LAT3_MOUSE
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 03-AUG-2022, entry version 135.
DE RecName: Full=Large neutral amino acids transporter small subunit 3;
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 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 [6]
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 [7]
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: Sodium-independent, high affinity transport of large neutral
CC amino acids. Has narrower substrate selectivity compared to SLC7A5 and
CC SLC7A8 and mainly transports branched-chain amino acids and
CC phenylalanine (By similarity). {ECO:0000250|UniProtKB:O75387}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27305.1; Type=Frameshift; Evidence={ECO:0000305};
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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.ENSMUSP00000107252; -.
DR GlyGen; Q8BSM7; 4 sites.
DR iPTMnet; Q8BSM7; -.
DR PhosphoSitePlus; Q8BSM7; -.
DR jPOST; Q8BSM7; -.
DR MaxQB; Q8BSM7; -.
DR PaxDb; Q8BSM7; -.
DR PRIDE; Q8BSM7; -.
DR ProteomicsDB; 264976; -.
DR Antibodypedia; 14174; 111 antibodies from 23 providers.
DR DNASU; 72401; -.
DR Ensembl; ENSMUST00000111624; ENSMUSP00000107251; ENSMUSG00000027075.
DR Ensembl; ENSMUST00000121114; ENSMUSP00000112642; ENSMUSG00000027075.
DR GeneID; 72401; -.
DR KEGG; mmu:72401; -.
DR UCSC; uc008kjk.1; mouse.
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; AIMWGWA; -.
DR OrthoDB; 639867at2759; -.
DR PhylomeDB; Q8BSM7; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 72401; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8BSM7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BSM7; protein.
DR Bgee; ENSMUSG00000027075; Expressed in hindlimb stylopod muscle and 113 other tissues.
DR ExpressionAtlas; Q8BSM7; baseline and differential.
DR Genevisible; Q8BSM7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; 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
