VIAAT_MACFA
ID VIAAT_MACFA Reviewed; 525 AA.
AC Q95KE2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
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:0000250|UniProtKB:Q9H598}; Synonyms=VGAT, VIAAT;
GN ORFNames=QccE-21148;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUN-2001) 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:0000305}.
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; AB062931; BAB60726.1; -; mRNA.
DR RefSeq; NP_001272325.1; NM_001285396.1.
DR AlphaFoldDB; Q95KE2; -.
DR SMR; Q95KE2; -.
DR STRING; 9541.XP_005569052.1; -.
DR Ensembl; ENSMFAT00000009354; ENSMFAP00000035119; ENSMFAG00000004019.
DR GeneID; 102130972; -.
DR CTD; 140679; -.
DR VEuPathDB; HostDB:ENSMFAG00000004019; -.
DR eggNOG; KOG4303; Eukaryota.
DR GeneTree; ENSGT00490000043380; -.
DR OMA; KTFFQDG; -.
DR OrthoDB; 570025at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR Bgee; ENSMFAG00000004019; Expressed in frontal cortex and 2 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0051286; C:cell tip; IEA:Ensembl.
DR GO; GO:0044316; C:cone cell pedicle; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044292; C:dendrite terminus; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
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:0015495; F:gamma-aminobutyric acid:proton symporter activity; IEA:Ensembl.
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 Nitration; Reference proteome; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..525
FT /note="Vesicular inhibitory amino acid transporter"
FT /id="PRO_0000093821"
FT TOPO_DOM 1..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..204
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..305
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..383
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..461
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..525
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000250|UniProtKB:O35458"
FT REGION 69..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35633"
SQ SEQUENCE 525 AA; 57393 MW; 2CF17504CB2FD1C9 CRC64;
MATLLRSKLS NVATSVSNKS QAKVSGMFAR MGFQAATDEE AVGFAHCDDL DFEHRQGLQM
DILKAEGEPC GDEGAEPPVE GDIHYQRGSG APLPPSGSKD QVGAGGEFGG HDKPKITAWE
AGWNVTNAIQ GMFVLGLPYA ILHGGYLGLF LIIFAAVVCC YTGKILIACL YEENEDGEVV
RVRDSYVAIA NACCAPRFPT LGGRVVNVAQ IIELVMTCIL YVVVSGNLMY NSFPGLPVSQ
KSWSIIATAV LLPCAFLKNL KAVSKFSLLC TLAHFVINIL VIAYCLSRAR DWAWEKVKFY
IDVKKFPISI GIIVFSYTSQ IFLPSLEGNM QQPSEFHCMM NWTHIAACVL KGLFALVAYL
TWADETKEVI TDNLPGSIRA VVNIFLVAKA LLSYPLPFFA AVEVLEKSLF QEGSRAFFPA
CYGGDGRLKS WGLTLRCALV VFTLLMAIYV PHFALLMGLT GSLTGAGLCF LLPSLFHLRL
LWRKLLWHQV FFDVAIFVIG GICSVSGFVH SLEGLIEAYR TNAED
