VIAAT_XENTR
ID VIAAT_XENTR Reviewed; 518 AA.
AC Q6DIV6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Vesicular inhibitory amino acid transporter {ECO:0000250|UniProtKB:Q9H598};
DE AltName: Full=GABA and glycine transporter;
DE AltName: Full=Solute carrier family 32 member 1;
DE AltName: Full=Vesicular GABA transporter;
GN Name=slc32a1 {ECO:0000312|EMBL:AAH75429.1};
GN Synonyms=viaat {ECO:0000250|UniProtKB:Q6PF45};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH75429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=F6 {ECO:0000312|EMBL:AAH75429.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Antiporter that exchanges vesicular protons for cytosolic 4-
CC aminobutanoate or to a lesser extend glycine, thus allowing their
CC secretion from nerve terminals. The transport is equally dependent on
CC the chemical and electrical components of the proton gradient (By
CC similarity). May also transport beta-alanine (By similarity).
CC Acidification of GABAergic synaptic vesicles is a prerequisite for 4-
CC aminobutanoate uptake (By similarity). {ECO:0000250|UniProtKB:O35458,
CC ECO:0000250|UniProtKB:O35633}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(out) + n H(+)(in) = 4-aminobutanoate(in) + n
CC H(+)(out); Xref=Rhea:RHEA:70979, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:O35633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(out) + n H(+)(in) = glycine(in) + n H(+)(out);
CC Xref=Rhea:RHEA:70983, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000250|UniProtKB:O35633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(out) + n H(+)(in) = beta-alanine(in) + n
CC H(+)(out); Xref=Rhea:RHEA:70987, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57966; Evidence={ECO:0000250|UniProtKB:O35458};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:O35458}; Multi-pass membrane protein
CC {ECO:0000255}. Presynapse {ECO:0000250|UniProtKB:O35633}. Note=Presents
CC in glycine-, GABA- or GABA- and glycine-containing boutons.
CC {ECO:0000250|UniProtKB:O35458}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000255}.
CC -!- CAUTION: Juge et al. shows that SLC32A1 is a symporter of both 4-
CC aminobutanoate or glycine or beta-alanine with Cl(-) that operates
CC according an electrical gradient without the need for a chemical
CC gradient (By similarity). However Farsi et al. and Egashira et al.
CC confirm that SLC32A1 is an antiporter that exchanges vesicular protons
CC for cytosolic 4-aminobutanoate or glycine and exclude any coupling with
CC chloride (By similarity). {ECO:0000250|UniProtKB:O35458,
CC ECO:0000250|UniProtKB:O35633}.
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DR EMBL; BC075429; AAH75429.1; -; mRNA.
DR RefSeq; NP_001004943.1; NM_001004943.1.
DR RefSeq; XP_012827085.1; XM_012971631.2.
DR RefSeq; XP_012827086.1; XM_012971632.2.
DR AlphaFoldDB; Q6DIV6; -.
DR SMR; Q6DIV6; -.
DR STRING; 8364.ENSXETP00000054324; -.
DR PaxDb; Q6DIV6; -.
DR DNASU; 448348; -.
DR Ensembl; ENSXETT00000054324; ENSXETP00000054324; ENSXETG00000025497.
DR GeneID; 448348; -.
DR KEGG; xtr:448348; -.
DR CTD; 140679; -.
DR Xenbase; XB-GENE-489830; slc32a1.
DR eggNOG; KOG4303; Eukaryota.
DR HOGENOM; CLU_036432_0_0_1; -.
DR InParanoid; Q6DIV6; -.
DR OMA; SDANDEH; -.
DR OrthoDB; 570025at2759; -.
DR PhylomeDB; Q6DIV6; -.
DR TreeFam; TF312818; -.
DR Reactome; R-XTR-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR Reactome; R-XTR-888590; GABA synthesis, release, reuptake and degradation.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025497; Expressed in brain and 2 other tissues.
DR GO; GO:0044292; C:dendrite terminus; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0044306; C:neuron projection terminus; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015495; F:gamma-aminobutyric acid:proton symporter activity; IBA:GO_Central.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0051939; P:gamma-aminobutyric acid import; ISS:UniProtKB.
DR GO; GO:0015812; P:gamma-aminobutyric acid transport; ISS:UniProtKB.
DR GO; GO:0015816; P:glycine transport; ISS:UniProtKB.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasmic vesicle; Membrane; Neurotransmitter transport;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="Vesicular inhibitory amino acid transporter"
FT /id="PRO_0000341536"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..197
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..298
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..376
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..454
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..518
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT REGION 66..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 57156 MW; 1B0B04020851C78B CRC64;
MATLIRSKLS NVATSVSNKS QAKVSGMFAR MGFQAATDEE ALGFAHCDDL DMEHRQGLQM
DILKTEVPSG DPTAEGDSHY QRDGTGPPSS ASKDEGLCSE LSSYGKPKIT AWEAGWNVTN
AIQGMFVLGL PYAILHGGYL GLFLIIFAAV VCCYTGKILI ACLYEENEDG ETVRVRDSYV
DIANACCAPR FPKLGGRVVN VAQIIELVMT CILYVVVSGN LMYNSFPSLP ISQKSWSIIA
TAMLLPCAFL KNLKAVSKFS LLCTLAHFVI NVLVIAYCLS RARDWAWDKV KFYIDVKKFP
ISIGIIVFSY TSQIFLPSLE GNMQSPKEFH CMMNWTHIAA CILKGLFALV AYLTWADETK
EVITDNLPST IRAVVNLFLV AKALLSYPLP FFAAVEVLEK SLFQEGARAF FPNCYGGDGR
LKSWGLTLRC ALVVFTLLMA IYVPHFALLM GLTGSLTGAG LCFLLPSLFH LKLLWRKLQW
HQVFFDVSIF VIGSICSVSG FVHSLEGLIE AFRFNIED
