BAT1_RAT
ID BAT1_RAT Reviewed; 487 AA.
AC P82252; Q4KM04;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=b(0,+)-type amino acid transporter 1;
DE Short=b(0,+)AT;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=10506124; DOI=10.1074/jbc.274.41.28845;
RA Chairoungdua A., Segawa H., Kim J.Y., Miyamoto K., Haga H., Fukui Y.,
RA Mizoguchi K., Ito H., Takeda E., Endou H., Kanai Y.;
RT "Identification of an amino acid transporter associated with the
RT cystinuria-related type II membrane glycoprotein.";
RL J. Biol. Chem. 274:28845-28848(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CAV1.
RX PubMed=16358225;
RA Kwak J.O., Kim H.W., Jung S.M., Song J.H., Hong S.B., Oh K.J., Ko C.B.,
RA Cha S.H.;
RT "Co-localization and interaction of b0,+-type amino acid transporter 1
RT (BAT1) with caveolin-1 in rat kidney.";
RL J. Nephrol. 18:681-689(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:10506124}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A1. Interacts with CAV1. {ECO:0000269|PubMed:10506124,
CC ECO:0000269|PubMed:16358225}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10506124, ECO:0000269|PubMed:16358225}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:10506124,
CC ECO:0000305|PubMed:16358225}.
CC -!- TISSUE SPECIFICITY: Outer medulla of kidney (at protein level). Kidney
CC and small intestine. In the kidney localized to the apical membrane of
CC the proximal tubules. {ECO:0000269|PubMed:10506124,
CC ECO:0000269|PubMed:16358225}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; AB029559; BAA85186.1; -; mRNA.
DR EMBL; BC098909; AAH98909.1; -; mRNA.
DR RefSeq; NP_446381.1; NM_053929.1.
DR RefSeq; XP_006228937.1; XM_006228875.2.
DR RefSeq; XP_006228938.1; XM_006228876.3.
DR RefSeq; XP_006228939.1; XM_006228877.3.
DR RefSeq; XP_008757325.1; XM_008759103.2.
DR RefSeq; XP_008757326.1; XM_008759104.1.
DR AlphaFoldDB; P82252; -.
DR SMR; P82252; -.
DR STRING; 10116.ENSRNOP00000016919; -.
DR TCDB; 2.A.3.8.15; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P82252; -.
DR PhosphoSitePlus; P82252; -.
DR PaxDb; P82252; -.
DR PRIDE; P82252; -.
DR Ensembl; ENSRNOT00000016919; ENSRNOP00000016919; ENSRNOG00000012344.
DR GeneID; 116726; -.
DR KEGG; rno:116726; -.
DR UCSC; RGD:619905; rat.
DR CTD; 11136; -.
DR RGD; 619905; Slc7a9.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000156370; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; P82252; -.
DR OMA; HKAFGIH; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; P82252; -.
DR TreeFam; TF313355; -.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:P82252; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012344; Expressed in jejunum and 10 other tissues.
DR Genevisible; P82252; RN.
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; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:RGD.
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; IDA:RGD.
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_0000054260"
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..23
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:0007744|PubMed:22673903"
SQ SEQUENCE 487 AA; 53658 MW; EB43AA1FCC8DC3A7 CRC64;
MEETSPRRRR EDEKSVHSTE PKTTSLQKEV GLLSGICIIV GTIIGSGIFI SPKSVLANTE
SVGPCLIIWA ACGVLATLGA LCFAELGTMI TKSGGEYPYL MEAFGPIPAY LFSWTSLIVM
KPSSFAIICL SFSEYVCAAF YLGCRPPAVV VKLLAAAAIL LITTVNALSV RLGSYVQNVF
TAAKLVIVAI IIISGLVLLA QGNVKNFQNS FEGSQTSVGS ISLAFYNGLW AYDGWNQLNY
ITEELRNPYR NLPMAIVIGI PLVTVCYILM NIAYFTVMTP TELLQSQAVA VTFGDRVLYP
ASWVVPLFVA FSTIGAANGT CFTAGRLIYV AGREGHMLKV LSYISVKRLT PAPALVFYGI
IAIIYIIPGD INSLVNYFSF AAWLFYGMTI LGLVVMRFTR KDLERPIKVP IFIPIIVILV
SVFLILAPII SSPAWEYLYC VLFILSGLIF YFLFVHYKFR WAQKISRPIT KHLQMLMEVV
PPEKDPE
