S6A13_HUMAN
ID S6A13_HUMAN Reviewed; 602 AA.
AC Q9NSD5; B4DJL1; Q8TCC2; Q8WW56;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Sodium- and chloride-dependent GABA transporter 2;
DE Short=GAT-2;
DE AltName: Full=Solute carrier family 6 member 13;
GN Name=SLC6A13; Synonyms=GAT2;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11824941; DOI=10.1139/y01-082;
RA Gong Y., Zhang M., Cui L., Minuk G.Y.;
RT "Sequence and chromosomal assignment of a human novel cDNA: similarity to
RT gamma-aminobutyric acid transporter.";
RL Can. J. Physiol. Pharmacol. 79:977-984(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, TRANSPORTER ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=17502375; DOI=10.1074/jbc.m702111200;
RA Christiansen B., Meinild A.-K., Jensen A.A., Braeuner-Osborne H.;
RT "Cloning and characterization of a functional human gamma-aminobutyric acid
RT (GABA) transporter, human GAT-2.";
RL J. Biol. Chem. 282:19331-19341(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Kidney;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-48; GLY-51 AND VAL-132,
RP TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22932902; DOI=10.1074/jbc.m112.388157;
RA Schlessinger A., Wittwer M.B., Dahlin A., Khuri N., Bonomi M., Fan H.,
RA Giacomini K.M., Sali A.;
RT "High selectivity of the gamma-aminobutyric acid transporter 2 (GAT-2,
RT SLC6A13) revealed by structure-based approach.";
RL J. Biol. Chem. 287:37745-37756(2012).
CC -!- FUNCTION: Mediates sodium- and chloride-dependent transport of gamma-
CC aminobutyric acid (GABA) (PubMed:17502375, PubMed:22932902). Mediates
CC transport of beta-alanine (PubMed:17502375). Can also mediate transport
CC of taurine and hypotaurine (By similarity).
CC {ECO:0000250|UniProtKB:P31649, ECO:0000269|PubMed:17502375,
CC ECO:0000269|PubMed:22932902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:17502375,
CC ECO:0000269|PubMed:22932902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC Evidence={ECO:0000305|PubMed:17502375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + 2 Na(+)(out) + taurine(out) = chloride(in) + 2
CC Na(+)(in) + taurine(in); Xref=Rhea:RHEA:71223, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:P31649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71224;
CC Evidence={ECO:0000250|UniProtKB:P31649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(out) + chloride(out) + 2 Na(+)(out) = beta-
CC alanine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71247,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000269|PubMed:17502375};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71248;
CC Evidence={ECO:0000305|PubMed:17502375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC Evidence={ECO:0000250|UniProtKB:P31649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC Evidence={ECO:0000250|UniProtKB:P31649};
CC -!- ACTIVITY REGULATION: GABA transport is inhibited by beta-alanine, 2,3-
CC diaminopropionic acid and SNAP-5114. {ECO:0000269|PubMed:17502375}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.24 uM for GABA {ECO:0000269|PubMed:17502375};
CC KM=26.2 uM for GABA {ECO:0000269|PubMed:22932902};
CC Vmax=0.39 pmol/min/ug enzyme for GABA {ECO:0000269|PubMed:22932902};
CC -!- INTERACTION:
CC Q9NSD5-3; Q92870-2: APBB2; NbExp=3; IntAct=EBI-25831241, EBI-21535880;
CC Q9NSD5-3; P54253: ATXN1; NbExp=6; IntAct=EBI-25831241, EBI-930964;
CC Q9NSD5-3; P22607: FGFR3; NbExp=3; IntAct=EBI-25831241, EBI-348399;
CC Q9NSD5-3; P04792: HSPB1; NbExp=3; IntAct=EBI-25831241, EBI-352682;
CC Q9NSD5-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25831241, EBI-10975473;
CC Q9NSD5-3; P49810: PSEN2; NbExp=3; IntAct=EBI-25831241, EBI-2010251;
CC Q9NSD5-3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25831241, EBI-396669;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22932902};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P31649}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NSD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSD5-2; Sequence=VSP_043070;
CC Name=3;
CC IsoId=Q9NSD5-3; Sequence=VSP_044887, VSP_044888;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, lung, liver and testis.
CC {ECO:0000269|PubMed:11824941, ECO:0000269|PubMed:17502375}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A13 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64247.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U76343; AAF64247.1; ALT_FRAME; mRNA.
DR EMBL; AK296127; BAG58873.1; -; mRNA.
DR EMBL; AF462445; AAP97713.1; -; mRNA.
DR EMBL; AK313511; BAG36291.1; -; mRNA.
DR EMBL; AC007406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88974.1; -; Genomic_DNA.
DR EMBL; BC020867; AAH20867.1; -; mRNA.
DR EMBL; BC022392; AAH22392.1; -; mRNA.
DR CCDS; CCDS53729.1; -. [Q9NSD5-2]
DR CCDS; CCDS58198.1; -. [Q9NSD5-3]
DR CCDS; CCDS8502.1; -. [Q9NSD5-1]
DR RefSeq; NP_001177926.1; NM_001190997.2. [Q9NSD5-2]
DR RefSeq; NP_001230321.1; NM_001243392.1. [Q9NSD5-3]
DR RefSeq; NP_057699.2; NM_016615.4. [Q9NSD5-1]
DR AlphaFoldDB; Q9NSD5; -.
DR SMR; Q9NSD5; -.
DR BioGRID; 112431; 3.
DR IntAct; Q9NSD5; 7.
DR STRING; 9606.ENSP00000339260; -.
DR BindingDB; Q9NSD5; -.
DR ChEMBL; CHEMBL4535; -.
DR DrugBank; DB08848; Guvacine.
DR TCDB; 2.A.22.3.10; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9NSD5; 2 sites.
DR iPTMnet; Q9NSD5; -.
DR PhosphoSitePlus; Q9NSD5; -.
DR BioMuta; SLC6A13; -.
DR DMDM; 209572724; -.
DR jPOST; Q9NSD5; -.
DR MassIVE; Q9NSD5; -.
DR MaxQB; Q9NSD5; -.
DR PaxDb; Q9NSD5; -.
DR PeptideAtlas; Q9NSD5; -.
DR PRIDE; Q9NSD5; -.
DR ProteomicsDB; 74864; -.
DR ProteomicsDB; 82535; -. [Q9NSD5-1]
DR ProteomicsDB; 82536; -. [Q9NSD5-2]
DR Antibodypedia; 62641; 87 antibodies from 18 providers.
DR DNASU; 6540; -.
DR Ensembl; ENST00000343164.9; ENSP00000339260.4; ENSG00000010379.16. [Q9NSD5-1]
DR Ensembl; ENST00000436453.1; ENSP00000389316.1; ENSG00000010379.16. [Q9NSD5-3]
DR Ensembl; ENST00000445055.6; ENSP00000407104.2; ENSG00000010379.16. [Q9NSD5-2]
DR GeneID; 6540; -.
DR KEGG; hsa:6540; -.
DR MANE-Select; ENST00000343164.9; ENSP00000339260.4; NM_016615.5; NP_057699.2.
DR UCSC; uc001qic.3; human. [Q9NSD5-1]
DR CTD; 6540; -.
DR DisGeNET; 6540; -.
DR GeneCards; SLC6A13; -.
DR HGNC; HGNC:11046; SLC6A13.
DR HPA; ENSG00000010379; Tissue enriched (kidney).
DR MIM; 615097; gene.
DR neXtProt; NX_Q9NSD5; -.
DR OpenTargets; ENSG00000010379; -.
DR PharmGKB; PA35909; -.
DR VEuPathDB; HostDB:ENSG00000010379; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000157478; -.
DR HOGENOM; CLU_006855_9_1_1; -.
DR InParanoid; Q9NSD5; -.
DR OMA; TIWFVSR; -.
DR OrthoDB; 1609941at2759; -.
DR PhylomeDB; Q9NSD5; -.
DR TreeFam; TF343812; -.
DR PathwayCommons; Q9NSD5; -.
DR Reactome; R-HSA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-HSA-888593; Reuptake of GABA.
DR SABIO-RK; Q9NSD5; -.
DR SignaLink; Q9NSD5; -.
DR SIGNOR; Q9NSD5; -.
DR BioGRID-ORCS; 6540; 8 hits in 1063 CRISPR screens.
DR GenomeRNAi; 6540; -.
DR Pharos; Q9NSD5; Tchem.
DR PRO; PR:Q9NSD5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NSD5; protein.
DR Bgee; ENSG00000010379; Expressed in pigmented layer of retina and 149 other tissues.
DR ExpressionAtlas; Q9NSD5; baseline and differential.
DR Genevisible; Q9NSD5; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0005308; F:creatine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005368; F:taurine transmembrane transporter activity; ISS:ARUK-UCL.
DR GO; GO:0005369; F:taurine:sodium symporter activity; IEA:Ensembl.
DR GO; GO:0089718; P:amino acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015881; P:creatine transmembrane transport; ISS:ARUK-UCL.
DR GO; GO:0051939; P:gamma-aminobutyric acid import; ISS:ARUK-UCL.
DR GO; GO:0051936; P:gamma-aminobutyric acid reuptake; TAS:Reactome.
DR GO; GO:0015718; P:monocarboxylic acid transport; IDA:ARUK-UCL.
DR GO; GO:0071705; P:nitrogen compound transport; IDA:ARUK-UCL.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IDA:ARUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0015734; P:taurine transport; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002981; Na/ntran_symport_GABA_GAT2.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR01196; GAT2TRNSPORT.
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; Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="Sodium- and chloride-dependent GABA transporter 2"
FT /id="PRO_0000214792"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 587
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31649"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31649"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 153..162
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT VAR_SEQ 68..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043070"
FT VAR_SEQ 69..97
FT /note="AFFIPYLVFLFTCGIPVFLLETALGQYTS -> EMRALVPPHPLLEGGYFHL
FT LHLRPLWGVP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_044887"
FT VAR_SEQ 98..602
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_044888"
FT VARIANT 426
FT /note="V -> I (in dbSNP:rs577294)"
FT /id="VAR_011594"
FT MUTAGEN 48
FT /note="E->A: 50% reduction of GABA-uptake."
FT /evidence="ECO:0000269|PubMed:22932902"
FT MUTAGEN 48
FT /note="E->L,Y: 90% reduction of GABA-uptake."
FT /evidence="ECO:0000269|PubMed:22932902"
FT MUTAGEN 51
FT /note="G->A,L: Complete loss of GABA-uptake."
FT /evidence="ECO:0000269|PubMed:22932902"
FT MUTAGEN 132
FT /note="V->I: Complete loss of GABA-uptake."
FT /evidence="ECO:0000269|PubMed:22932902"
FT CONFLICT 19..36
FT /note="Missing (in Ref. 1; AAF64247)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="N -> H (in Ref. 1; AAF64247)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..321
FT /note="Missing (in Ref. 1; AAF64247)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="L -> P (in Ref. 1; AAF64247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 68009 MW; 3BA3AB4BABBDC980 CRC64;
MDSRVSGTTS NGETKPVYPV MEKKEEDGTL ERGHWNNKME FVLSVAGEII GLGNVWRFPY
LCYKNGGGAF FIPYLVFLFT CGIPVFLLET ALGQYTSQGG VTAWRKICPI FEGIGYASQM
IVILLNVYYI IVLAWALFYL FSSFTIDLPW GGCYHEWNTE HCMEFQKTNG SLNGTSENAT
SPVIEFWERR VLKISDGIQH LGALRWELAL CLLLAWVICY FCIWKGVKST GKVVYFTATF
PYLMLVVLLI RGVTLPGAAQ GIQFYLYPNL TRLWDPQVWM DAGTQIFFSF AICLGCLTAL
GSYNKYHNNC YRDCIALCFL NSGTSFVAGF AIFSILGFMS QEQGVPISEV AESGPGLAFI
AYPRAVVMLP FSPLWACCFF FMVVLLGLDS QFVCVESLVT ALVDMYPHVF RKKNRREVLI
LGVSVVSFLV GLIMLTEGGM YVFQLFDYYA ASGMCLLFVA IFESLCVAWV YGAKRFYDNI
EDMIGYRPWP LIKYCWLFLT PAVCTATFLF SLIKYTPLTY NKKYTYPWWG DALGWLLALS
SMVCIPAWSL YRLGTLKGPF RERIRQLMCP AEDLPQRNPA GPSAPATPRT SLLRLTELES
HC
