SC6A9_XENLA
ID SC6A9_XENLA Reviewed; 633 AA.
AC A7Y2W8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Sodium- and chloride-dependent glycine transporter 1;
DE Short=GlyT-1;
DE Short=GlyT1;
DE Short=xGlyT1;
DE AltName: Full=Solute carrier family 6 member 9;
GN Name=slc6a9 {ECO:0000250|UniProtKB:P48067};
GN Synonyms=glyt1 {ECO:0000312|EMBL:ABV03172.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABV03172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Tadpole {ECO:0000269|PubMed:18262473};
RX PubMed=18262473; DOI=10.1016/j.gep.2007.12.005;
RA Wester M.R., Teasley D.C., Byers S.L., Saha M.S.;
RT "Expression patterns of glycine transporters (xGlyT1, xGlyT2, and xVIAAT)
RT in Xenopus laevis during early development.";
RL Gene Expr. Patterns 8:261-270(2008).
CC -!- FUNCTION: Sodium- and chloride-dependent glycine transporter which is
CC essential for regulating glycine concentrations at inhibitory
CC glycinergic synapses. {ECO:0000250|UniProtKB:P28571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) +
CC glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000250|UniProtKB:P28571};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28572};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: First expressed in early tailbud stage embryos in
CC the midbrain and anterior spinal cord, and weakly in the hindbrain. By
CC late tailbud stages, expression extends posteriorly in the spinal cord
CC to appear in between somites. Expressed in the forebrain, retina,
CC between the somites and in the blood islands by the swimming tadpole
CC stages. {ECO:0000269|PubMed:18262473}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A9 subfamily. {ECO:0000305}.
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DR EMBL; EU117185; ABV03172.1; -; mRNA.
DR RefSeq; NP_001104228.1; NM_001110758.1.
DR AlphaFoldDB; A7Y2W8; -.
DR SMR; A7Y2W8; -.
DR GeneID; 108714278; -.
DR CTD; 108714278; -.
DR Xenbase; XB-GENE-17338334; slc6a9.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 108714278; Expressed in egg cell and 15 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015375; F:glycine:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0060092; P:regulation of synaptic transmission, glycinergic; ISS:UniProtKB.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR003028; Na/ntran_symport_glycine_GLY1.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR01204; GLY1TRNSPORT.
DR PRINTS; PR00176; NANEUSMPORT.
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; Cell membrane; Glycoprotein; Membrane;
KW Neurotransmitter transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..633
FT /note="Sodium- and chloride-dependent glycine transporter
FT 1"
FT /id="PRO_0000341534"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 588..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 71022 MW; 9B78B51B4B1E3A71 CRC64;
MGLCVNGAVP SEATKKDENL KRGNWGNQIE FVLTSVGYAV GLGNVWRFPY LCYRNGGGAF
MFPYFIMLIF CGIPLFFMEL SFGQFASQGC LGVWRVSPIF KGVGYGMMVV STYIGIYYNV
VICIAFYYFF ASMNRVLPWT YCNNLWNTNN CAGVLSPNSS ASFNLSSQQN LLNLTLGLNQ
TLKRTSPSEE YWRRHVLKIS EDIGDFGEVQ LPLLGCLGVS WLVVFLCLIR GVKSSGKVVY
FTATFPYVVL TILFIRGITL EGAINGILYY LTPQWDKILH AMVWGDAASQ IFYSLGCAWG
GLITMASYNK FHNNCYRDSI IISITNCATS VYAGFVIFSI LGFMATHLGV DVSEVADHGP
GLAFVAYPEA LTLLPISPLW SILFFFMLIL LGLGTQFCLL ETLVTAVVDE IGNDWIIRWK
TLVTLGVAII GFLLGIPLTT QAGIYWLLLM DNYAASFSLV IISCIMCIAV MYIYGHRKYF
KDIEMMLGFP PPLFFQICWR FISPGIIFFI LIFTVIQYRP IQYNDYLYPD WAITIGFLMA
LSSVICIPLY AIFKIWCSEG DTFLQRLKNA VKPSKDWGPA LQEHRTGRYA QMSSTRSESN
PEAQPLNPEK MKEDLSLTIQ GSNGQAHTQD SKV