ID LAT3_MOUSE Reviewed; 564 AA. AC Q8BSM7; A2ATS3; Q9D0H7; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 143. DE RecName: Full=Large neutral amino acids transporter small subunit 3 {ECO:0000305}; DE AltName: Full=L-type amino acid transporter 3; DE AltName: Full=Solute carrier family 43 member 1; GN Name=Slc43a1 {ECO:0000312|MGI:MGI:1931352}; Synonyms=Lat3; 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] {ECO:0000305, ECO:0000312|EMBL:BAD10947.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB/N {ECO:0000312|EMBL:BAD10947.1}; RC TISSUE=Salivary gland {ECO:0000312|EMBL:BAD10947.1}; RA Babu E., Kanai Y., Chairoungdua A., Li Y., Anzai N., Endou H.; RT "Identification and characterization of mouse LAT3 system L amino acid RT transporter."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Forelimb; 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 [3] 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 [4] {ECO:0000312|EMBL:AAH53747.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334}; RC TISSUE=Embryo {ECO:0000312|EMBL:AAH53747.1}; 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 FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND INDUCTION. RX PubMed=17322374; DOI=10.2353/ajpath.2007.060428; RA Fukuhara D., Kanai Y., Chairoungdua A., Babu E., Bessho F., Kawano T., RA Akimoto Y., Endou H., Yan K.; RT "Protein characterization of NA+-independent system L amino acid RT transporter 3 in mice: a potential role in supply of branched-chain amino RT acids under nutrient starvation."; RL Am. J. Pathol. 170:888-898(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=19443642; DOI=10.1681/asn.2008070809; RA Sekine Y., Nishibori Y., Akimoto Y., Kudo A., Ito N., Fukuhara D., RA Kurayama R., Higashihara E., Babu E., Kanai Y., Asanuma K., Nagata M., RA Majumdar A., Tryggvason K., Yan K.; RT "Amino acid transporter LAT3 is required for podocyte development and RT function."; RL J. Am. Soc. Nephrol. 20:1586-1596(2009). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and RC 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: Uniport that mediates the transport of neutral amino acids CC such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine CC (PubMed:17322374). The transport activity is sodium ions-independent, CC electroneutral and mediated by a facilitated diffusion CC (PubMed:17322374). {ECO:0000269|PubMed:17322374}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-leucine(in) = D-leucine(out); Xref=Rhea:RHEA:73015, CC ChEBI:CHEBI:143079; Evidence={ECO:0000250|UniProtKB:O75387}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucine(in) = L-leucine(out); Xref=Rhea:RHEA:73011, CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:17322374}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-isoleucine(in) = L-isoleucine(out); Xref=Rhea:RHEA:70943, CC ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:17322374}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionine(in) = L-methionine(out); Xref=Rhea:RHEA:70939, CC ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:O75387}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanine(in) = L-phenylalanine(out); CC Xref=Rhea:RHEA:27950, ChEBI:CHEBI:58095; CC Evidence={ECO:0000269|PubMed:17322374}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-valine(in) = L-valine(out); Xref=Rhea:RHEA:29703, CC ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:17322374}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17322374}; CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane CC {ECO:0000250|UniProtKB:O75387}; Multi-pass membrane protein CC {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17322374}; Multi-pass membrane protein CC {ECO:0000255}. Note=Located in the apical plasma membrane of the CC podocyte foot processes (By similarity). Located in the plasma membrane CC of liver and skeletal muscle, and in the endoplasmic reticulum and in CC crystalline inclusions in pancreatic acinar cells (PubMed:17322374). CC {ECO:0000250|UniProtKB:O75387, ECO:0000269|PubMed:17322374}. CC -!- TISSUE SPECIFICITY: Expressed in the kidney cortex as well as liver, CC pancreas, and skeletal muscle (PubMed:19443642). In kidney expressed in CC the glomerular tuft (at protein level) (PubMed:19443642). Expressed in CC liver, skeletal muscle and pancreas (at protein level) CC (PubMed:17322374). {ECO:0000269|PubMed:17322374, CC ECO:0000269|PubMed:19443642}. CC -!- INDUCTION: By nutrient starvation. {ECO:0000269|PubMed:17322374, CC ECO:0000269|PubMed:19443642}. CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB27605.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAC27305.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AB103034; BAD10947.1; -; mRNA. DR EMBL; AK011417; BAB27605.1; ALT_FRAME; mRNA. DR EMBL; AK031215; BAC27305.1; ALT_FRAME; mRNA. DR EMBL; AL928914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC053747; AAH53747.1; -; mRNA. DR CCDS; CCDS38163.1; -. DR RefSeq; NP_001077278.1; NM_001083809.1. DR RefSeq; NP_078773.1; NM_024497.1. DR RefSeq; XP_006500293.1; XM_006500230.3. DR AlphaFoldDB; Q8BSM7; -. DR BioGRID; 215358; 1. DR STRING; 10090.ENSMUSP00000028469; -. DR GlyCosmos; Q8BSM7; 4 sites, No reported glycans. DR GlyGen; Q8BSM7; 4 sites. DR iPTMnet; Q8BSM7; -. DR PhosphoSitePlus; Q8BSM7; -. DR SwissPalm; Q8BSM7; -. DR jPOST; Q8BSM7; -. DR MaxQB; Q8BSM7; -. DR PaxDb; 10090-ENSMUSP00000107252; -. DR ProteomicsDB; 264976; -. DR Antibodypedia; 14174; 135 antibodies from 23 providers. DR DNASU; 72401; -. DR Ensembl; ENSMUST00000111624.8; ENSMUSP00000107251.2; ENSMUSG00000027075.17. DR Ensembl; ENSMUST00000121114.8; ENSMUSP00000112642.2; ENSMUSG00000027075.17. DR GeneID; 72401; -. DR KEGG; mmu:72401; -. DR UCSC; uc008kjk.1; mouse. DR AGR; MGI:1931352; -. DR CTD; 8501; -. DR MGI; MGI:1931352; Slc43a1. DR VEuPathDB; HostDB:ENSMUSG00000027075; -. DR eggNOG; ENOG502QUZ1; Eukaryota. DR GeneTree; ENSGT00940000153576; -. DR HOGENOM; CLU_035676_0_0_1; -. DR InParanoid; Q8BSM7; -. DR OMA; INWPRES; -. DR OrthoDB; 5384516at2759; -. DR PhylomeDB; Q8BSM7; -. DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane. DR BioGRID-ORCS; 72401; 0 hits in 77 CRISPR screens. DR PRO; PR:Q8BSM7; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q8BSM7; Protein. DR Bgee; ENSMUSG00000027075; Expressed in hindlimb stylopod muscle and 115 other cell types or tissues. DR ExpressionAtlas; Q8BSM7; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098846; C:podocyte foot; ISO:MGI. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI. DR GO; GO:0015188; F:L-isoleucine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005304; F:L-valine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015818; P:isoleucine transport; IDA:UniProtKB. DR GO; GO:0015807; P:L-amino acid transport; IDA:MGI. DR GO; GO:1903785; P:L-valine transmembrane transport; IDA:UniProtKB. DR GO; GO:0015820; P:leucine transport; IDA:UniProtKB. 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; IDA:UniProtKB. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR20766; -; 1. DR PANTHER; PTHR20766:SF0; LARGE NEUTRAL AMINO ACIDS TRANSPORTER SMALL SUBUNIT 3; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR Genevisible; Q8BSM7; MM. PE 1: Evidence at protein level; KW Amino-acid transport; Cell membrane; Endoplasmic reticulum; Glycoprotein; KW Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..564 FT /note="Large neutral amino acids transporter small subunit FT 3" FT /id="PRO_0000218641" FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 105..124 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 131..151 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 191..211 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 357..377 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 424..444 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 451..471 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 490..510 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 515..535 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75387" FT MOD_RES 267 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O75387" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 396 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 558 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 564 AA; 62644 MW; AEC14BF1F3438BB8 CRC64; MAPTLKQAYR RRWWMACTAV VENLFFSAVL LGWASLLIML KKEGFYSSLC PAENRTNTTQ DEQHQWTSCD QQEKMLNLGF TIGSFLLSAT TLPLGILMDR FGPRPLRLVG SACFAASCTL MALASRDTEV LSPLIFLALS LNGFAGICLT FTSLTLPNMF GNLRSTFMAL MIGSYASSAI TFPGIKLIYD AGVPFTVIMF TWSGLACLIF LNCALNWPAE AFPAPEEVDY TKKIKLIGLA LDHKVTGDRF YTHVTIVGQR LSQKSPSLEE GADAFISSPD IPGTSEETPE KSVPFRKSLC SPIFLWSLVT MGMTQLRVIF YMGAMNKILE FIVTGGKERE TNEQRQKVEE TVEFYSSIFG VMQLLCLLTC PLIGYIMDWR IKDCVDAPTE GTLNENASFG DARDGASTKF TRPRYRKVQK LTNAINAFTL TNILLVGFGI ACLIKNLHLQ LLAFVLHTIV RGFFHSACGG LYAAVFPSNH FGTLTGLQSL ISAVFALLQQ LLFMAMVGPL HGDPFWVNLG LLLLSFLGFL LPSYLYYYRS RLQREYATNL VDPQKVLNTS KVAT //