Eukaryota.
DR InParanoid; Q9MZ34; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0005369; F:taurine:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0015734; P:taurine transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002434; Na/ntran_symport_taurine.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01200; TAUTRANSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Sodium- and chloride-dependent taurine transporter"
FT /id="PRO_0000214765"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..236
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..262
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..315
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..348
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..400
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..448
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..525
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..563
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00589"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 620 AA; 69751 MW; 3D5E8F79D336FDA6 CRC64;
MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEAEGKPPQ REKWASRIDF VLSVAGGFVG
LGNVWRFPYL CYKNGGGAFL IPYFIFLFGG GLPVFFLEVI IGQYTSEGGI TCWEKICPLF
AGIGYASIVI VSLLNIYYII ILAWAMYYLF QSFQSELPWA KCNHSWNTPH CLEDTLRRNR
SLWISNSTAN FTSPVTEFWE RKVLSLSSGI DEPGALKWDL ALCLLLVWLV CFFCIWKGVK
STGKVVYFTA TFPFAMLLVL LVRGLTLPGA GAGIKFYLYP DISRLEDPQV WIDAGTQIFF
SYAICLGAMT SLGSYNKYKY NSYRDCMLLG CLNSGTSFVS GFAIFSILGF MAQEQGVDIA
DVAESGPGLA FIAYPKAVTM MPLPTFWSIL FFIMLLLLGL DSQFVEVEGQ ITSLVDLHPS
LLRKGFHREI FIASICCVTY LLGLTMVTEG GMYVFQLFDY YAASGVCLLW VAFFECFAIA
WIYGSDNFYD GIEDMIGYRP GPWMKYCWAV VTPLLCTGCF IFSLVKYVPL TYNKVYTYPT
WAIGLGWCLA LSSMVCVPLV MVIRLAQTEG PFLVRLKYLL TPREPNRWAV EHEGAMPYSS
RMAVNNTLRK PTHIIVETMM
