YLAT2_MOUSE
ID YLAT2_MOUSE Reviewed; 515 AA.
AC Q8BGK6; Q3TMY5; Q3U084; Q6ZQF5; Q8CFY3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Y+L amino acid transporter 2;
DE AltName: Full=Solute carrier family 7 member 6;
DE AltName: Full=y(+)L-type amino acid transporter 2;
DE Short=Y+LAT2;
DE Short=y+LAT-2;
GN Name=Slc7a6 {ECO:0000312|MGI:MGI:2142598};
GN Synonyms=Kiaa0245 {ECO:0000312|EMBL:BAC97909.1};
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:BAC97909.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC97909.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC33770.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33770.1}, and
RC NOD {ECO:0000312|EMBL:BAE33971.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC33770.1},
RC Embryonic stem cell {ECO:0000312|EMBL:BAE38304.1},
RC Embryonic stomach {ECO:0000312|EMBL:BAE37866.1},
RC Eye {ECO:0000312|EMBL:BAC35581.1}, Lung {ECO:0000312|EMBL:BAE38497.1}, and
RC Spleen {ECO:0000312|EMBL:BAE33971.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH38404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH38404.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH38404.1};
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-293 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10903140; DOI=10.1042/bj3490787;
RA Broeer A., Wagner C.A., Lang F., Broeer S.;
RT "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine
RT efflux in exchange with glutamine.";
RL Biochem. J. 349:787-795(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, 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).
CC -!- FUNCTION: Involved in the sodium-independent uptake of dibasic amino
CC acids and sodium-dependent uptake of some neutral amino acids. Requires
CC coexpression with SLC3A2/4F2hc to mediate the uptake of arginine,
CC leucine and glutamine. Also acts as an arginine/glutamine exchanger,
CC following an antiport mechanism for amino acid transport, influencing
CC arginine release in exchange for extracellular amino acids. Plays a
CC role in nitric oxide synthesis via transport of L-arginine. Involved in
CC the transport of L-arginine in monocytes. Reduces uptake of ornithine
CC in retinal pigment epithelial cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:Q92536}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q92536}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q92536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q8BGK6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14621295};
CC IsoId=Q8BGK6-2; Sequence=VSP_052833, VSP_052834;
CC -!- TISSUE SPECIFICITY: Strongest expression in brain but also detected in
CC testis, parotis, small intestine, heart and kidney. Weakly expressed in
CC spleen, lung and liver. {ECO:0000269|PubMed:10903140}.
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:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH38404.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC97909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129099; BAC97909.1; ALT_INIT; mRNA.
DR EMBL; AK049478; BAC33770.1; -; mRNA.
DR EMBL; AK053899; BAC35581.1; -; mRNA.
DR EMBL; AK157127; BAE33971.1; -; mRNA.
DR EMBL; AK164666; BAE37866.1; -; mRNA.
DR EMBL; AK165629; BAE38304.1; -; mRNA.
DR EMBL; AK165979; BAE38497.1; -; mRNA.
DR EMBL; BC038404; AAH38404.1; ALT_FRAME; mRNA.
DR CCDS; CCDS22631.1; -. [Q8BGK6-1]
DR RefSeq; NP_848913.1; NM_178798.3. [Q8BGK6-1]
DR RefSeq; XP_006531200.1; XM_006531137.3.
DR RefSeq; XP_006531201.1; XM_006531138.3. [Q8BGK6-1]
DR RefSeq; XP_017168357.1; XM_017312868.1. [Q8BGK6-1]
DR AlphaFoldDB; Q8BGK6; -.
DR SMR; Q8BGK6; -.
DR BioGRID; 237036; 1.
DR STRING; 10090.ENSMUSP00000034378; -.
DR iPTMnet; Q8BGK6; -.
DR PhosphoSitePlus; Q8BGK6; -.
DR EPD; Q8BGK6; -.
DR MaxQB; Q8BGK6; -.
DR PaxDb; Q8BGK6; -.
DR PeptideAtlas; Q8BGK6; -.
DR PRIDE; Q8BGK6; -.
DR ProteomicsDB; 275118; -. [Q8BGK6-1]
DR ProteomicsDB; 275119; -. [Q8BGK6-2]
DR Antibodypedia; 55124; 110 antibodies from 17 providers.
DR DNASU; 330836; -.
DR Ensembl; ENSMUST00000034378; ENSMUSP00000034378; ENSMUSG00000031904. [Q8BGK6-1]
DR GeneID; 330836; -.
DR KEGG; mmu:330836; -.
DR UCSC; uc009nfl.1; mouse. [Q8BGK6-1]
DR UCSC; uc009nfo.1; mouse. [Q8BGK6-2]
DR CTD; 9057; -.
DR MGI; MGI:2142598; Slc7a6.
DR VEuPathDB; HostDB:ENSMUSG00000031904; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000158295; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q8BGK6; -.
DR OMA; QIVFRRR; -.
DR OrthoDB; 621852at2759; -.
DR PhylomeDB; Q8BGK6; -.
DR TreeFam; TF313355; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 330836; 25 hits in 70 CRISPR screens.
DR ChiTaRS; Slc7a6; mouse.
DR PRO; PR:Q8BGK6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGK6; protein.
DR Bgee; ENSMUSG00000031904; Expressed in spermatocyte and 243 other tissues.
DR ExpressionAtlas; Q8BGK6; baseline and differential.
DR Genevisible; Q8BGK6; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015822; P:ornithine transport; ISO:MGI.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Antiport; Cell membrane;
KW Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Y+L amino acid transporter 2"
FT /id="PRO_0000341478"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_052833"
FT VAR_SEQ 165..216
FT /note="ACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQ
FT -> MFFFLPLPCFLSLFFFLLLFHLFNSPSVFFLFFTFLLSPFSFAWSPTRLCPT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_052834"
FT CONFLICT 129
FT /note="W -> R (in Ref. 2; BAE33971)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="L -> P (in Ref. 2; BAE38304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56771 MW; 8DF8352607228507 CRC64;
MEAQELGSPT PTYHLLPKAN QHTVKEDAGS PSQGSPETMQ LKKEISLLNG VSLVVGNMIG
SGIFVSPKGV LKYTASYGLS LIVWAIGGLF SVVGALCYAE LGTTITKSGA SYAYILEAFG
GFIAFIRLWV SLLIVEPTSQ AIIAITFANY IIKPSFPTCD PPYVACRLLA AACVCLLTFV
NCAYVKWGTR VQDTFTYAKV LALIAIIIMG LVKLCQGHTE HFQDAFKGSS WNVGDLSLAL
YSALFSYSGW DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNIQDVHK
SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG HLPNLLSMIH
IERFTPVPAL LFNCTMTLIY LVVKDVFLLI NYFSFSYWFF VGLSVVGQLY LRWKEPDWPR
PLKLSLFFPI VFCVCSLFLV AVPLFSDTIN SLIGIGIALS GVPVYFLGVY LPESRRPLFI
RNVLATVTRV TQKLCFCVLT ELDVTEEKNV ERKTD
