LAT2_MOUSE
ID LAT2_MOUSE Reviewed; 531 AA.
AC Q9QXW9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Large neutral amino acids transporter small subunit 2;
DE AltName: Full=L-type amino acid transporter 2;
DE Short=mLAT2;
DE AltName: Full=Solute carrier family 7 member 8;
GN Name=Slc7a8; Synonyms=Lat2;
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10574970; DOI=10.1074/jbc.274.49.34948;
RA Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F., Kuehn L.C.;
RT "LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of
RT kidney and intestine.";
RL J. Biol. Chem. 274:34948-34954(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10610726; DOI=10.1006/geno.1999.5978;
RA Bassi M.T., Sperandeo M.P., Incerti B., Bulfone A., Pepe A., Surace E.M.,
RA Gattuso C., de Grandi A., Buoninconti A., Riboni M., Manzoni M., Andria G.,
RA Ballabio A., Borsani G., Sebastio G.;
RT "SLC7A8, a gene mapping within the lysinuric protein intolerance critical
RT region, encodes a new member of the glycoprotein-associated amino acid
RT transporter family.";
RL Genomics 62:297-303(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21; SER-27 AND
RP SER-28, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, and Testis;
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: Sodium-independent, high-affinity transport of small and
CC large neutral amino acids such as alanine, serine, threonine, cysteine,
CC phenylalanine, tyrosine, leucine, arginine and tryptophan, when
CC associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has
CC higher affinity for L-phenylalanine than LAT1 but lower affinity for
CC glutamine and serine. L-alanine is transported at physiological
CC concentrations. Plays a role in basolateral (re)absorption of neutral
CC amino acids. Involved in the uptake of methylmercury (MeHg) when
CC administered as the L-cysteine or D,L-homocysteine complexes, and hence
CC plays a role in metal ion homeostasis and toxicity. Involved in the
CC cellular activity of small molecular weight nitrosothiols, via the
CC stereoselective transport of L-nitrosocysteine (L-CNSO) across the
CC transmembrane. Plays an essential role in the reabsorption of neutral
CC amino acids from the epithelial cells to the bloodstream in the kidney.
CC {ECO:0000269|PubMed:10574970}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.2 uM for L-phenylalanine {ECO:0000269|PubMed:10574970};
CC KM=48 uM for L-leucine {ECO:0000269|PubMed:10574970};
CC KM=167 uM for L-alanine {ECO:0000269|PubMed:10574970};
CC KM=275 uM for L-glutamine {ECO:0000269|PubMed:10574970};
CC KM=294 uM for L-histidine {ECO:0000269|PubMed:10574970};
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10574970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Basolateral cell
CC membrane {ECO:0000269|PubMed:10574970}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10574970}. Note=Localized to the cytoplasm when
CC expressed alone (By similarity). When coexpressed with SLC3A2/4F2hc, is
CC localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the
CC basolateral membrane of kidney cortex proximal tubules and small
CC intestine epithelia of the villi. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in kidney and small intestine.
CC Moderately present in placenta, ovary and brain.
CC {ECO:0000269|PubMed:10574970}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC {ECO:0000305}.
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DR EMBL; AF171668; AAF20380.1; -; mRNA.
DR EMBL; Y19022; CAB69072.1; -; mRNA.
DR EMBL; BC059004; AAH59004.1; -; mRNA.
DR CCDS; CCDS27101.1; -.
DR RefSeq; NP_058668.1; NM_016972.2.
DR AlphaFoldDB; Q9QXW9; -.
DR SMR; Q9QXW9; -.
DR BioGRID; 206166; 1.
DR STRING; 10090.ENSMUSP00000022787; -.
DR iPTMnet; Q9QXW9; -.
DR PhosphoSitePlus; Q9QXW9; -.
DR SwissPalm; Q9QXW9; -.
DR jPOST; Q9QXW9; -.
DR MaxQB; Q9QXW9; -.
DR PaxDb; Q9QXW9; -.
DR PeptideAtlas; Q9QXW9; -.
DR PRIDE; Q9QXW9; -.
DR ProteomicsDB; 264975; -.
DR Antibodypedia; 22403; 241 antibodies from 24 providers.
DR DNASU; 50934; -.
DR Ensembl; ENSMUST00000022787; ENSMUSP00000022787; ENSMUSG00000022180.
DR GeneID; 50934; -.
DR KEGG; mmu:50934; -.
DR UCSC; uc007txa.1; mouse.
DR CTD; 23428; -.
DR MGI; MGI:1355323; Slc7a8.
DR VEuPathDB; HostDB:ENSMUSG00000022180; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000158278; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9QXW9; -.
DR OMA; FTHLWND; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; Q9QXW9; -.
DR TreeFam; TF313355; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR SABIO-RK; Q9QXW9; -.
DR BioGRID-ORCS; 50934; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc7a8; mouse.
DR PRO; PR:Q9QXW9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QXW9; protein.
DR Bgee; ENSMUSG00000022180; Expressed in yolk sac and 164 other tissues.
DR Genevisible; Q9QXW9; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISA:MGI.
DR GO; GO:0005275; F:amine transmembrane transporter activity; ISA:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; ISO:MGI.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:MGI.
DR GO; GO:0006865; P:amino acid transport; ISA:MGI.
DR GO; GO:0015816; P:glycine transport; IMP:ARUK-UCL.
DR GO; GO:1904273; P:L-alanine import across plasma membrane; ISO:MGI.
DR GO; GO:0015807; P:L-amino acid transport; IDA:MGI.
DR GO; GO:1903801; P:L-leucine import across plasma membrane; ISO:MGI.
DR GO; GO:0098713; P:leucine import across plasma membrane; ISO:MGI.
DR GO; GO:0015820; P:leucine transport; IMP:ARUK-UCL.
DR GO; GO:0015804; P:neutral amino acid transport; IBA:GO_Central.
DR GO; GO:0035524; P:proline transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0070327; P:thyroid hormone transport; IMP:ARUK-UCL.
DR GO; GO:0015827; P:tryptophan transport; IMP:ARUK-UCL.
DR GO; GO:0015829; P:valine transport; IMP:ARUK-UCL.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004760; L_AA_transporter.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00911; 2A0308; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Cytoplasm; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..531
FT /note="Large neutral amino acids transporter small subunit
FT 2"
FT /id="PRO_0000054274"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..531
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:21183079"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVR6"
SQ SEQUENCE 531 AA; 57873 MW; AE9C3B42F3B24F8C CRC64;
MEKGARQRNN TAKNHPGSDT SPEAEASSGG GGVALKKEIG LVSACGIIVG NIIGSGIFVS
PKGVLENAGS VGLALIVWIV TGIITAVGAL CYAELGVTIP KSGGDYSYVK DIFGGLAGFL
RLWIAVLVIY PTNQAVIALT FSNYVLQPLF PTCFPPESGL RLLAAICLLL LTWVNCSSVR
WATRVQDIFT AGKLLALALI IIMGIVQICK GEFFWLEPKN AFENFQEPDI GLVALAFLQG
SFAYGGWNFL NYVTEELVDP YKNLPRAIFI SIPLVTFVYV FANIAYVTAM SPQELLASNA
VAVTFGEKLL GVMAWIMPIS VALSTFGGVN GSLFTSSRLF FAGAREGHLP SVLAMIHVKR
CTPIPALLFT CLSTLLMLVT SDMYTLINYV GFINYLFYGV TVAGQIVLRW KKPDIPRPIK
VSLLFPIIYL LFWAFLLIFS LWSEPVVCGI GLAIMLTGVP VYFLGVYWQH KPKCFNDFIK
SLTLVSQKMC VVVYPQEGNS GAEETTDDLE EQHKPIFKPT PVKDPDSEEQ P
