SC6A5_MOUSE
ID SC6A5_MOUSE Reviewed; 799 AA.
AC Q761V0; Q8CFM5; Q91ZQ2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sodium- and chloride-dependent glycine transporter 2;
DE Short=GlyT-2;
DE Short=GlyT2;
DE AltName: Full=Solute carrier family 6 member 5;
GN Name=Slc6a5 {ECO:0000312|MGI:MGI:105090};
GN Synonyms=Glyt2 {ECO:0000312|EMBL:AAN11408.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD16781.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv {ECO:0000312|EMBL:BAD16781.1};
RX PubMed=15081419; DOI=10.1016/j.bbrc.2004.03.125;
RA Ebihara S., Yamamoto T., Obata K., Yanagawa Y.;
RT "Gene structure and alternative splicing of the mouse glycine transporter
RT type-2.";
RL Biochem. Biophys. Res. Commun. 317:857-864(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL17054.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL17054.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAL17054.1};
RA Liu Q.-R., Li Q.-F.;
RT "Cloning and expression of mouse sodium-dependent glycine transporter 2
RT (Glyt2).";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:P58295}.
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:P58295};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y345};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:15081419};
CC IsoId=Q761V0-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:15081419};
CC IsoId=Q761V0-2; Sequence=VSP_051603;
CC -!- TISSUE SPECIFICITY: [Isoform a]: Expressed at high levels in brain stem
CC and spinal cord and is also expressed in the cerebellum.
CC {ECO:0000269|PubMed:15081419}.
CC -!- TISSUE SPECIFICITY: [Isoform b]: Expressed at high levels in brain stem
CC and spinal cord. {ECO:0000269|PubMed:15081419}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Y345}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A5 subfamily. {ECO:0000305}.
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DR EMBL; AB118159; BAD16781.1; -; mRNA.
DR EMBL; AF411042; AAL17054.1; -; mRNA.
DR EMBL; AY147186; AAN11408.1; -; mRNA.
DR CCDS; CCDS21308.1; -. [Q761V0-2]
DR AlphaFoldDB; Q761V0; -.
DR SMR; Q761V0; -.
DR STRING; 10090.ENSMUSP00000058699; -.
DR TCDB; 2.A.22.2.6; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q761V0; 5 sites.
DR iPTMnet; Q761V0; -.
DR PhosphoSitePlus; Q761V0; -.
DR MaxQB; Q761V0; -.
DR PaxDb; Q761V0; -.
DR PRIDE; Q761V0; -.
DR ProteomicsDB; 255350; -. [Q761V0-1]
DR ProteomicsDB; 255351; -. [Q761V0-2]
DR UCSC; uc012fle.1; mouse. [Q761V0-1]
DR MGI; MGI:105090; Slc6a5.
DR eggNOG; KOG3660; Eukaryota.
DR InParanoid; Q761V0; -.
DR PhylomeDB; Q761V0; -.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR PRO; PR:Q761V0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q761V0; protein.
DR GO; GO:0031045; C:dense core granule; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISO:MGI.
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:1903804; P:glycine import across plasma membrane; ISO:MGI.
DR GO; GO:0015816; P:glycine transport; ISO:MGI.
DR GO; GO:0098810; P:neurotransmitter reuptake; IDA:SynGO.
DR GO; GO:0001504; P:neurotransmitter uptake; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Sodium; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..799
FT /note="Sodium- and chloride-dependent glycine transporter
FT 2"
FT /id="PRO_0000214763"
FT TOPO_DOM 1..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 210
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 211
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 215
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 479
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 511
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 576
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 579
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58295"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..322
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:15081419, ECO:0000303|Ref.2"
FT /id="VSP_051603"
FT CONFLICT 151
FT /note="V -> E (in Ref. 2; AAL17054/AAN11408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 87861 MW; 92AC7750C7023D45 CRC64;
MDCSAPKEMN KQPANILEAA VPGHRDSPRA PRTSPEQDLP AEAPAATVQP PRVPRSASTG
AQTFQSADAR ACEAQQSGVG FCNLSSPRAQ ATSAALRDLS EGHSAQANPP SGPAGAGNAL
HCKIPALRGP EEDANVSVGK GTLEHNNTPA VGWVNMSQST VVLGTDGIAS VLPGSVATTT
IPEDEQGDEN KARGNWSSKL DFILSMVGYA VGLGNVWRFP YLAFQNGGGA FLIPYLMMLA
LAGLPIFFLE VSLGQFASQG PVSVWKAIPA LQGCGIAMLI ISVLIAIYYN VIICYTLFYL
FASFVSVLPW GSCNNPWNTP ECKDKTKLLL DSCVIGDHPK IQIKNSTFCM TAYPNLTMVN
FTSQTNKTFV SGSEEYFKYF VLKISAGIEY PGEIRWPLAF CLFLAWVIVY ASLAKGIKSS
GKVVYFTATF PYVVLVILLI RGVTLPGAGA GIWYFITPKW EKLTDATVWK DAATQIFFSL
SAAWGGLITL SSYNKFHNNC YRDTLIVTCT NSATSIFAGF VIFSVIGFMA NERKVNIENV
ADQGPGIAFV VYPEALTRLP LSPFWAIIFF LMLLTLGLDT MFATIETIVT SISDEFPKYL
RTHKPVFTLG CCICFFIMGF PMITQGGIYM FQLVDTYAAS YALVIIAIFE LVGISYVYGL
QRFCEDIEMM IGFKPNIFWK VCWAFVTPTI LTFILCFSFY QWEPMTYGSY RYPNWSMVLG
WLMLACSVIW IPIMFVIKMY LAPGRFIERL KLVCSPQPDW GPFLAQHRGE RYKNMIDPLG
TSSLGLKLPV KDLELGTQC
