VIAAT_XENLA
ID VIAAT_XENLA Reviewed; 518 AA.
AC Q6PF45;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
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;
DE Short=xVIAAT;
GN Name=slc32a1 {ECO:0000250|UniProtKB:Q9H598};
GN Synonyms=viaat {ECO:0000303|PubMed:18262473};
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:0000312|EMBL:AAH57733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH57733.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
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: 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 -!- TISSUE SPECIFICITY: Initially expressed in late neurula stages in the
CC anterior spinal cord. By early tailbud stages, expression extends
CC posteriorly along the entire developing spinal cord and appears in the
CC hindbrain. In late tailbud embryos, expressed in the forebrain,
CC midbrain, hindbrain, spinal cord and retina. In swimming tadpoles,
CC expressed in an extended and more intense pattern including
CC interneurons. {ECO:0000269|PubMed:18262473}.
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; BC057733; AAH57733.1; -; mRNA.
DR RefSeq; NP_001079961.1; NM_001086492.1.
DR AlphaFoldDB; Q6PF45; -.
DR SMR; Q6PF45; -.
DR DNASU; 379652; -.
DR GeneID; 379652; -.
DR KEGG; xla:379652; -.
DR CTD; 379652; -.
DR Xenbase; XB-GENE-865905; slc32a1.S.
DR OMA; KTFFQDG; -.
DR OrthoDB; 570025at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 379652; Expressed in brain and 2 other tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; ISS:UniProtKB.
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:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
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_0000341535"
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"
SQ SEQUENCE 518 AA; 57191 MW; 0DE19ED16BD84C0D CRC64;
MATLIRSKLS NVATSVSNKS QAKVSGMFAR MGFQAATDEE ALGFAHCDDL DTEHRQGLQM
DILKTEVPTG DAPPEGDIHY QRDGTGLPPS ASKDEGLCSE LSSSEKPQIT AWEAGWNVTN
AIQGMFVLGL PYAILHGGYL GLFLIIFAAV VCCYTGKILI ACLYEENEDG ETVRVRDSYV
DIANACCAPR FPKLGGRVVN VAQIIELVMT CILYVVVSGN LMYNSFPNLP ISQKSWSIMA
TAVLLPCAFL KNLKAVSKFS LLCTVAHFVI NILVIAYCLS RARDWAWDKV KFYIDVKKFP
ISIGIIVFSY TSQIFLPSLE GNMQSPREFH CMMNWTHIAA CILKGLFALV AYLTWADETK
EVITDNLPST IRAVVNLFLV SKALLSYPLP FFAAVEVLEK SLFQEGARAF FPNCYGGDGR
LKSWGLTLRC ALVVFTLLMA IYVPHFALLM GLTGSLTGAG LCFLLPSLFH LKLMWRQLLW
HQVFFDVSIF VIGSICSVSG FVHSLEGLIE AYAYNIED
