EAA3_HUMAN
ID EAA3_HUMAN Reviewed; 524 AA.
AC P43005; O75587; Q5VZ24; Q8N199; Q9UEW2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Excitatory amino acid transporter 3 {ECO:0000305};
DE AltName: Full=Excitatory amino-acid carrier 1;
DE AltName: Full=Neuronal and epithelial glutamate transporter;
DE AltName: Full=Sodium-dependent glutamate/aspartate transporter 3;
DE AltName: Full=Solute carrier family 1 member 1;
GN Name=SLC1A1 {ECO:0000312|HGNC:HGNC:10939};
GN Synonyms=EAAC1, EAAT3 {ECO:0000303|PubMed:7521911},
GN HEAAC1 {ECO:0000303|PubMed:7914198};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7859077; DOI=10.1016/0006-8993(94)90819-2;
RA Shashidharan P., Huntley G.W., Meyer T., Morrison J.H., Plaitakis A.;
RT "Neuron-specific human glutamate transporter: molecular cloning,
RT characterization and expression in human brain.";
RL Brain Res. 662:245-250(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7914198; DOI=10.1016/s0021-9258(17)32035-5;
RA Kanai Y., Stelzner M., Nussberger S., Khawaja S., Hebert S.C., Smith C.P.,
RA Hediger M.A.;
RT "The neuronal and epithelial human high affinity glutamate transporter.
RT Insights into structure and mechanism of transport.";
RL J. Biol. Chem. 269:20599-20606(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain cortex;
RX PubMed=7521911; DOI=10.1523/jneurosci.14-09-05559.1994;
RA Arriza J.L., Fairman W.A., Wendy A., Wadiche J.I., Murdoch G.H.,
RA Kavanaugh M.P., Amara S.G.;
RT "Functional comparisons of three glutamate transporter subtypes cloned from
RT human motor cortex.";
RL J. Neurosci. 14:5559-5569(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11317217; DOI=10.1038/sj.mp.4000806;
RA Veenstra-VanderWeele J., Kim S.J., Gonen D., Hanna G.L., Leventhal B.L.,
RA Cook E.H. Jr.;
RT "Genomic organization of the SLC1A1/EAAC1 gene and mutation screening in
RT early-onset obsessive-compulsive disorder.";
RL Mol. Psychiatry 6:160-167(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RA Yasuda-Kamatani Y.;
RT "A glutamate transporter related to EAAT3 from human brain.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 268-446.
RC TISSUE=Placenta;
RA Rome S., Mertani H.C., Lee K.O., Lobie P.E., Tome D.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8857541; DOI=10.1038/383634a0;
RA Zerangue N., Kavanaugh M.P.;
RT "Flux coupling in a neuronal glutamate transporter.";
RL Nature 383:634-637(1996).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TRANSPORTER ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26690923; DOI=10.1007/s00232-015-9863-0;
RA Abousaab A., Warsi J., Elvira B., Lang F.;
RT "Caveolin-1 Sensitivity of Excitatory Amino Acid Transporters EAAT1, EAAT2,
RT EAAT3, and EAAT4.";
RL J. Membr. Biol. 249:239-249(2016).
RN [11] {ECO:0007744|PDB:6X2L, ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E, ECO:0007744|PDB:6X3F}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.85 ANGSTROMS) IN COMPLEX WITH SODIUM
RP AND L-ASPARTATE, FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=33658209; DOI=10.1126/sciadv.abf5814;
RA Qiu B., Matthies D., Fortea E., Yu Z., Boudker O.;
RT "Cryo-EM structures of excitatory amino acid transporter 3 visualize
RT coupled substrate, sodium, and proton binding and transport.";
RL Sci. Adv. 7:0-0(2021).
RN [12]
RP INVOLVEMENT IN SCZD18.
RX PubMed=21982423; DOI=10.1016/j.biopsych.2011.08.009;
RA Melhem N., Middleton F., McFadden K., Klei L., Faraone S.V., Vinogradov S.,
RA Tiobech J., Yano V., Kuartei S., Roeder K., Byerley W., Devlin B.,
RA Myles-Worsley M.;
RT "Copy number variants for schizophrenia and related psychotic disorders in
RT Oceanic Palau: risk and transmission in extended pedigrees.";
RL Biol. Psychiatry 70:1115-1121(2011).
RN [13]
RP INVOLVEMENT IN SCZD18.
RX PubMed=23341099; DOI=10.1002/ajmg.b.32125;
RA Myles-Worsley M., Tiobech J., Browning S.R., Korn J., Goodman S.,
RA Gentile K., Melhem N., Byerley W., Faraone S.V., Middleton F.A.;
RT "Deletion at the SLC1A1 glutamate transporter gene co-segregates with
RT schizophrenia and bipolar schizoaffective disorder in a 5-generation
RT family.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 162B:87-95(2013).
RN [14]
RP VARIANTS DCBXA ILE-395 DEL AND TRP-445, CHARACTERIZATION OF VARIANTS DCBXA
RP ILE-395 DEL AND TRP-445, INVOLVEMENT IN DCBXA, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21123949; DOI=10.1172/jci44474;
RA Bailey C.G., Ryan R.M., Thoeng A.D., Ng C., King K., Vanslambrouck J.M.,
RA Auray-Blais C., Vandenberg R.J., Broer S., Rasko J.E.;
RT "Loss-of-function mutations in the glutamate transporter SLC1A1 cause human
RT dicarboxylic aminoaciduria.";
RL J. Clin. Invest. 121:446-453(2011).
CC -!- FUNCTION: Sodium-dependent, high-affinity amino acid transporter that
CC mediates the uptake of L-glutamate and also L-aspartate and D-aspartate
CC (PubMed:7914198, PubMed:7521911, PubMed:8857541, PubMed:26690923,
CC PubMed:21123949, PubMed:33658209). Can also transport L-cysteine
CC (PubMed:21123949). Functions as a symporter that transports one amino
CC acid molecule together with two or three Na(+) ions and one proton, in
CC parallel with the counter-transport of one K(+) ion (PubMed:7521911,
CC PubMed:8857541, PubMed:26690923, PubMed:33658209). Mediates Cl(-) flux
CC that is not coupled to amino acid transport; this avoids the
CC accumulation of negative charges due to aspartate and Na(+) symport
CC (PubMed:8857541, PubMed:26690923). Plays an important role in L-
CC glutamate and L-aspartate reabsorption in renal tubuli
CC (PubMed:21123949). Plays a redundant role in the rapid removal of
CC released glutamate from the synaptic cleft, which is essential for
CC terminating the postsynaptic action of glutamate (By similarity).
CC Contributes to glutathione biosynthesis and protection against
CC oxidative stress via its role in L-glutamate and L-cysteine transport
CC (By similarity). Negatively regulated by ARL6IP5 (By similarity).
CC {ECO:0000250|UniProtKB:P51906, ECO:0000250|UniProtKB:P51907,
CC ECO:0000269|PubMed:21123949, ECO:0000269|PubMed:26690923,
CC ECO:0000269|PubMed:33658209, ECO:0000269|PubMed:7521911,
CC ECO:0000269|PubMed:7914198, ECO:0000269|PubMed:8857541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29985;
CC Evidence={ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:7914198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) =
CC H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29991;
CC Evidence={ECO:0000269|PubMed:7521911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-
CC aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:29990;
CC Evidence={ECO:0000269|PubMed:7521911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=268 uM for L-glutamate (when transfected in Xenopus laevis
CC oocytes) {ECO:0000269|PubMed:26690923};
CC KM=30 uM for L-glutamate {ECO:0000269|PubMed:7914198};
CC KM=62 uM for L-glutamate {ECO:0000269|PubMed:7521911};
CC KM=47 uM for D-aspartate {ECO:0000269|PubMed:7521911};
CC KM=28 uM for L-glutamate (when transfected in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:7521911};
CC KM=47 uM for D-aspartate (when transfected in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:7521911};
CC KM=39 uM for L-aspartate (when transfected in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:33658209};
CC KM=24 uM for L-aspartate (when transfected in Xenopus laevis oocytes)
CC {ECO:0000269|PubMed:7521911};
CC -!- SUBUNIT: Homotrimer (PubMed:33658209). Interacts with ARL6IP5.
CC Interacts with RTN2 (via N-terminus); the interaction promotes cell
CC surface expression of SLC1A1. Interacts with SORCS2; this interaction
CC is important for normal expression at the cell membrane (By
CC similarity). {ECO:0000250|UniProtKB:P51906,
CC ECO:0000269|PubMed:33658209}.
CC -!- INTERACTION:
CC P43005; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-745376, EBI-781551;
CC P43005; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-745376, EBI-18304435;
CC P43005; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-745376, EBI-12175685;
CC P43005; Q5T700: LDLRAD1; NbExp=4; IntAct=EBI-745376, EBI-10173166;
CC P43005; O75459: PAGE1; NbExp=3; IntAct=EBI-745376, EBI-2559100;
CC P43005; Q99942: RNF5; NbExp=6; IntAct=EBI-745376, EBI-348482;
CC P43005; P78382: SLC35A1; NbExp=3; IntAct=EBI-745376, EBI-12870360;
CC P43005; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-745376, EBI-10273251;
CC P43005; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-745376, EBI-11724423;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21123949,
CC ECO:0000269|PubMed:26690923, ECO:0000269|PubMed:7521911,
CC ECO:0000269|PubMed:7914198, ECO:0000269|PubMed:8857541}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P43003}. Apical cell membrane
CC {ECO:0000269|PubMed:21123949}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P43003}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P51906}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P51906}. Late endosome membrane
CC {ECO:0000250|UniProtKB:P51906}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P51906}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including liver,
CC muscle, testis, ovary, retinoblastoma cell line, neurons and brain (in
CC which there was dense expression in substantia nigra, red nucleus,
CC hippocampus and in cerebral cortical layers).
CC {ECO:0000269|PubMed:7521911, ECO:0000269|PubMed:7859077,
CC ECO:0000269|PubMed:7914198}.
CC -!- DOMAIN: Contains eight transmembrane regions plus two helical hairpins
CC that dip into the membrane. These helical hairpin structures play an
CC important role in the transport process. The first enters the membrane
CC from the cytoplasmic side, the second one from the extracellular side.
CC During the transport cycle, the regions involved in amino acid
CC transport, and especially the helical hairpins, move vertically by
CC about 15-18 Angstroms, alternating between exposure to the aqueous
CC phase and reinsertion in the lipid bilayer. In contrast, the regions
CC involved in trimerization do not move. {ECO:0000250|UniProtKB:P43003}.
CC -!- PTM: Glycosylated.
CC -!- DISEASE: Dicarboxylic aminoaciduria (DCBXA) [MIM:222730]: An autosomal
CC recessive disorder characterized by abnormal excretion of urinary
CC glutamate and aspartate, resulting from the incomplete reabsorption of
CC anionic amino acids from the glomerular filtrate in the kidney. It can
CC be associated with intellectual disability.
CC {ECO:0000269|PubMed:21123949}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Schizophrenia 18 (SCZD18) [MIM:615232]: A complex,
CC multifactorial psychotic disorder or group of disorders characterized
CC by disturbances in the form and content of thought (e.g. delusions,
CC hallucinations), in mood (e.g. inappropriate affect), in sense of self
CC and relationship to the external world (e.g. loss of ego boundaries,
CC withdrawal), and in behavior (e.g bizarre or apparently purposeless
CC behavior). Although it affects emotions, it is distinguished from mood
CC disorders in which such disturbances are primary. Similarly, there may
CC be mild impairment of cognitive function, and it is distinguished from
CC the dementias in which disturbed cognitive function is considered
CC primary. Some patients manifest schizophrenic as well as bipolar
CC disorder symptoms and are often given the diagnosis of schizoaffective
CC disorder. {ECO:0000269|PubMed:21982423, ECO:0000269|PubMed:23341099}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry. A deletion at the chromosome 9p24.2
CC locus, including SLC1A1, has been identified in patients with psychotic
CC disorders (PubMed:21982423). This 84 kb deletion is immediately
CC upstream of the SLC1A1 gene in a regulatory region that contains the
CC full native promoter sequence, extends through exon 1 of the SLC1A1
CC mRNA, co-segregates with disease in an extended 5-generation pedigree
CC and increases disease risk more than 18-fold for family members
CC (PubMed:23341099). {ECO:0000269|PubMed:21982423,
CC ECO:0000269|PubMed:23341099}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. SLC1A1 subfamily. {ECO:0000305}.
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DR EMBL; U08989; AAA68628.1; -; mRNA.
DR EMBL; U06469; AAA53215.1; -; mRNA.
DR EMBL; U03506; AAA50430.1; -; mRNA.
DR EMBL; AF074911; AAC27511.3; -; Genomic_DNA.
DR EMBL; AF143773; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074903; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074904; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074905; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074906; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074907; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074908; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074909; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AF074910; AAC27511.3; JOINED; Genomic_DNA.
DR EMBL; AB008536; BAB83767.1; -; mRNA.
DR EMBL; AL162587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033040; AAH33040.1; -; mRNA.
DR EMBL; AF037982; AAC25029.1; -; mRNA.
DR CCDS; CCDS6452.1; -.
DR PIR; A54856; A54856.
DR PIR; I38433; I38433.
DR PIR; I38560; I38560.
DR RefSeq; NP_004161.4; NM_004170.5.
DR PDB; 6S3Q; EM; 3.34 A; A/B/C=1-480.
DR PDB; 6X2L; EM; 2.85 A; A/B/C=1-524.
DR PDB; 6X2Z; EM; 3.03 A; A=1-524.
DR PDB; 6X3E; EM; 3.42 A; A/B/C=1-524.
DR PDB; 6X3F; EM; 3.03 A; A/B/C=1-524.
DR PDB; 7NSG; EM; 3.34 A; A/B/C=1-480.
DR PDBsum; 6S3Q; -.
DR PDBsum; 6X2L; -.
DR PDBsum; 6X2Z; -.
DR PDBsum; 6X3E; -.
DR PDBsum; 6X3F; -.
DR PDBsum; 7NSG; -.
DR AlphaFoldDB; P43005; -.
DR SMR; P43005; -.
DR BioGRID; 112396; 197.
DR IntAct; P43005; 38.
DR STRING; 9606.ENSP00000262352; -.
DR BindingDB; P43005; -.
DR ChEMBL; CHEMBL2721; -.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00230; Pregabalin.
DR DrugCentral; P43005; -.
DR GuidetoPHARMACOLOGY; 870; -.
DR TCDB; 2.A.23.2.3; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR GlyGen; P43005; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P43005; -.
DR PhosphoSitePlus; P43005; -.
DR BioMuta; SLC1A1; -.
DR DMDM; 1352332; -.
DR EPD; P43005; -.
DR jPOST; P43005; -.
DR MassIVE; P43005; -.
DR MaxQB; P43005; -.
DR PaxDb; P43005; -.
DR PeptideAtlas; P43005; -.
DR PRIDE; P43005; -.
DR ProteomicsDB; 55571; -.
DR ABCD; P43005; 1 sequenced antibody.
DR Antibodypedia; 3650; 376 antibodies from 37 providers.
DR DNASU; 6505; -.
DR Ensembl; ENST00000262352.8; ENSP00000262352.3; ENSG00000106688.12.
DR GeneID; 6505; -.
DR KEGG; hsa:6505; -.
DR MANE-Select; ENST00000262352.8; ENSP00000262352.3; NM_004170.6; NP_004161.4.
DR UCSC; uc003zij.3; human.
DR CTD; 6505; -.
DR DisGeNET; 6505; -.
DR GeneCards; SLC1A1; -.
DR HGNC; HGNC:10939; SLC1A1.
DR HPA; ENSG00000106688; Tissue enhanced (epididymis, intestine, kidney).
DR MalaCards; SLC1A1; -.
DR MIM; 133550; gene.
DR MIM; 222730; phenotype.
DR MIM; 615232; phenotype.
DR neXtProt; NX_P43005; -.
DR OpenTargets; ENSG00000106688; -.
DR Orphanet; 2195; Dicarboxylic aminoaciduria.
DR Orphanet; 166412; Hot water reflex epilepsy.
DR PharmGKB; PA35826; -.
DR VEuPathDB; HostDB:ENSG00000106688; -.
DR eggNOG; KOG3787; Eukaryota.
DR GeneTree; ENSGT00940000155397; -.
DR HOGENOM; CLU_019375_3_2_1; -.
DR InParanoid; P43005; -.
DR OMA; YFCTTII; -.
DR OrthoDB; 1184392at2759; -.
DR PhylomeDB; P43005; -.
DR TreeFam; TF315206; -.
DR PathwayCommons; P43005; -.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-425393; Transport of inorganic cations/anions and amino acids/oligopeptides.
DR Reactome; R-HSA-5619067; Defective SLC1A1 is implicated in schizophrenia 18 (SCZD18) and dicarboxylic aminoaciduria (DCBXA).
DR SignaLink; P43005; -.
DR SIGNOR; P43005; -.
DR BioGRID-ORCS; 6505; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; SLC1A1; human.
DR GeneWiki; SLC1A1; -.
DR GenomeRNAi; 6505; -.
DR Pharos; P43005; Tchem.
DR PRO; PR:P43005; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P43005; protein.
DR Bgee; ENSG00000106688; Expressed in corpus epididymis and 166 other tissues.
DR ExpressionAtlas; P43005; baseline and differential.
DR Genevisible; P43005; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISS:ARUK-UCL.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0032279; C:asymmetric synapse; ISS:ARUK-UCL.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISS:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; ISS:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; ISS:ARUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:ARUK-UCL.
DR GO; GO:0150002; C:distal dendrite; ISS:ARUK-UCL.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; ISS:ARUK-UCL.
DR GO; GO:0099544; C:perisynaptic space; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:ARUK-UCL.
DR GO; GO:1990635; C:proximal dendrite; ISS:ARUK-UCL.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043083; C:synaptic cleft; ISS:ARUK-UCL.
DR GO; GO:0005253; F:anion channel activity; IEA:Ensembl.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0033229; F:cysteine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0140010; F:D-aspartate transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0005314; F:high-affinity L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:ARUK-UCL.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEA:Ensembl.
DR GO; GO:1903926; P:cellular response to bisphenol A; IEA:Ensembl.
DR GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl.
DR GO; GO:0071288; P:cellular response to mercury ion; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
DR GO; GO:1990708; P:conditioned place preference; IEA:Ensembl.
DR GO; GO:0042883; P:cysteine transport; IDA:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0070777; P:D-aspartate transport; IDA:ARUK-UCL.
DR GO; GO:0042417; P:dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0090461; P:glutamate homeostasis; IEA:Ensembl.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:Ensembl.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0140009; P:L-aspartate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0070778; P:L-aspartate transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0051938; P:L-glutamate import; IDA:UniProtKB.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISS:ARUK-UCL.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0061744; P:motor behavior; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; ISS:ARUK-UCL.
DR GO; GO:0098877; P:neurotransmitter receptor transport to plasma membrane; IEA:Ensembl.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
DR GO; GO:0090313; P:regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0072347; P:response to anesthetic; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0036293; P:response to decreased oxygen levels; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR GO; GO:0070633; P:transepithelial transport; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISS:ARUK-UCL.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IEA:Ensembl.
DR Gene3D; 1.10.3860.10; -; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR Pfam; PF00375; SDF; 1.
DR SUPFAM; SSF118215; SSF118215; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Cell membrane; Chloride;
KW Disease variant; Endosome; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Potassium; Reference proteome; Schizophrenia; Sodium;
KW Symport; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..524
FT /note="Excitatory amino acid transporter 3"
FT /id="PRO_0000202065"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..61
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..205
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 230..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..266
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 267..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 309..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 314..344
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 345..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..380
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 381..393
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 394..427
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 428..440
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 441..462
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P43003"
FT TOPO_DOM 463..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 98
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 102
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 331
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E"
FT BINDING 333
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E"
FT BINDING 362
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 364
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 366
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 368
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 370
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E"
FT BINDING 405
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 406
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 408
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 411
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X3E"
FT BINDING 447
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E"
FT BINDING 448
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 451
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z, ECO:0007744|PDB:6X3E"
FT BINDING 451
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT BINDING 455
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33658209,
FT ECO:0007744|PDB:6X2Z"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51906"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51906"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 27
FT /note="A -> G (in dbSNP:rs2229885)"
FT /id="VAR_023309"
FT VARIANT 50
FT /note="F -> Y (in dbSNP:rs2228621)"
FT /id="VAR_023308"
FT VARIANT 395
FT /note="Missing (in DCBXA; inhibits L-glutamate and L-
FT cysteine transport activities)"
FT /evidence="ECO:0000269|PubMed:21123949"
FT /id="VAR_071953"
FT VARIANT 445
FT /note="R -> W (in DCBXA; reduces L-glutamate and L-cysteine
FT transport activities; reduces cell membrane expression;
FT dbSNP:rs587777696)"
FT /evidence="ECO:0000269|PubMed:21123949"
FT /id="VAR_071954"
FT CONFLICT 10
FT /note="E -> PS (in Ref. 3; AAA50430)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="L -> V (in Ref. 7; AAH33040)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> V (in Ref. 1; AAA68628 and 4; AAC27511)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="V -> L (in Ref. 2; AAA53215)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="K -> N (in Ref. 2; AAA53215)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="P -> A (in Ref. 2; AAA53215)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="L -> H (in Ref. 2; AAA53215)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="R -> A (in Ref. 1; AAA68628)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="V -> G (in Ref. 8; AAC25029)"
FT /evidence="ECO:0000305"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:6S3Q"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 54..85
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 90..116
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6X2L"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6X2L"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6X2L"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 212..229
FT /evidence="ECO:0007829|PDB:6X2L"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 234..272
FT /evidence="ECO:0007829|PDB:6X2L"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 278..298
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:6X2L"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6X2Z"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:6X2L"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 368..384
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:6X2L"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6S3Q"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:6X2L"
FT HELIX 440..465
FT /evidence="ECO:0007829|PDB:6X2L"
FT TURN 468..472
FT /evidence="ECO:0007829|PDB:6X2L"
SQ SEQUENCE 524 AA; 57100 MW; FC6244ADC9EA228F CRC64;
MGKPARKGCE WKRFLKNNWV LLSTVAAVVL GITTGVLVRE HSNLSTLEKF YFAFPGEILM
RMLKLIILPL IISSMITGVA ALDSNVSGKI GLRAVVYYFC TTLIAVILGI VLVVSIKPGV
TQKVGEIART GSTPEVSTVD AMLDLIRNMF PENLVQACFQ QYKTKREEVK PPSDPEMNMT
EESFTAVMTT AISKNKTKEY KIVGMYSDGI NVLGLIVFCL VFGLVIGKMG EKGQILVDFF
NALSDATMKI VQIIMCYMPL GILFLIAGKI IEVEDWEIFR KLGLYMATVL TGLAIHSIVI
LPLIYFIVVR KNPFRFAMGM AQALLTALMI SSSSATLPVT FRCAEENNQV DKRITRFVLP
VGATINMDGT ALYEAVAAVF IAQLNDLDLG IGQIITISIT ATSASIGAAG VPQAGLVTMV
IVLSAVGLPA EDVTLIIAVD WLLDRFRTMV NVLGDAFGTG IVEKLSKKEL EQMDVSSEVN
IVNPFALEST ILDNEDSDTK KSYVNGGFAV DKSDTISFTQ TSQF
