SC6A5_XENLA
ID SC6A5_XENLA Reviewed; 790 AA.
AC A7Y2X0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Sodium- and chloride-dependent glycine transporter 2;
DE Short=GlyT-2;
DE Short=GlyT2;
DE Short=xGlyT2;
DE AltName: Full=Solute carrier family 6 member 5;
GN Name=slc6a5 {ECO:0000250|UniProtKB:Q9Y345};
GN Synonyms=glyt2 {ECO:0000312|EMBL:ABV03173.1};
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:ABV03173.1}
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.
CC Terminates the action of glycine by its high affinity sodium-dependent
CC reuptake into presynaptic terminals. May be responsible for the
CC termination of neurotransmission at strychnine-sensitive glycinergic
CC synapses (By similarity). {ECO:0000250|UniProtKB:Q9Y345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + glycine(out) + 3 Na(+)(out) = chloride(in) +
CC glycine(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70695, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000250|UniProtKB:Q9Y345};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y345};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: First expressed in late neurula stages in the
CC anterior spinal cord, where expression intensifies through the tailbud
CC stages, and by hatching, expression is seen in the hindbrain. During
CC late hatching stages, expression extends along most of the length of
CC the spinal cord, mildly intensifies in the hindbrain, and appears in
CC localized regions of the lateral forebrain and medial midbrain. By the
CC swimming tadpole stage, weak expression appears in the anterior
CC hindbrain, with stronger expression in the posterior, postmitotic
CC neurons. {ECO:0000269|PubMed:18262473}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A5 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; EU117186; ABV03173.1; -; mRNA.
DR RefSeq; NP_001104197.1; NM_001110727.1.
DR AlphaFoldDB; A7Y2X0; -.
DR SMR; A7Y2X0; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015375; F:glycine:sodium symporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Neurotransmitter transport; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..790
FT /note="Sodium- and chloride-dependent glycine transporter
FT 2"
FT /id="PRO_0000341533"
FT TOPO_DOM 1..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 201
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 202
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 206
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 470
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 502
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 567
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 570
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 304..313
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
SQ SEQUENCE 790 AA; 87452 MW; 2F1683C27918BE72 CRC64;
MDYVNVVDGS KKTMNSPEGA APGLIGATGI TNPTPDNDLP LQASNKLTRL SQSTSNDSKL
IAAGEPKACD LERSRVGGSC KMTTPGHSNF VLKRDSVEGC PAKNSSMAES NGQTNPMHCR
IVPLQSAEGD TNQGFGKNSL EQNNAKGDWV PISQSTVVLG TDGNTSVFPG TLTGDEEGDE
NKARGNWSNK LDFILSMVGY AVGLGNVWRF PYLAFKNGGG AFLIPYLTML ALAGLPIFYL
EVALGQFASQ GPISVWKAIP ALQGCGIAML IISVLIAIYY NIIMCYTIFY LFASLVYVLP
WASCNNPWNT PDCKDKDRLL LDSCIISSQP NIQIKNSTFC MTAYPNLTMV NFTSHGNKSF
VSGSEEYFKY NMLKISAGIE YPGEIRWPLV FCLFLAWIIV YASLAKGIKT SGKVVYSTAT
FPYVVLVILL FRGVTLPGAG DGIWWFIMPK WEKLMDATVW KDAATQIFFS LSAAWGGLIT
LSSYNKFHNN LYRDTLIVTC INSATSIFAG FVIFSVIGFM AHILNVDIEK VADQGPGIAF
VVYPEALTRL PLSPFWAIIF FLMLLTLGLD TMFATIETIV TSVSDEFPKL LRTHKPLFTL
VCCVAFFIMG FPMITQGGIY MLQLVDNYAA SYSLVIIAIF ELVGISYIYG LQRFCEDIEM
MIGFQPSRFW KICWAFVTPT ILTFILGFSF YQWEPMTYGS YHYPSWSMVM GWLMLACSVI
WIPIMFVIKM FLAPGTFIER LKLVCSPQPD WGPFLAKHRG ERYKNMIDPL GTSSLGLKLP
PKDFELGTQC
