ID SLC31_RAT Reviewed; 683 AA.
AC Q64319; Q62672;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Amino acid transporter heavy chain SLC3A1;
DE AltName: Full=D2 {ECO:0000303|PubMed:1376924};
DE AltName: Full=Neutral and basic amino acid transport protein {ECO:0000303|PubMed:8052618};
DE Short=NBAT {ECO:0000303|PubMed:8052618};
DE AltName: Full=Solute carrier family 3 member 1;
DE AltName: Full=b(0,+)-type amino acid transporter-related heavy chain;
DE Short=NAA-TR {ECO:0000303|PubMed:1729674};
DE Short=rBAT {ECO:0000303|PubMed:10506124};
GN Name=Slc3a1; Synonyms=Nbat;
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, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
RX PubMed=1376924; DOI=10.1073/pnas.89.12.5596;
RA Wells R.G., Hediger M.A.;
RT "Cloning of a rat kidney cDNA that stimulates dibasic and neutral amino
RT acid transport and has sequence similarity to glucosidases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5596-5600(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=1729674; DOI=10.1073/pnas.89.1.1;
RA Tate S.S., Yan N., Udenfriend S.;
RT "Expression cloning of a Na(+)-independent neutral amino acid transporter
RT from rat kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1-5(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE OF 1-140.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8052618; DOI=10.1073/pnas.91.16.7548;
RA Yan N., Mosckovitz R., Gerber L.D., Mathew S., Murty V.V.V.S., Tate S.S.,
RA Udenfriend S.;
RT "Characterization of the promoter region of the gene for the rat neutral
RT and basic amino acid transporter and chromosomal localization of the human
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7548-7552(1994).
RN [5]
RP SUBUNIT, AND TISSUE SPECIFICITY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-383, AND
RP IDENTIFICATION BY 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: Acts as a chaperone that facilitates biogenesis and
CC trafficking of functional transporter heteromers to the plasma membrane
CC (PubMed:1376924, PubMed:1729674) (By similarity). Associates with
CC SLC7A9 to form a functional transporter complex that mediates the
CC electrogenic exchange between cationic amino acids and neutral amino
CC acids, with a stoichiometry of 1:1. SLC7A9-SLC3A1 transporter has
CC system b(0,+)-like activity with high affinity for extracellular
CC cationic amino acids and L-cystine and lower affinity for intracellular
CC neutral amino acids. Substrate exchange is driven by high concentration
CC of intracellular neutral amino acids and the intracellular reduction of
CC L-cystine to L-cysteine. SLC7A9-SLC3A1 acts as a major transporter for
CC reabsorption of L-cystine and dibasic amino acids across the brush
CC border membrane in early proximal tubules (PubMed:1376924,
CC PubMed:1729674) (By similarity). Associates with SLC7A13 to form a
CC functional complex that transports anionic and neutral amino acids via
CC exchange or facilitated diffusion. SLC7A13-SLC3A1 may act as a major
CC transporter for L-cystine in late proximal tubules, ensuring its
CC reabsorption from the luminal fluid in exchange for cytosolic L-
CC glutamate or L-aspartate (By similarity).
CC {ECO:0000250|UniProtKB:Q07837, ECO:0000250|UniProtKB:Q91WV7,
CC ECO:0000269|PubMed:1376924, ECO:0000269|PubMed:1729674}.
CC -!- SUBUNIT: Disulfide-linked heterodimer composed of the catalytic light
CC subunit SLC7A9 and the heavy subunit SLC3A1. The heterodimer is the
CC minimal functional unit. Assembles in non-covalently linked
CC heterotetramers (dimers of heterodimers) and higher order oligomers;
CC the oligomerization is mediated by SLC3A1 likely to prevent degradation
CC in the endoplasmic reticulum and facilitate heteromer trafficking to
CC the plasma membrane (By similarity) (PubMed:10506124). Disulfide-linked
CC heterodimer composed of the catalytic light subunit SLC7A13 and the
CC heavy subunit SLC3A1 (By similarity). {ECO:0000250|UniProtKB:Q07837,
CC ECO:0000250|UniProtKB:Q91WV7, ECO:0000269|PubMed:10506124}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91WV7};
CC Single-pass type II membrane protein {ECO:0000255}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q91WV7}; Single-pass type II membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and intestine. In
CC kidney localized to the apical membrane of the proximal tubules.
CC {ECO:0000269|PubMed:10506124, ECO:0000269|PubMed:1376924,
CC ECO:0000269|PubMed:1729674}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M80804; AAA73144.1; -; mRNA.
DR EMBL; M77345; AAA41544.1; -; mRNA.
DR EMBL; BC078852; AAH78852.1; -; mRNA.
DR EMBL; U10110; AAA20394.1; -; Unassigned_DNA.
DR PIR; A41785; A41785.
DR RefSeq; NP_058912.1; NM_017216.1.
DR AlphaFoldDB; Q64319; -.
DR SMR; Q64319; -.
DR STRING; 10116.ENSRNOP00000009581; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GlyCosmos; Q64319; 7 sites, No reported glycans.
DR GlyGen; Q64319; 7 sites.
DR iPTMnet; Q64319; -.
DR PhosphoSitePlus; Q64319; -.
DR PaxDb; 10116-ENSRNOP00000009581; -.
DR Ensembl; ENSRNOT00000009581.5; ENSRNOP00000009581.2; ENSRNOG00000007006.5.
DR Ensembl; ENSRNOT00055032680; ENSRNOP00055026470; ENSRNOG00055019152.
DR Ensembl; ENSRNOT00060007198; ENSRNOP00060005457; ENSRNOG00060004289.
DR Ensembl; ENSRNOT00065012552; ENSRNOP00065009246; ENSRNOG00065007957.
DR GeneID; 29484; -.
DR KEGG; rno:29484; -.
DR UCSC; RGD:3709; rat.
DR AGR; RGD:3709; -.
DR CTD; 6519; -.
DR RGD; 3709; Slc3a1.
DR eggNOG; KOG0471; Eukaryota.
DR GeneTree; ENSGT00940000158103; -.
DR HOGENOM; CLU_006462_8_0_1; -.
DR InParanoid; Q64319; -.
DR OMA; PNGEKWA; -.
DR OrthoDB; 3680211at2759; -.
DR PhylomeDB; Q64319; -.
DR TreeFam; TF314498; -.
DR Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR PRO; PR:Q64319; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007006; Expressed in kidney and 20 other cell types or tissues.
DR Genevisible; Q64319; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0006865; P:amino acid transport; IDA:RGD.
DR GO; GO:0015810; P:aspartate transmembrane transport; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0015811; P:L-cystine transport; ISO:RGD.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISO:RGD.
DR CDD; cd11359; AmyAc_SLC3A1; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..683
FT /note="Amino acid transporter heavy chain SLC3A1"
FT /id="PRO_0000071951"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..683
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111
FT /note="Interchain (with C-144 in SLC7A5)"
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT DISULFID 239..270
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT DISULFID 568..664
FT /evidence="ECO:0000250|UniProtKB:Q07837"
FT DISULFID 671..683
FT /evidence="ECO:0000250|UniProtKB:Q07837"
SQ SEQUENCE 683 AA; 78507 MW; 201C1F2A2F404311 CRC64;
MNEDKDKRDS IQMSMKGCRT NNGFVQNEDI QEQDPDSRDT PQSNAVSIPA PEEPQLKVVR
PYAGMPKEVL FQFSGQARYR VPREILFWLT VVSVFLLIGA TIAIIIISPK CLDWWQAGPM
YQIYPRSFKD SDKDGNGDLK GIQEKLDYIT ALNIKTIWIT SFYKSPLKDF RYAVEDFKEI
DPIFGTMKDF ENLVAAVHDK GLKLIIDFIP NHTSDKHPWF QSSRTRSGKY TDYYIWHNCT
HANGVTTPPN NWLSVYGNSS WQFDEERKQC YFHQFLKEQP DLNFRNPAVQ EEIKEIIKFW
LSKGVDGFSF DAVKFLLEAK DLRNEIQVNT SQIPDTVTRY SELYHDFTTT QVGMHDLVRD
FRQTMNQFSR EPGRYRFMGT EVSAESTERT MVYYGLSFIQ EADFPFNKYL ATLDTLSGHT
VYEAITSWME NMPEGKWPNW MIGGPETSRL TSRVGSEYVN AMNMLLFTLP GTPITYYGEE
IGMGDISITN LNERYDTNAL LSKSPMQWDN SSNAGFTEAN HTWLPTNSDY HTVNVDVQKT
QPSSALRLYQ DLSLLHAREL LLSRGWFCLL RDDNHSVVYT RELDGIDKVF LVVLNFGESS
TVLNLQETIS DVPTKLRIRL STNPASKGSD VDTHAVSLEK GEGLILEHSM KTLLHHQKAF
RDKCFISNRA CYSSVLDLLY SSC
//
