BAT1_MOUSE
ID BAT1_MOUSE Reviewed; 487 AA.
AC Q9QXA6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=b(0,+)-type amino acid transporter 1;
DE Short=b(0,+)AT1;
DE AltName: Full=Glycoprotein-associated amino acid transporter b0,+AT1;
DE AltName: Full=Solute carrier family 7 member 9;
GN Name=Slc7a9; Synonyms=Bat1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J, and FVB/N;
RX PubMed=10588648; DOI=10.1091/mbc.10.12.4135;
RA Pfeiffer R., Loffing J., Rossier G., Bauch C., Meier C., Eggermann T.,
RA Loffing-Cueni D., Kuehn L.C., Verrey F.;
RT "Luminal heterodimeric amino acid transporter defective in cystinuria.";
RL Mol. Biol. Cell 10:4135-4147(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10799513; DOI=10.1074/jbc.275.19.14331;
RA Rajan D.P., Huang W., Kekuda R., George R.L., Wang J., Conway S.J.,
RA Devoe L.D., Leibach F.H., Prasad P.D., Ganapathy V.;
RT "Differential influence of the 4F2 heavy chain and the protein related to
RT b(0,+) amino acid transport on substrate affinity of the heteromeric b(0,+)
RT amino acid transporter.";
RL J. Biol. Chem. 275:14331-14335(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12167606; DOI=10.1152/ajprenal.00071.2002;
RA Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A., Palacin M.,
RA Chillaron J.;
RT "rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for
RT cystine in the kidney.";
RL Am. J. Physiol. 283:F540-F548(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the high-affinity, sodium-independent transport
CC of cystine and neutral and dibasic amino acids (system B(0,+)-like
CC activity). Thought to be responsible for the high-affinity reabsorption
CC of cystine in the kidney proximal tubule.
CC {ECO:0000269|PubMed:10588648}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A1. Interacts with CAV1. {ECO:0000250|UniProtKB:P82252}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000305|PubMed:12167606}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:12167606}.
CC -!- TISSUE SPECIFICITY: Expressed in the brush border membrane in the
CC kidney (at protein level). {ECO:0000269|PubMed:12167606}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; AJ249198; CAB54042.1; -; mRNA.
DR EMBL; AF192310; AAG28396.1; -; mRNA.
DR EMBL; BC010746; AAH10746.1; -; mRNA.
DR CCDS; CCDS21150.1; -.
DR RefSeq; NP_001185944.1; NM_001199015.1.
DR RefSeq; NP_001185945.1; NM_001199016.1.
DR RefSeq; NP_067266.1; NM_021291.3.
DR RefSeq; XP_006540107.1; XM_006540044.2.
DR RefSeq; XP_006540108.1; XM_006540045.2.
DR RefSeq; XP_011248893.1; XM_011250591.1.
DR RefSeq; XP_011248894.1; XM_011250592.2.
DR AlphaFoldDB; Q9QXA6; -.
DR SMR; Q9QXA6; -.
DR STRING; 10090.ENSMUSP00000032703; -.
DR PhosphoSitePlus; Q9QXA6; -.
DR PaxDb; Q9QXA6; -.
DR PRIDE; Q9QXA6; -.
DR ProteomicsDB; 277112; -.
DR Antibodypedia; 28931; 92 antibodies from 18 providers.
DR DNASU; 30962; -.
DR Ensembl; ENSMUST00000032703; ENSMUSP00000032703; ENSMUSG00000030492.
DR Ensembl; ENSMUST00000118383; ENSMUSP00000113181; ENSMUSG00000030492.
DR Ensembl; ENSMUST00000118969; ENSMUSP00000112726; ENSMUSG00000030492.
DR GeneID; 30962; -.
DR KEGG; mmu:30962; -.
DR UCSC; uc009gjw.2; mouse.
DR CTD; 11136; -.
DR MGI; MGI:1353656; Slc7a9.
DR VEuPathDB; HostDB:ENSMUSG00000030492; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000156370; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9QXA6; -.
DR OMA; HKAFGIH; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; Q9QXA6; -.
DR TreeFam; TF313355; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 30962; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ddx39; mouse.
DR PRO; PR:Q9QXA6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QXA6; protein.
DR Bgee; ENSMUSG00000030492; Expressed in small intestine Peyer's patch and 81 other tissues.
DR ExpressionAtlas; Q9QXA6; baseline and differential.
DR Genevisible; Q9QXA6; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB.
DR GO; GO:0006865; P:amino acid transport; ISO:MGI.
DR GO; GO:0015811; P:L-cystine transport; ISS:UniProtKB.
DR GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..487
FT /note="b(0,+)-type amino acid transporter 1"
FT /id="PRO_0000054259"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82252"
SQ SEQUENCE 487 AA; 53747 MW; A53F3613AA2558BF CRC64;
MEETSLRRRR EDEKSTHSTE LKTTSLQKEV GLLSGICIIV GTIIGSGIFI SPKSVLANTE
SVGPCLIIWA ACGILATLGA LCFAELGTMI TKSGGEYPYL MEAFGPIPAY LFSWTSLIVM
KPSSFAIICL SFSEYVCAAF YSGCKPPAVV VKLLAAAAIL FITTVNALSV RLGSYVQNVF
TAAKMVIVAI IIISGLVFLA QGNVKNFQNS FEGTQTSVGA ISLAFYNGLW AYDGWNQLNY
ITEELRNPYR NLPMAIVIGI PLVTVCYILM NIAYFTVMTP TELLQSQAVA VTFGDRVLYP
ASWVVPLFVA FSTIGAANGT CFTAGRLIYV AGREGHMLKV LSYISVKRLT PAPALIFYGI
IAIIYIIPGD INSLVNYFSF AAWLFYGMTI LGLVVMRFTR KDLERPIKVP LFIPIIVILV
SLFLILAPII SEPAWEYLYC VLFILSGLIF YFLFVYYKFG WAQRISRPVT KHLQMLMEVV
PPEKDPE
