SC6A5_HUMAN
ID SC6A5_HUMAN Reviewed; 797 AA.
AC Q9Y345; O95288; Q4VAM7; Q9BX77;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 183.
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; Synonyms=GLYT2, NET1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND VARIANTS SER-124 AND
RP GLY-162.
RX PubMed=9845349; DOI=10.1016/s0014-5793(98)01390-8;
RA Morrow J.A., Collie I.T., Dunbar D.R., Walker G.B., Shahid M., Hill D.R.;
RT "Molecular cloning and functional expression of the human glycine
RT transporter GlyT2 and chromosomal localisation of the gene in the human
RT genome.";
RL FEBS Lett. 439:334-340(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING (ISOFORMS 2 AND 3),
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS
RP SER-102; SER-124 AND GLY-162.
RC TISSUE=Spinal cord;
RX PubMed=10381548; DOI=10.1016/s0169-328x(99)00135-7;
RA Gallagher M.J., Burgess L.H., Brunden K.R.;
RT "Characterization of multiple forms of the human glycine transporter type-
RT 2.";
RL Brain Res. Mol. Brain Res. 70:101-115(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS SER-124; GLY-162; ARG-184; ASN-463
RP AND ALA-751, AND CHARACTERIZATION OF VARIANTS ARG-184; ASN-463 AND ALA-751.
RC TISSUE=Spinal cord;
RX PubMed=10606742; DOI=10.1016/s0014-5793(99)01636-1;
RA Evans J., Herdon H., Cairns W., O'Brien E., Chapman C., Terrett J.,
RA Gloger I.;
RT "Cloning, functional characterisation and population analysis of a variant
RT form of the human glycine type 2 transporter.";
RL FEBS Lett. 463:301-306(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-124 AND GLY-162.
RA Luyten W.;
RT "Cloning and expression of a human glycine transporter type II.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-124 AND GLY-162.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP VARIANTS HKPX3 VAL-306; MET-425; CYS-482; CYS-491; SER-509 AND ARG-510,
RP VARIANT GLU-89, CHARACTERIZATION OF VARIANTS HKPX3 VAL-306; MET-425;
RP CYS-482; CYS-491; SER-509 AND ARG-510, CHARACTERIZATION OF VARIANT GLU-89,
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16751771; DOI=10.1038/ng1814;
RA Rees M.I., Harvey K., Pearce B.R., Chung S.K., Duguid I.C., Thomas P.,
RA Beatty S., Graham G.E., Armstrong L., Shiang R., Abbott K.J., Zuberi S.M.,
RA Stephenson J.B., Owen M.J., Tijssen M.A., van den Maagdenberg A.M.,
RA Smart T.G., Supplisson S., Harvey R.J.;
RT "Mutations in the gene encoding GlyT2 (SLC6A5) define a presynaptic
RT component of human startle disease.";
RL Nat. Genet. 38:801-806(2006).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-632.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [9]
RP VARIANT HKPX3 LEU-429, CHARACTERIZATION OF VARIANT HKPX3 LEU-429, FUNCTION,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TRANSPORTER ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31370103; DOI=10.1111/ejn.14533;
RA Kitzenmaier A., Schaefer N., Kasaragod V.B., Polster T., Hantschmann R.,
RA Schindelin H., Villmann C.;
RT "The P429L loss of function mutation of the human glycine transporter 2
RT associated with hyperekplexia.";
RL Eur. J. Neurosci. 50:3906-3920(2019).
CC -!- FUNCTION: Sodium- and chloride-dependent glycine transporter
CC (PubMed:9845349, PubMed:10381548, PubMed:10606742, PubMed:31370103,
CC PubMed:16751771). Terminates the action of glycine by its high affinity
CC sodium-dependent reuptake into presynaptic terminals (PubMed:9845349).
CC May be responsible for the termination of neurotransmission at
CC strychnine-sensitive glycinergic synapses (PubMed:9845349).
CC {ECO:0000269|PubMed:10381548, ECO:0000269|PubMed:10606742,
CC ECO:0000269|PubMed:16751771, ECO:0000269|PubMed:31370103,
CC ECO:0000269|PubMed:9845349}.
CC -!- FUNCTION: [Isoform 2]: Lacks sodium- and chloride-dependent glycine
CC transporter activity. {ECO:0000269|PubMed:10381548}.
CC -!- FUNCTION: [Isoform 3]: Lacks sodium- and chloride-dependent glycine
CC transporter activity. {ECO:0000269|PubMed:10381548}.
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:0000269|PubMed:10381548, ECO:0000269|PubMed:10606742,
CC ECO:0000269|PubMed:16751771, ECO:0000269|PubMed:31370103,
CC ECO:0000269|PubMed:9845349};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=108 uM for glycine {ECO:0000269|PubMed:9845349};
CC KM=10.4 uM for glycine {ECO:0000269|PubMed:10381548};
CC KM=160 uM for glycine {ECO:0000269|PubMed:10606742};
CC KM=66 uM for glycine {ECO:0000269|PubMed:16751771};
CC KM=239 uM for glycine {ECO:0000269|PubMed:31370103};
CC Vmax=190 pmol/min/mg enzyme for glycine
CC {ECO:0000269|PubMed:10381548};
CC Vmax=3734 pmol/min/mg enzyme for glycine
CC {ECO:0000269|PubMed:10606742};
CC Vmax=1.64 nmol/min/mg enzyme for glycine
CC {ECO:0000269|PubMed:16751771};
CC Vmax=8.8 nmol/min/mg enzyme for glycine
CC {ECO:0000269|PubMed:31370103};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16751771,
CC ECO:0000269|PubMed:31370103}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y345-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y345-2; Sequence=VSP_061562;
CC Name=3;
CC IsoId=Q9Y345-3; Sequence=VSP_061563;
CC -!- TISSUE SPECIFICITY: Expressed in medulla, and to a lesser extent in
CC spinal cord and cerebellum. {ECO:0000269|PubMed:9845349}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:31370103}.
CC -!- DISEASE: Hyperekplexia 3 (HKPX3) [MIM:614618]: A neurologic disorder
CC characterized by neonatal hypertonia, an exaggerated startle response
CC to tactile or acoustic stimuli, and life-threatening neonatal apnea
CC episodes. Notably, in some cases, symptoms resolved in the first year
CC of life. {ECO:0000269|PubMed:16751771, ECO:0000269|PubMed:31370103}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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; AF085412; AAC95145.1; -; mRNA.
DR EMBL; AF142501; AAD27892.1; -; mRNA.
DR EMBL; AF352733; AAK29670.1; -; mRNA.
DR EMBL; AF117999; AAK12641.1; -; mRNA.
DR EMBL; AC090707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096319; AAH96319.1; -; mRNA.
DR CCDS; CCDS7854.1; -.
DR RefSeq; NP_001305298.1; NM_001318369.1.
DR RefSeq; NP_004202.3; NM_004211.4.
DR AlphaFoldDB; Q9Y345; -.
DR SMR; Q9Y345; -.
DR BioGRID; 114599; 39.
DR IntAct; Q9Y345; 10.
DR STRING; 9606.ENSP00000434364; -.
DR BindingDB; Q9Y345; -.
DR ChEMBL; CHEMBL3060; -.
DR DrugBank; DB00145; Glycine.
DR DrugCentral; Q9Y345; -.
DR GuidetoPHARMACOLOGY; 936; -.
DR TCDB; 2.A.22.2.10; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9Y345; 4 sites.
DR iPTMnet; Q9Y345; -.
DR PhosphoSitePlus; Q9Y345; -.
DR BioMuta; SLC6A5; -.
DR DMDM; 296452967; -.
DR MassIVE; Q9Y345; -.
DR PaxDb; Q9Y345; -.
DR PeptideAtlas; Q9Y345; -.
DR PRIDE; Q9Y345; -.
DR ProteomicsDB; 85975; -.
DR Antibodypedia; 25288; 74 antibodies from 22 providers.
DR DNASU; 9152; -.
DR Ensembl; ENST00000525748.6; ENSP00000434364.2; ENSG00000165970.12.
DR GeneID; 9152; -.
DR KEGG; hsa:9152; -.
DR MANE-Select; ENST00000525748.6; ENSP00000434364.2; NM_004211.5; NP_004202.4.
DR UCSC; uc001mqd.4; human.
DR CTD; 9152; -.
DR DisGeNET; 9152; -.
DR GeneCards; SLC6A5; -.
DR GeneReviews; SLC6A5; -.
DR HGNC; HGNC:11051; SLC6A5.
DR HPA; ENSG00000165970; Tissue enriched (brain).
DR MalaCards; SLC6A5; -.
DR MIM; 604159; gene.
DR MIM; 614618; phenotype.
DR neXtProt; NX_Q9Y345; -.
DR OpenTargets; ENSG00000165970; -.
DR Orphanet; 3197; Hereditary hyperekplexia.
DR PharmGKB; PA35911; -.
DR VEuPathDB; HostDB:ENSG00000165970; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000154963; -.
DR HOGENOM; CLU_006855_4_0_1; -.
DR InParanoid; Q9Y345; -.
DR OMA; GAPKEMN; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q9Y345; -.
DR TreeFam; TF343812; -.
DR PathwayCommons; Q9Y345; -.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-HSA-5619089; Defective SLC6A5 causes hyperekplexia 3 (HKPX3).
DR SignaLink; Q9Y345; -.
DR BioGRID-ORCS; 9152; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; SLC6A5; human.
DR GeneWiki; Glycine_transporter_2; -.
DR GenomeRNAi; 9152; -.
DR Pharos; Q9Y345; Tchem.
DR PRO; PR:Q9Y345; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y345; protein.
DR Bgee; ENSG00000165970; Expressed in secondary oocyte and 27 other tissues.
DR ExpressionAtlas; Q9Y345; baseline and differential.
DR Genevisible; Q9Y345; HS.
DR GO; GO:0031045; C:dense core granule; ISS:ARUK-UCL.
DR GO; GO:0005768; C:endosome; ISS:ARUK-UCL.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0015375; F:glycine:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:1903804; P:glycine import across plasma membrane; IDA:FlyBase.
DR GO; GO:0001504; P:neurotransmitter uptake; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:FlyBase.
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; Disease variant; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Sodium; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..797
FT /note="Sodium- and chloride-dependent glycine transporter
FT 2"
FT /id="PRO_0000214762"
FT TOPO_DOM 1..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..247
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..412
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..438
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..491
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..524
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..576
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..622
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..698
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..735
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 208
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 209
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 213
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 477
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 509
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 574
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 577
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58295"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q761V0"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q761V0"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 311..320
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10381548"
FT /id="VSP_061562"
FT VAR_SEQ 496..511
FT /note="NNCYRDTLIVTCTNSA -> VP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10381548"
FT /id="VSP_061563"
FT VARIANT 89
FT /note="A -> E (no effect on subcellular location; no effect
FT on glycine transport; dbSNP:rs61736602)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044163"
FT VARIANT 102
FT /note="G -> S (in dbSNP:rs1443547)"
FT /evidence="ECO:0000269|PubMed:10381548"
FT /id="VAR_044164"
FT VARIANT 124
FT /note="F -> S (in dbSNP:rs1443548)"
FT /evidence="ECO:0000269|PubMed:10381548,
FT ECO:0000269|PubMed:10606742, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9845349, ECO:0000269|Ref.4"
FT /id="VAR_044165"
FT VARIANT 132
FT /note="A -> G (in dbSNP:rs34243519)"
FT /id="VAR_044166"
FT VARIANT 162
FT /note="A -> G (in dbSNP:rs1443549)"
FT /evidence="ECO:0000269|PubMed:10381548,
FT ECO:0000269|PubMed:10606742, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9845349, ECO:0000269|Ref.4"
FT /id="VAR_044167"
FT VARIANT 184
FT /note="Q -> R (no effect on glycine transport)"
FT /evidence="ECO:0000269|PubMed:10606742"
FT /id="VAR_011591"
FT VARIANT 306
FT /note="L -> V (in HKPX3; compound heterozygote with S-509;
FT impairment of glycine transport when coexpressed with S-509
FT in vitro; dbSNP:rs121908496)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044168"
FT VARIANT 425
FT /note="T -> M (in HKPX3; no effect on subcellular location;
FT impairs glycine transport; dbSNP:rs121908498)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044169"
FT VARIANT 429
FT /note="P -> L (in HKPX3; impairs glycine transport; no
FT effect on subcellular location; dbSNP:rs745539706)"
FT /evidence="ECO:0000269|PubMed:31370103"
FT /id="VAR_082588"
FT VARIANT 457
FT /note="K -> N (in dbSNP:rs3740870)"
FT /id="VAR_044170"
FT VARIANT 463
FT /note="D -> N (no effect on glycine transport;
FT dbSNP:rs1805091)"
FT /evidence="ECO:0000269|PubMed:10606742"
FT /id="VAR_011592"
FT VARIANT 482
FT /note="W -> C (in HKPX3; no effect on subcellular location;
FT impairs glycine transport)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044171"
FT VARIANT 491
FT /note="Y -> C (in HKPX3; no effect on subcellular location;
FT impairs glycine transport; dbSNP:rs121908494)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044172"
FT VARIANT 499
FT /note="Y -> F (in dbSNP:rs7944684)"
FT /id="VAR_044173"
FT VARIANT 509
FT /note="N -> S (in HKPX3; compound heterozygote with V-306;
FT no effect on subcellular location; impairs glycine
FT transport; dbSNP:rs121908497)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044174"
FT VARIANT 510
FT /note="S -> R (in HKPX3; results in the formation of large
FT aggregates in the cytoplasm; impairs glycine transport;
FT dbSNP:rs281864926)"
FT /evidence="ECO:0000269|PubMed:16751771"
FT /id="VAR_044175"
FT VARIANT 632
FT /note="V -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036160"
FT VARIANT 751
FT /note="V -> A (no effect on glycine transport)"
FT /evidence="ECO:0000269|PubMed:10606742"
FT /id="VAR_011593"
FT VARIANT 767
FT /note="G -> R (in dbSNP:rs16906628)"
FT /id="VAR_044176"
FT CONFLICT 24
FT /note="G -> S (in Ref. 2; AAD27892)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="S -> G (in Ref. 2; AAD27892)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="N -> D (in Ref. 2; AAD27892)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="Q -> L (in Ref. 2; AAD27892)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="T -> S (in Ref. 2; AAD27892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 797 AA; 87434 MW; 47D8A9B179896CE0 CRC64;
MDCSAPKEMN KLPANSPEAA AAQGHPDGPC APRTSPEQEL PAAAAPPPPR VPRSASTGAQ
TFQSADARAC EAERPGVGSC KLSSPRAQAA SAALRDLREA QGAQASPPPG SSGPGNALHC
KIPFLRGPEG DANVSVGKGT LERNNTPVVG WVNMSQSTVV LATDGITSVL PGSVATVATQ
EDEQGDENKA RGNWSSKLDF ILSMVGYAVG LGNVWRFPYL AFQNGGGAFL IPYLMMLALA
GLPIFFLEVS LGQFASQGPV SVWKAIPALQ GCGIAMLIIS VLIAIYYNVI ICYTLFYLFA
SFVSVLPWGS CNNPWNTPEC KDKTKLLLDS CVISDHPKIQ IKNSTFCMTA YPNVTMVNFT
SQANKTFVSG SEEYFKYFVL KISAGIEYPG EIRWPLALCL FLAWVIVYAS LAKGIKTSGK
VVYFTATFPY VVLVILLIRG VTLPGAGAGI WYFITPKWEK LTDATVWKDA ATQIFFSLSA
AWGGLITLSS YNKFHNNCYR DTLIVTCTNS ATSIFAGFVI FSVIGFMANE RKVNIENVAD
QGPGIAFVVY PEALTRLPLS PFWAIIFFLM LLTLGLDTMF ATIETIVTSI SDEFPKYLRT
HKPVFTLGCC ICFFIMGFPM ITQGGIYMFQ LVDTYAASYA LVIIAIFELV GISYVYGLQR
FCEDIEMMIG FQPNIFWKVC WAFVTPTILT FILCFSFYQW EPMTYGSYRY PNWSMVLGWL
MLACSVIWIP IMFVIKMHLA PGRFIERLKL VCSPQPDWGP FLAQHRGERY KNMIDPLGTS
SLGLKLPVKD LELGTQC
