LAT4_MOUSE
ID LAT4_MOUSE Reviewed; 568 AA.
AC Q8CGA3; Q5CD76;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Large neutral amino acids transporter small subunit 4;
DE AltName: Full=L-type amino acid transporter 4;
DE AltName: Full=Solute carrier family 43 member 2;
GN Name=Slc43a2; Synonyms=Lat4;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND FUNCTION.
RC STRAIN=FVB/N;
RX PubMed=15659399; DOI=10.1074/jbc.m408638200;
RA Bodoy S., Martin L., Zorzano A., Palacin M., Estevez R., Bertran J.;
RT "Identification of LAT4, a novel amino acid transporter with system L
RT activity.";
RL J. Biol. Chem. 280:12002-12011(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Chairoungdua A., Kanai Y., Babu E., Iribe Y., Kim D., Tangtrongsup S.,
RA Jutabha P., Li Y., Anzai N., Endou H.;
RT "Identification of a novel epithelial type neutral amino acid transporter
RT with the properties of system L2.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, and Spleen;
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-, chloride-, and pH-independent, high affinity
CC transport of large neutral amino acids. {ECO:0000269|PubMed:15659399}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15659399}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15659399}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, kidney, brain and adipose
CC tissue, heart and testis. In the kidney, is detected in epithelial
CC cells of the distal tubule and collecting duct. In the intestine, is
CC expressed mainly in crypt cells of the intestinal microvilli and
CC epithelial cells in the base of the villus.
CC {ECO:0000269|PubMed:15659399}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15659399}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
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DR EMBL; BK005643; DAA05677.1; -; mRNA.
DR EMBL; AB120363; BAD91090.1; -; mRNA.
DR EMBL; AK143773; BAE25533.1; -; mRNA.
DR EMBL; AK159144; BAE34852.1; -; mRNA.
DR EMBL; AL591440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042513; AAH42513.1; -; mRNA.
DR CCDS; CCDS25051.1; -.
DR RefSeq; NP_001186212.1; NM_001199283.1.
DR RefSeq; NP_001186213.1; NM_001199284.1.
DR RefSeq; NP_775564.1; NM_173388.2.
DR RefSeq; XP_006532890.1; XM_006532827.3.
DR AlphaFoldDB; Q8CGA3; -.
DR STRING; 10090.ENSMUSP00000104071; -.
DR GlyGen; Q8CGA3; 1 site.
DR iPTMnet; Q8CGA3; -.
DR PhosphoSitePlus; Q8CGA3; -.
DR SwissPalm; Q8CGA3; -.
DR EPD; Q8CGA3; -.
DR jPOST; Q8CGA3; -.
DR MaxQB; Q8CGA3; -.
DR PaxDb; Q8CGA3; -.
DR PeptideAtlas; Q8CGA3; -.
DR PRIDE; Q8CGA3; -.
DR ProteomicsDB; 264916; -.
DR Antibodypedia; 10476; 114 antibodies from 20 providers.
DR Ensembl; ENSMUST00000042561; ENSMUSP00000046074; ENSMUSG00000038178.
DR Ensembl; ENSMUST00000108433; ENSMUSP00000104071; ENSMUSG00000038178.
DR Ensembl; ENSMUST00000169547; ENSMUSP00000126838; ENSMUSG00000038178.
DR GeneID; 215113; -.
DR KEGG; mmu:215113; -.
DR UCSC; uc007keb.2; mouse.
DR CTD; 124935; -.
DR MGI; MGI:2442746; Slc43a2.
DR VEuPathDB; HostDB:ENSMUSG00000038178; -.
DR eggNOG; ENOG502QTQJ; Eukaryota.
DR GeneTree; ENSGT00940000153576; -.
DR HOGENOM; CLU_035676_0_0_1; -.
DR InParanoid; Q8CGA3; -.
DR OMA; IQMLRLN; -.
DR OrthoDB; 639867at2759; -.
DR PhylomeDB; Q8CGA3; -.
DR TreeFam; TF328358; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 215113; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc43a2; mouse.
DR PRO; PR:Q8CGA3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CGA3; protein.
DR Bgee; ENSMUSG00000038178; Expressed in stroma of bone marrow and 233 other tissues.
DR ExpressionAtlas; Q8CGA3; baseline and differential.
DR Genevisible; Q8CGA3; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015807; P:L-amino acid transport; IDA:MGI.
DR GO; GO:0051956; P:negative regulation of amino acid transport; ISO:MGI.
DR GO; GO:0060358; P:negative regulation of leucine import; ISO:MGI.
DR GO; GO:0015804; P:neutral amino acid transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR027201; LAT4.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR20766:SF2; PTHR20766:SF2; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="Large neutral amino acids transporter small subunit
FT 4"
FT /id="PRO_0000307273"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 395..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N370"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N370"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 237
FT /note="P -> S (in Ref. 2; BAD91090)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="K -> E (in Ref. 2; BAD91090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 62430 MW; 02F076C32FE5988E CRC64;
MAPTLATAHR RRWWMACTAV LENLLFSAVL LGWGSLLIML KSEGFYSYLC TKPENVTNST
VGGSAEPEPE ELSLVNGWLS CKAQDEILNL AFTVGSFLLS AITLPLGIIM DKYGPRKLRL
LGSACFAVSC LLIAYGASNP DSLSVLIFIA LALNGFGGMC MTFTSLTLPN MFGDLRSTFI
ALMIGSYASS AVTFPGIKLI YDAGASFIGI LVVWAGCSGL VFFNCFFNWP LEPFPGPEDM
DYSVKIKFSW LGFDHKITGK QFYKQVTTVG RRLSVGSSMR TAKEQAALQE GHKLCLSTVD
LEVKCQPDAA AAPSFMHSVF SPLLVLSLVT MCVTQLRLIF YMGAMNSILE FLVRGDQKTV
ALYTSIFGAL QLLCLLTAPV IGYIMDWKLK ECEDTSEEPE EKEGTQGEKK QKRDRQIQKV
TNAMRAFAFT NVLLVGFGVT CLIPNLPLQI FSFVLHTIVR GFIHSAVGGL YAAVYPSTQF
GSLTGLQSLV SALFALLQQP LYLAMMGPLG GDPLWVNVGL LAMSMLGFCL PLYLICYRRQ
LERQLQQKRE DSKLFLKING SSNREAFV
