Full text data of SLC1A7
SLC1A7
(EAAT5)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Excitatory amino acid transporter 5 (Retinal glutamate transporter; Solute carrier family 1 member 7)
Excitatory amino acid transporter 5 (Retinal glutamate transporter; Solute carrier family 1 member 7)
hRBCD
IPI00100081
IPI00100081 Solute carrier family 1 (Glutamate transporter), member 7 Solute carrier family 1 (Glutamate transporter), member 7 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00100081 Solute carrier family 1 (Glutamate transporter), member 7 Solute carrier family 1 (Glutamate transporter), member 7 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O00341
ID EAA5_HUMAN Reviewed; 560 AA.
AC O00341; Q5VVZ0; Q969Z8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Excitatory amino acid transporter 5;
DE AltName: Full=Retinal glutamate transporter;
DE AltName: Full=Solute carrier family 1 member 7;
GN Name=SLC1A7; Synonyms=EAAT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-537.
RC TISSUE=Retina;
RX PubMed=9108121; DOI=10.1073/pnas.94.8.4155;
RA Arriza J.L., Eliasof S., Kavanaugh M.P., Amara S.G.;
RT "Excitatory amino acid transporter 5, a retinal glutamate transporter
RT coupled to a chloride conductance.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4155-4160(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-537.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-537.
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-41.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transports L-glutamate; the L-glutamate uptake is
CC sodium- and voltage-dependent and chloride-independent. Its
CC associated chloride conductance may participate in visual
CC processing.
CC -!- SUBUNIT: Interacts with the PDZ domains of DLG4.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed primarily in retina. Detectable in
CC liver, heart, muscle and brain.
CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter
CC (TC 2.A.23) family. SLC1A7 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U76362; AAB53971.1; -; mRNA.
DR EMBL; AL445183; CAH72594.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06755.1; -; Genomic_DNA.
DR EMBL; BC012119; AAH12119.1; -; mRNA.
DR EMBL; BC017242; AAH17242.1; -; mRNA.
DR RefSeq; NP_006662.3; NM_006671.4.
DR UniGene; Hs.104637; -.
DR ProteinModelPortal; O00341; -.
DR SMR; O00341; 19-474.
DR IntAct; O00341; 1.
DR STRING; 9606.ENSP00000360549; -.
DR BindingDB; O00341; -.
DR ChEMBL; CHEMBL4390; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR GuidetoPHARMACOLOGY; 872; -.
DR TCDB; 2.A.23.2.5; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR PhosphoSite; O00341; -.
DR PaxDb; O00341; -.
DR PRIDE; O00341; -.
DR DNASU; 6512; -.
DR Ensembl; ENST00000371494; ENSP00000360549; ENSG00000162383.
DR GeneID; 6512; -.
DR KEGG; hsa:6512; -.
DR UCSC; uc001cuy.3; human.
DR CTD; 6512; -.
DR GeneCards; GC01M053552; -.
DR H-InvDB; HIX0000592; -.
DR H-InvDB; HIX0159667; -.
DR HGNC; HGNC:10945; SLC1A7.
DR HPA; HPA049124; -.
DR MIM; 604471; gene.
DR neXtProt; NX_O00341; -.
DR PharmGKB; PA35832; -.
DR eggNOG; COG1301; -.
DR HOGENOM; HOG000208776; -.
DR HOVERGEN; HBG000080; -.
DR InParanoid; O00341; -.
DR KO; K05618; -.
DR OMA; GFSIVRF; -.
DR OrthoDB; EOG7RV9G2; -.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_19419; Amino acid and oligopeptide SLC transporters.
DR GeneWiki; Excitatory_amino-acid_transporter_5; -.
DR GenomeRNAi; 6512; -.
DR NextBio; 25323; -.
DR PRO; PR:O00341; -.
DR ArrayExpress; O00341; -.
DR Bgee; O00341; -.
DR CleanEx; HS_SLC1A7; -.
DR Genevestigator; O00341; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; TAS:UniProtKB.
DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR PANTHER; PTHR11958; PTHR11958; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Glycoprotein; Membrane; Polymorphism;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 560 Excitatory amino acid transporter 5.
FT /FTId=PRO_0000202073.
FT TOPO_DOM 1 16 Cytoplasmic (Potential).
FT TRANSMEM 17 37 Helical; (Potential).
FT TRANSMEM 60 80 Helical; (Potential).
FT TRANSMEM 94 114 Helical; (Potential).
FT TOPO_DOM 115 216 Extracellular (Potential).
FT TRANSMEM 217 237 Helical; (Potential).
FT TRANSMEM 260 280 Helical; (Potential).
FT TRANSMEM 300 320 Helical; (Potential).
FT TRANSMEM 330 350 Helical; (Potential).
FT TRANSMEM 372 392 Helical; (Potential).
FT TRANSMEM 414 434 Helical; (Potential).
FT TRANSMEM 457 477 Helical; (Potential).
FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential).
FT VARIANT 41 41 R -> C (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035707.
FT VARIANT 537 537 Q -> R (in dbSNP:rs1288401).
FT /FTId=VAR_052488.
FT CONFLICT 5 5 A -> T (in Ref. 1; AAB53971).
FT CONFLICT 70 70 V -> F (in Ref. 1; AAB53971).
FT CONFLICT 244 244 A -> G (in Ref. 1; AAB53971).
FT CONFLICT 412 412 A -> G (in Ref. 1; AAB53971).
FT CONFLICT 449 449 A -> G (in Ref. 1; AAB53971).
SQ SEQUENCE 560 AA; 60658 MW; 17C527B745BB01E6 CRC64;
MVPHAILARG RDVCRRNGLL ILSVLSVIVG CLLGFFLRTR RLSPQEISYF QFPGELLMRM
LKMMILPLVV SSLMSGLASL DAKTSSRLGV LTVAYYLWTT FMAVIVGIFM VSIIHPGSAA
QKETTEQSGK PIMSSADALL DLIRNMFPAN LVEATFKQYR TKTTPVVKSP KVAPEEAPPR
RILIYGVQEE NGSHVQNFAL DLTPPPEVVY KSEPGTSDGM NVLGIVFFSA TMGIMLGRMG
DSGAPLVSFC QCLNESVMKI VAVAVWYFPF GIVFLIAGKI LEMDDPRAVG KKLGFYSVTV
VCGLVLHGLF ILPLLYFFIT KKNPIVFIRG ILQALLIALA TSSSSATLPI TFKCLLENNH
IDRRIARFVL PVGATINMDG TALYEAVAAI FIAQVNNYEL DFGQIITISI TATAASIGAA
GIPQAGLVTM VIVLTSVGLP TDDITLIIAV DWALDRFRTM INVLGDALAA GIMAHICRKD
FARDTGTEKL LPCETKPVSL QEIVAAQQNG CVKSVAEASE LTLGPTCPHH VPVQVEQDEE
LPAASLNHCT IQISELETNV
//
ID EAA5_HUMAN Reviewed; 560 AA.
AC O00341; Q5VVZ0; Q969Z8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Excitatory amino acid transporter 5;
DE AltName: Full=Retinal glutamate transporter;
DE AltName: Full=Solute carrier family 1 member 7;
GN Name=SLC1A7; Synonyms=EAAT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-537.
RC TISSUE=Retina;
RX PubMed=9108121; DOI=10.1073/pnas.94.8.4155;
RA Arriza J.L., Eliasof S., Kavanaugh M.P., Amara S.G.;
RT "Excitatory amino acid transporter 5, a retinal glutamate transporter
RT coupled to a chloride conductance.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4155-4160(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-537.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-537.
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-41.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transports L-glutamate; the L-glutamate uptake is
CC sodium- and voltage-dependent and chloride-independent. Its
CC associated chloride conductance may participate in visual
CC processing.
CC -!- SUBUNIT: Interacts with the PDZ domains of DLG4.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed primarily in retina. Detectable in
CC liver, heart, muscle and brain.
CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter
CC (TC 2.A.23) family. SLC1A7 subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U76362; AAB53971.1; -; mRNA.
DR EMBL; AL445183; CAH72594.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06755.1; -; Genomic_DNA.
DR EMBL; BC012119; AAH12119.1; -; mRNA.
DR EMBL; BC017242; AAH17242.1; -; mRNA.
DR RefSeq; NP_006662.3; NM_006671.4.
DR UniGene; Hs.104637; -.
DR ProteinModelPortal; O00341; -.
DR SMR; O00341; 19-474.
DR IntAct; O00341; 1.
DR STRING; 9606.ENSP00000360549; -.
DR BindingDB; O00341; -.
DR ChEMBL; CHEMBL4390; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR GuidetoPHARMACOLOGY; 872; -.
DR TCDB; 2.A.23.2.5; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family.
DR PhosphoSite; O00341; -.
DR PaxDb; O00341; -.
DR PRIDE; O00341; -.
DR DNASU; 6512; -.
DR Ensembl; ENST00000371494; ENSP00000360549; ENSG00000162383.
DR GeneID; 6512; -.
DR KEGG; hsa:6512; -.
DR UCSC; uc001cuy.3; human.
DR CTD; 6512; -.
DR GeneCards; GC01M053552; -.
DR H-InvDB; HIX0000592; -.
DR H-InvDB; HIX0159667; -.
DR HGNC; HGNC:10945; SLC1A7.
DR HPA; HPA049124; -.
DR MIM; 604471; gene.
DR neXtProt; NX_O00341; -.
DR PharmGKB; PA35832; -.
DR eggNOG; COG1301; -.
DR HOGENOM; HOG000208776; -.
DR HOVERGEN; HBG000080; -.
DR InParanoid; O00341; -.
DR KO; K05618; -.
DR OMA; GFSIVRF; -.
DR OrthoDB; EOG7RV9G2; -.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_19419; Amino acid and oligopeptide SLC transporters.
DR GeneWiki; Excitatory_amino-acid_transporter_5; -.
DR GenomeRNAi; 6512; -.
DR NextBio; 25323; -.
DR PRO; PR:O00341; -.
DR ArrayExpress; O00341; -.
DR Bgee; O00341; -.
DR CleanEx; HS_SLC1A7; -.
DR Genevestigator; O00341; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; TAS:UniProtKB.
DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR PANTHER; PTHR11958; PTHR11958; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Glycoprotein; Membrane; Polymorphism;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 560 Excitatory amino acid transporter 5.
FT /FTId=PRO_0000202073.
FT TOPO_DOM 1 16 Cytoplasmic (Potential).
FT TRANSMEM 17 37 Helical; (Potential).
FT TRANSMEM 60 80 Helical; (Potential).
FT TRANSMEM 94 114 Helical; (Potential).
FT TOPO_DOM 115 216 Extracellular (Potential).
FT TRANSMEM 217 237 Helical; (Potential).
FT TRANSMEM 260 280 Helical; (Potential).
FT TRANSMEM 300 320 Helical; (Potential).
FT TRANSMEM 330 350 Helical; (Potential).
FT TRANSMEM 372 392 Helical; (Potential).
FT TRANSMEM 414 434 Helical; (Potential).
FT TRANSMEM 457 477 Helical; (Potential).
FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential).
FT VARIANT 41 41 R -> C (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_035707.
FT VARIANT 537 537 Q -> R (in dbSNP:rs1288401).
FT /FTId=VAR_052488.
FT CONFLICT 5 5 A -> T (in Ref. 1; AAB53971).
FT CONFLICT 70 70 V -> F (in Ref. 1; AAB53971).
FT CONFLICT 244 244 A -> G (in Ref. 1; AAB53971).
FT CONFLICT 412 412 A -> G (in Ref. 1; AAB53971).
FT CONFLICT 449 449 A -> G (in Ref. 1; AAB53971).
SQ SEQUENCE 560 AA; 60658 MW; 17C527B745BB01E6 CRC64;
MVPHAILARG RDVCRRNGLL ILSVLSVIVG CLLGFFLRTR RLSPQEISYF QFPGELLMRM
LKMMILPLVV SSLMSGLASL DAKTSSRLGV LTVAYYLWTT FMAVIVGIFM VSIIHPGSAA
QKETTEQSGK PIMSSADALL DLIRNMFPAN LVEATFKQYR TKTTPVVKSP KVAPEEAPPR
RILIYGVQEE NGSHVQNFAL DLTPPPEVVY KSEPGTSDGM NVLGIVFFSA TMGIMLGRMG
DSGAPLVSFC QCLNESVMKI VAVAVWYFPF GIVFLIAGKI LEMDDPRAVG KKLGFYSVTV
VCGLVLHGLF ILPLLYFFIT KKNPIVFIRG ILQALLIALA TSSSSATLPI TFKCLLENNH
IDRRIARFVL PVGATINMDG TALYEAVAAI FIAQVNNYEL DFGQIITISI TATAASIGAA
GIPQAGLVTM VIVLTSVGLP TDDITLIIAV DWALDRFRTM INVLGDALAA GIMAHICRKD
FARDTGTEKL LPCETKPVSL QEIVAAQQNG CVKSVAEASE LTLGPTCPHH VPVQVEQDEE
LPAASLNHCT IQISELETNV
//
MIM
604471
*RECORD*
*FIELD* NO
604471
*FIELD* TI
*604471 SOLUTE CARRIER FAMILY 1 (GLUTAMATE TRANSPORTER), MEMBER 7; SLC1A7
;;EXCITATORY AMINO ACID TRANSPORTER 5; EAAT5;;
read moreGLUTAMATE TRANSPORTER, RETINA
*FIELD* TX
The uptake of glutamate and other excitatory amino acids is mediated by
a family of high-affinity sodium-dependent transporters, the excitatory
amino acid transporters (EAATs). The transport of glutamate is driven by
the cotransport of sodium ions and the countertransport of potassium
ions down their electrochemical gradients, and studies have suggested
that this complex process involves the cotransport of protons as well.
In addition to these transport currents, an uncoupled passive flux of
chloride ions has been detected. The relative magnitude of this
associated chloride conductance varies with each transporter subtype. A
glutamate-dependent current that has a transporter-like pharmacology is
carried largely by chloride ions in retinal cone and rod photoreceptors
and bipolar cells. By screening a human retina cDNA library with a
salamander retina cDNA encoding a glutamate transporter associated with
a large chloride conductance, Arriza et al. (1997) identified SLC1A7,
which they called EAAT5. They isolated an EAAT5 cDNA encoding a deduced
560-amino acid protein containing 8 putative transmembrane domains and a
single potential N-linked glycosylation site in the putative large
extracellular loop. Although EAAT5 shares the structural homologies of
the EAAT family, 1 novel feature of the EAAT5 sequence is a C-terminal
motif previously identified in N-methyl-D-aspartate receptors and
potassium channels and shown to confer interactions with a family of
synaptic proteins that promote ion channel clustering. EAAT5 has 46%
amino acid sequence identity with EAAT1 (SLC1A3; 600111), 43% identity
with EAAT4 (SLC1A6; 600637), 37% identity with EAAT3 (SLC1A1; 133550),
and 36% identity with EAAT2 (SLC1A2; 600300). Arriza et al. (1997)
measured the functional properties of EAAT5 in a Xenopus oocyte
expression system by measuring radiolabeled glutamate flux and
2-electrode voltage clamp recording. EAAT5-mediated L-glutamate uptake
was sodium- and voltage-dependent and chloride-independent. Transporter
currents elicited by glutamate were also sodium- and voltage-dependent,
but ion substitution experiments suggested that this current was largely
carried by chloride ions. Northern blot analysis of 8 human tissues
detected a major 3.1-kb EAAT5 transcript that was abundantly expressed
only in retina. Arriza et al. (1997) concluded that the properties of
EAAT5 are similar to the glutamate-elicited chloride conductances
described in retinal neurons, suggesting that the EAAT5-associated
chloride conductance may participate in visual processing.
*FIELD* RF
1. Arriza, J. L.; Eliasof, S.; Kavanaugh, M. P.; Amara, S. G.: Excitatory
amino acid transporter 5, a retinal glutamate transporter coupled
to a chloride conductance. Proc. Nat. Acad. Sci. 94: 4155-4160,
1997.
*FIELD* CD
Patti M. Sherman: 1/27/2000
*FIELD* ED
carol: 03/08/2002
terry: 3/8/2002
mgross: 1/31/2000
psherman: 1/28/2000
*RECORD*
*FIELD* NO
604471
*FIELD* TI
*604471 SOLUTE CARRIER FAMILY 1 (GLUTAMATE TRANSPORTER), MEMBER 7; SLC1A7
;;EXCITATORY AMINO ACID TRANSPORTER 5; EAAT5;;
read moreGLUTAMATE TRANSPORTER, RETINA
*FIELD* TX
The uptake of glutamate and other excitatory amino acids is mediated by
a family of high-affinity sodium-dependent transporters, the excitatory
amino acid transporters (EAATs). The transport of glutamate is driven by
the cotransport of sodium ions and the countertransport of potassium
ions down their electrochemical gradients, and studies have suggested
that this complex process involves the cotransport of protons as well.
In addition to these transport currents, an uncoupled passive flux of
chloride ions has been detected. The relative magnitude of this
associated chloride conductance varies with each transporter subtype. A
glutamate-dependent current that has a transporter-like pharmacology is
carried largely by chloride ions in retinal cone and rod photoreceptors
and bipolar cells. By screening a human retina cDNA library with a
salamander retina cDNA encoding a glutamate transporter associated with
a large chloride conductance, Arriza et al. (1997) identified SLC1A7,
which they called EAAT5. They isolated an EAAT5 cDNA encoding a deduced
560-amino acid protein containing 8 putative transmembrane domains and a
single potential N-linked glycosylation site in the putative large
extracellular loop. Although EAAT5 shares the structural homologies of
the EAAT family, 1 novel feature of the EAAT5 sequence is a C-terminal
motif previously identified in N-methyl-D-aspartate receptors and
potassium channels and shown to confer interactions with a family of
synaptic proteins that promote ion channel clustering. EAAT5 has 46%
amino acid sequence identity with EAAT1 (SLC1A3; 600111), 43% identity
with EAAT4 (SLC1A6; 600637), 37% identity with EAAT3 (SLC1A1; 133550),
and 36% identity with EAAT2 (SLC1A2; 600300). Arriza et al. (1997)
measured the functional properties of EAAT5 in a Xenopus oocyte
expression system by measuring radiolabeled glutamate flux and
2-electrode voltage clamp recording. EAAT5-mediated L-glutamate uptake
was sodium- and voltage-dependent and chloride-independent. Transporter
currents elicited by glutamate were also sodium- and voltage-dependent,
but ion substitution experiments suggested that this current was largely
carried by chloride ions. Northern blot analysis of 8 human tissues
detected a major 3.1-kb EAAT5 transcript that was abundantly expressed
only in retina. Arriza et al. (1997) concluded that the properties of
EAAT5 are similar to the glutamate-elicited chloride conductances
described in retinal neurons, suggesting that the EAAT5-associated
chloride conductance may participate in visual processing.
*FIELD* RF
1. Arriza, J. L.; Eliasof, S.; Kavanaugh, M. P.; Amara, S. G.: Excitatory
amino acid transporter 5, a retinal glutamate transporter coupled
to a chloride conductance. Proc. Nat. Acad. Sci. 94: 4155-4160,
1997.
*FIELD* CD
Patti M. Sherman: 1/27/2000
*FIELD* ED
carol: 03/08/2002
terry: 3/8/2002
mgross: 1/31/2000
psherman: 1/28/2000