SLC31_MOUSE
ID SLC31_MOUSE Reviewed; 685 AA.
AC Q91WV7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neutral and basic amino acid transport protein rBAT;
DE AltName: Full=Solute carrier family 3 member 1;
DE AltName: Full=b(0,+)-type amino acid transport protein;
DE Short=NBAT;
GN Name=Slc3a1; Synonyms=Nbat;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, Kidney, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 41-59; 70-80; 148-166; 174-202; 271-322; 365-372;
RP 376-410; 439-451; 541-583; 622-629 AND 637-663, IDENTIFICATION BY MASS
RP SPECTROMETRY, 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 of
CC cystine and neutral and dibasic amino acids (system B(0,+)-like
CC activity). May function as an activator of SLC7A9 and be involved in
CC the high-affinity reabsorption of cystine in the kidney proximal
CC tubule.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transporter
CC SLC7A9. {ECO:0000269|PubMed:12167606}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12167606}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:12167606}.
CC -!- TISSUE SPECIFICITY: Expressed in the brush border membrane in the
CC kidney (at protein level). {ECO:0000269|PubMed:12167606}.
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DR EMBL; AK052623; BAC35066.1; -; mRNA.
DR EMBL; AK132275; BAE21075.1; -; mRNA.
DR EMBL; AC113476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466537; EDL38594.1; -; Genomic_DNA.
DR EMBL; BC013441; AAH13441.1; -; mRNA.
DR CCDS; CCDS37711.1; -.
DR RefSeq; NP_033231.2; NM_009205.2.
DR AlphaFoldDB; Q91WV7; -.
DR SMR; Q91WV7; -.
DR BioGRID; 203311; 3.
DR STRING; 10090.ENSMUSP00000024944; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GlyGen; Q91WV7; 6 sites.
DR iPTMnet; Q91WV7; -.
DR PhosphoSitePlus; Q91WV7; -.
DR jPOST; Q91WV7; -.
DR MaxQB; Q91WV7; -.
DR PaxDb; Q91WV7; -.
DR PeptideAtlas; Q91WV7; -.
DR PRIDE; Q91WV7; -.
DR ProteomicsDB; 261075; -.
DR Antibodypedia; 29895; 235 antibodies from 28 providers.
DR DNASU; 20532; -.
DR Ensembl; ENSMUST00000024944; ENSMUSP00000024944; ENSMUSG00000024131.
DR GeneID; 20532; -.
DR KEGG; mmu:20532; -.
DR UCSC; uc008dtl.1; mouse.
DR CTD; 6519; -.
DR MGI; MGI:1195264; Slc3a1.
DR VEuPathDB; HostDB:ENSMUSG00000024131; -.
DR eggNOG; KOG0471; Eukaryota.
DR GeneTree; ENSGT00940000158103; -.
DR HOGENOM; CLU_006462_8_0_1; -.
DR InParanoid; Q91WV7; -.
DR OMA; PNGEKWA; -.
DR OrthoDB; 1384693at2759; -.
DR PhylomeDB; Q91WV7; -.
DR TreeFam; TF314498; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 20532; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slc3a1; mouse.
DR PRO; PR:Q91WV7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91WV7; protein.
DR Bgee; ENSMUSG00000024131; Expressed in right kidney and 82 other tissues.
DR Genevisible; Q91WV7; MM.
DR GO; GO:0016324; C:apical plasma membrane; IPI:MGI.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005774; C:vacuolar membrane; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006865; P:amino acid transport; ISO:MGI.
DR GO; GO:0015810; P:aspartate transmembrane transport; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0015811; P:L-cystine transport; IDA:MGI.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 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 Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..685
FT /note="Neutral and basic amino acid transport protein rBAT"
FT /id="PRO_0000425741"
FT TOPO_DOM 1..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64319"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 685 AA; 78118 MW; 3316EBB9858AF9AB CRC64;
MDEDKGKRDP IQMSLKGCRT NNGFVQNEDI PEQDPDPGSR DTPQPNAVSI PAPEEPHLKA
VRPYAGMPKE VLFQFSGQAR YRVPREILFW LTVVSVFLLI GATIAIIVIS PKCLDWWQAG
PIYQIYPRSF KDSDKDGNGD LKGIQEKLDY ITALNIKTLW ITSFYKSSLK DFRYAVEDFK
EIDPIFGTMK DFENLVAAIH DKGLKLIIDF IPNHTSDKHP WFQSSRTRSG KYTDYYIWHN
CTHVNGVTTP PNNWLSVYGN SSWHFDEVRK QCYFHQFLKE QPDLNFRNPA VQEEIKEIIT
FWLSKGVDGF SFDAVKFLLE AKDLRNEIQV NTSQIPDTVT HYSELYHDFT TTQVGMHDIV
RDFRQTMNQY SREPGRYRFM GAEASAESIE RTMMYYGLPF IQEADFPFNK YFTTIGTLSG
HTVYEVITSW MENMPEGKWP NWMTGGPETP RLTSRVGSEY VNAMHMLLFT LPGTPITYYG
EEIGMGDISV TNFNESYDST TLVSKSPMQW DNSSNAGFTE ANHTWLPTNS DYHTVNVDVQ
KTQPSSALRL YQDLSLLHAT ELVLSRGWFC LLRDDSHSVV YTRELDGIDN VFLVVLNFGE
SSTVLNLQGI ISDLPPELRI RLSTNSASKG SAVDTRAISL EKGEGLVLEH STKAPLHQQA
AFRDRCFVSS RACYSSALDI LYSSC
