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Protein

Neutral and basic amino acid transport protein rBAT

Gene

Slc3a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the high-affinity sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney proximal tubule.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-352230. Amino acid transport across the plasma membrane.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral and basic amino acid transport protein rBAT
Alternative name(s):
Solute carrier family 3 member 1
b(0,+)-type amino acid transport protein
Short name:
NBAT
Gene namesi
Name:Slc3a1
Synonyms:Nbat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1195264. Slc3a1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8888CytoplasmicSequence analysisAdd
BLAST
Transmembranei89 – 10921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini110 – 685576ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • brush border membrane Source: UniProtKB
  • extracellular exosome Source: MGI
  • integral component of plasma membrane Source: Ensembl
  • mitochondrial inner membrane Source: MGI
  • vacuolar membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 685685Neutral and basic amino acid transport protein rBATPRO_0000425741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence analysis
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence analysis
Modified residuei385 – 3851PhosphoserineBy similarity
Glycosylationi512 – 5121N-linked (GlcNAc...)Sequence analysis
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ91WV7.
PaxDbiQ91WV7.
PRIDEiQ91WV7.

PTM databases

iPTMnetiQ91WV7.

Expressioni

Tissue specificityi

Expressed in the brush border membrane in the kidney (at protein level).1 Publication

Gene expression databases

GenevisibleiQ91WV7. MM.

Interactioni

Subunit structurei

Disulfide-linked heterodimer with the amino acid transporter SLC7A9.1 Publication

Protein-protein interaction databases

BioGridi203311. 1 interaction.
IntActiQ91WV7. 2 interactions.
MINTiMINT-4121539.
STRINGi10090.ENSMUSP00000024944.

Structurei

3D structure databases

ProteinModelPortaliQ91WV7.
SMRiQ91WV7. Positions 115-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.
GeneTreeiENSGT00530000063127.
HOVERGENiHBG053002.
InParanoidiQ91WV7.
KOiK14210.
OMAiCTHENGK.
OrthoDBiEOG78D7JQ.
PhylomeDBiQ91WV7.
TreeFamiTF314498.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91WV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEDKGKRDP IQMSLKGCRT NNGFVQNEDI PEQDPDPGSR DTPQPNAVSI
60 70 80 90 100
PAPEEPHLKA VRPYAGMPKE VLFQFSGQAR YRVPREILFW LTVVSVFLLI
110 120 130 140 150
GATIAIIVIS PKCLDWWQAG PIYQIYPRSF KDSDKDGNGD LKGIQEKLDY
160 170 180 190 200
ITALNIKTLW ITSFYKSSLK DFRYAVEDFK EIDPIFGTMK DFENLVAAIH
210 220 230 240 250
DKGLKLIIDF IPNHTSDKHP WFQSSRTRSG KYTDYYIWHN CTHVNGVTTP
260 270 280 290 300
PNNWLSVYGN SSWHFDEVRK QCYFHQFLKE QPDLNFRNPA VQEEIKEIIT
310 320 330 340 350
FWLSKGVDGF SFDAVKFLLE AKDLRNEIQV NTSQIPDTVT HYSELYHDFT
360 370 380 390 400
TTQVGMHDIV RDFRQTMNQY SREPGRYRFM GAEASAESIE RTMMYYGLPF
410 420 430 440 450
IQEADFPFNK YFTTIGTLSG HTVYEVITSW MENMPEGKWP NWMTGGPETP
460 470 480 490 500
RLTSRVGSEY VNAMHMLLFT LPGTPITYYG EEIGMGDISV TNFNESYDST
510 520 530 540 550
TLVSKSPMQW DNSSNAGFTE ANHTWLPTNS DYHTVNVDVQ KTQPSSALRL
560 570 580 590 600
YQDLSLLHAT ELVLSRGWFC LLRDDSHSVV YTRELDGIDN VFLVVLNFGE
610 620 630 640 650
SSTVLNLQGI ISDLPPELRI RLSTNSASKG SAVDTRAISL EKGEGLVLEH
660 670 680
STKAPLHQQA AFRDRCFVSS RACYSSALDI LYSSC
Length:685
Mass (Da):78,118
Last modified:December 1, 2001 - v1
Checksum:i3316EBB9858AF9AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052623 mRNA. Translation: BAC35066.1.
AK132275 mRNA. Translation: BAE21075.1.
AC113476 Genomic DNA. No translation available.
CH466537 Genomic DNA. Translation: EDL38594.1.
BC013441 mRNA. Translation: AAH13441.1.
CCDSiCCDS37711.1.
RefSeqiNP_033231.2. NM_009205.2.
UniGeneiMm.227176.
Mm.461481.

Genome annotation databases

EnsembliENSMUST00000024944; ENSMUSP00000024944; ENSMUSG00000024131.
GeneIDi20532.
KEGGimmu:20532.
UCSCiuc008dtl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052623 mRNA. Translation: BAC35066.1.
AK132275 mRNA. Translation: BAE21075.1.
AC113476 Genomic DNA. No translation available.
CH466537 Genomic DNA. Translation: EDL38594.1.
BC013441 mRNA. Translation: AAH13441.1.
CCDSiCCDS37711.1.
RefSeqiNP_033231.2. NM_009205.2.
UniGeneiMm.227176.
Mm.461481.

3D structure databases

ProteinModelPortaliQ91WV7.
SMRiQ91WV7. Positions 115-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203311. 1 interaction.
IntActiQ91WV7. 2 interactions.
MINTiMINT-4121539.
STRINGi10090.ENSMUSP00000024944.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

PTM databases

iPTMnetiQ91WV7.

Proteomic databases

MaxQBiQ91WV7.
PaxDbiQ91WV7.
PRIDEiQ91WV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024944; ENSMUSP00000024944; ENSMUSG00000024131.
GeneIDi20532.
KEGGimmu:20532.
UCSCiuc008dtl.1. mouse.

Organism-specific databases

CTDi6519.
MGIiMGI:1195264. Slc3a1.

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.
GeneTreeiENSGT00530000063127.
HOVERGENiHBG053002.
InParanoidiQ91WV7.
KOiK14210.
OMAiCTHENGK.
OrthoDBiEOG78D7JQ.
PhylomeDBiQ91WV7.
TreeFamiTF314498.

Enzyme and pathway databases

ReactomeiR-MMU-352230. Amino acid transport across the plasma membrane.

Miscellaneous databases

ChiTaRSiSlc3a1. mouse.
PROiQ91WV7.
SOURCEiSearch...

Gene expression databases

GenevisibleiQ91WV7. MM.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Extraembryonic tissue, Kidney and Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  5. "rBAT-b(0,+)AT heterodimer is the main apical reabsorption system for cystine in the kidney."
    Fernandez E., Carrascal M., Rousaud F., Abian J., Zorzano A., Palacin M., Chillaron J.
    Am. J. Physiol. 283:F540-F548(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-59; 70-80; 148-166; 174-202; 271-322; 365-372; 376-410; 439-451; 541-583; 622-629 AND 637-663, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.

Entry informationi

Entry nameiSLC31_MOUSE
AccessioniPrimary (citable) accession number: Q91WV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.