BAT1_RABIT
ID BAT1_RABIT Reviewed; 487 AA.
AC Q9N1R6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=b(0,+)-type amino acid transporter 1;
DE Short=b(0,+)AT;
DE AltName: Full=4F2-LC6;
DE AltName: Full=Glycoprotein-associated amino acid transporter b0,+AT1;
DE AltName: Full=Solute carrier family 7 member 9;
GN Name=SLC7A9 {ECO:0000250|UniProtKB:P82251};
GN Synonyms=BAT1 {ECO:0000250|UniProtKB:P82251};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF26216.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Intestine {ECO:0000269|PubMed:10506149};
RX PubMed=10506149; DOI=10.1074/jbc.274.41.29005;
RA Rajan D.P., Kekuda R., Huang W., Wang H., Devoe L.D., Leibach F.H.,
RA Prasad P.D., Ganapathy V.;
RT "Cloning and expression of a b(0,+)-like amino acid transporter functioning
RT as a heterodimer with 4F2hc instead of rBAT. A new candidate gene for
RT cystinuria.";
RL J. Biol. Chem. 274:29005-29010(1999).
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 tubule. {ECO:0000269|PubMed:10506149}.
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:0000250|UniProtKB:P82251}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P82251}.
CC -!- TISSUE SPECIFICITY: Kidney and small intestine.
CC {ECO:0000269|PubMed:10506149}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000255}.
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DR EMBL; AF155119; AAF26216.1; -; mRNA.
DR RefSeq; NP_001075530.1; NM_001082061.1.
DR AlphaFoldDB; Q9N1R6; -.
DR SMR; Q9N1R6; -.
DR STRING; 9986.ENSOCUP00000004768; -.
DR PRIDE; Q9N1R6; -.
DR GeneID; 100008729; -.
DR KEGG; ocu:100008729; -.
DR CTD; 11136; -.
DR eggNOG; KOG1287; Eukaryota.
DR InParanoid; Q9N1R6; -.
DR OrthoDB; 621852at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; IPI:UniProtKB.
DR GO; GO:0015811; P:L-cystine transport; ISS:UniProtKB.
DR GO; GO:0015804; P:neutral amino acid transport; IDA: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_0000252232"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
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; 53611 MW; D688462E01A9F63B CRC64;
MGETVPRRRR EDEKSIQSDE PKTTSLQKEV GLISGICIIV GTIIGSGIFI SPKSVLSNTQ
AVGPCLIIWA ACGVLGTLGA LCFAELGTMI TKSGGEYPYL MEAFGPIPAY LFSWSSLLVM
KPSSFAIICL SFSEYVATPF YSGCEPPKVV VKCLAAAAIM LITTVNSLSV RLGSYVQNFF
TAAKLVIVAI IIISGLVLLA QGNTKNFENS FEGAEVSVGA ISLALYNGLW AYDGWNQLNY
ITEELRNPFR NLPLAIIFGI PLVTVCYILI NISYFTVMTP TELLQSQAVA VTFGDRVLYP
ASWIVPVFVA FSTIGAANGT CFTAGRLVYV AGREGHMLKV LSYISVRRLT PAPAIIFYGI
VATIYIIPGD INSLVNYFSF ATWLFYGLTI LGLIVMRFTR KELERPIKVP IFIPILVTFI
AAFLVLAPVI TNPAWEYLYC VLFILSGLVF YFLFVYYKFE WAQKISKPIT MHLQMLMEVV
PPEPDPK
