ID 4F2_MOUSE Reviewed; 526 AA. AC P10852; G3UWA6; Q54AH5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 24-JAN-2024, entry version 202. DE RecName: Full=Amino acid transporter heavy chain SLC3A2 {ECO:0000305}; DE AltName: Full=4F2 cell-surface antigen heavy chain {ECO:0000303|PubMed:2928113}; DE Short=4F2hc {ECO:0000250|UniProtKB:P08195}; DE AltName: Full=Solute carrier family 3 member 2 {ECO:0000250|UniProtKB:P08195}; DE AltName: CD_antigen=CD98; GN Name=Slc3a2 {ECO:0000312|MGI:MGI:96955}; Synonyms=Mdu1; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION. RC STRAIN=C57BL/6 X DBA/2, and ICR; TISSUE=Macrophage, and Pre-B cell; RX PubMed=2928113; DOI=10.1093/nar/17.5.1915; RA Parmacek M.S., Karpinski B.A., Gottsdiener K.M., Thompson C.B., RA Leiden J.M.; RT "Structure, expression and regulation of the murine 4F2 heavy chain."; RL Nucleic Acids Res. 17:1915-1931(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=ICR; TISSUE=Brain; RA Kanai Y., Watanabe M., Endou H.; RT "Localization of expression of system L neutral amino acid transporter LAT1 RT in brain."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis; 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 GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP PROTEIN SEQUENCE OF 43-53; 163-171; 456-463 AND 488-496, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [8] RP FUNCTION, SUBUNIT, INTERACTION WITH SLC7A5, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND MUTAGENESIS OF CYS-103. RC STRAIN=BALB/cJ; RX PubMed=9915839; DOI=10.1074/jbc.274.5.3009; RA Nakamura E., Sato M., Yang H., Miyagawa F., Harasaki M., Tomita K., RA Matsuoka S., Noma A., Iwai K., Minato N.; RT "4F2 (CD98) heavy chain is associated covalently with an amino acid RT transporter and controls intracellular trafficking and membrane topology of RT 4F2 heterodimer."; RL J. Biol. Chem. 274:3009-3016(1999). RN [9] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, AND INTERACTION WITH RP SLC7A8. 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 [10] RP FUNCTION, AND SUBUNIT. RX PubMed=11011012; DOI=10.1016/s0006-8993(00)02758-x; RA Kageyama T., Nakamura M., Matsuo A., Yamasaki Y., Takakura Y., Hashida M., RA Kanai Y., Naito M., Tsuruo T., Minato N., Shimohama S.; RT "The 4F2hc/LAT1 complex transports L-DOPA across the blood-brain barrier."; RL Brain Res. 879:115-121(2000). RN [11] RP FUNCTION, SUBUNIT, AND INTERACTION WITH SLC7A10. RC TISSUE=Brain; RX PubMed=10734121; DOI=10.1074/jbc.275.13.9690; RA Fukasawa Y., Segawa H., Kim J.Y., Chairoungdua A., Kim D.K., Matsuo H., RA Cha S.H., Endou H., Kanai Y.; RT "Identification and characterization of a Na+-independent neutral amino RT acid transporter that associates with the 4F2 heavy chain and exhibits RT substrate selectivity for small neutral D- and L- amino acids."; RL J. Biol. Chem. 275:9690-9698(2000). RN [12] RP DISRUPTION PHENOTYPE. RX PubMed=12927796; DOI=10.1016/s0006-291x(03)01473-6; RA Tsumura H., Suzuki N., Saito H., Kawano M., Otake S., Kozuka Y., Komada H., RA Tsurudome M., Ito Y.; RT "The targeted disruption of the CD98 gene results in embryonic lethality."; RL Biochem. Biophys. Res. Commun. 308:847-851(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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 [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-259; ASN-385 AND RP ASN-399. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-259; ASN-385 AND RP ASN-399. 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 105-526. RX PubMed=30958588; DOI=10.1002/prot.25686; RA Deuschle F.C., Schiefner A., Skerra A.; RT "Structural differences between the ectodomains of murine and human RT CD98hc."; RL Proteins 87:693-698(2019). CC -!- FUNCTION: Acts as a chaperone that facilitates biogenesis and CC trafficking of functional transporters heterodimers to the plasma CC membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, CC SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid CC antiporters (PubMed:9915839, PubMed:10574970, PubMed:11011012, CC PubMed:10734121). Heterodimers function as amino acids exchangers, the CC specificity of the substrate depending on the SLC7A subunit. CC Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of CC dibasic amino acids. Heterodimer SLC3A2/SLC7A11 functions as an CC antiporter by mediating the exchange of extracellular anionic L-cystine CC and intracellular L-glutamate across the cellular plasma membrane (By CC similarity). SLC3A2/SLC7A10 translocates small neutral L- and D-amino CC acids across the plasma membrane (By similarity). SLC3A2/SLC75 or CC SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, CC thyroid hormones and L-DOPA. SLC3A2 is essential for plasma membrane CC localization, stability, and the transport activity of SLC7A5 and CC SLC7A8. When associated with LAPTM4B, the heterodimer SLC7A5 is CC recruited to lysosomes to promote leucine uptake into these organelles, CC and thereby mediates mTORC1 activation. Modulates integrin-related CC signaling and is essential for integrin-dependent cell spreading, CC migration and tumor progression (By similarity). CC {ECO:0000250|UniProtKB:P08195, ECO:0000250|UniProtKB:P63115, CC ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:10734121, CC ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:9915839}. CC -!- SUBUNIT: Disulfide-linked heterodimer with a non-glycosylated light CC chain (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 or SLC7A11) CC (PubMed:9915839, PubMed:10574970, PubMed:11011012, PubMed:10734121). CC Interacts with TLCD3A/CT120 and ICAM1. Constitutively and specifically CC associates with beta-1 integrins (alpha-2/beta-1, alpha-3/beta-1, CC alpha-5/beta-1 and alpha-6/beta-1), but minimally with alpha-4/beta-1. CC Interacts with LAPTM4B; recruits SLC3A2 and SLC7A5 to lysosomes to CC promote leucine uptake into these organelles and is required for mTORC1 CC activation (By similarity). {ECO:0000250|UniProtKB:P08195, CC ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:10734121, CC ECO:0000269|PubMed:11011012, ECO:0000269|PubMed:9915839}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000250|UniProtKB:P08195}. Cell membrane CC {ECO:0000269|PubMed:9915839}; Single-pass type II membrane protein CC {ECO:0000250|UniProtKB:P08195}. Cell junction CC {ECO:0000269|PubMed:9915839}. Lysosome membrane CC {ECO:0000250|UniProtKB:P08195}. Melanosome CC {ECO:0000250|UniProtKB:P08195}. Basolateral cell membrane CC {ECO:0000269|PubMed:10574970}. Note=Localized at the plasma membrane CC when associated with SLC7A5 or SLC7A8. Localized to the apical membrane CC of placental syncytiotrophoblastic cells. Recruited to lysosomes by CC LAPTM4B (By similarity). Located selectively at cell-cell adhesion CC sites (PubMed:9915839). Colocalized with SLC7A8/LAT2 at the basolateral CC membrane of kidney proximal tubules and small intestine epithelia. CC Expressed in both luminal and abluminal membranes of brain capillary CC endothelial cells (By similarity). {ECO:0000250|UniProtKB:P08195, CC ECO:0000250|UniProtKB:Q794F9, ECO:0000269|PubMed:10574970, CC ECO:0000269|PubMed:9915839}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P10852-1; Sequence=Displayed; CC Name=2; CC IsoId=P10852-2; Sequence=VSP_054953; CC -!- TISSUE SPECIFICITY: Detected on the surface of embryonic epithelial CC cells in the epidermis, thymus, kidney, intestine, brain choroid CC plexus, and in retina. Detected in adult and embryonic brain, spleen, CC kidney, intestine and liver, and in adult testis (at protein level) CC (PubMed:9915839). Observed in all adult tissues tested with strongest CC expression in kidney, small intestine, spleen, thymus and liver CC (PubMed:9915839). Moderate expression in brain, stomach, heart, testis, CC lung, skin, pancreas and skeletal muscle. In brain expressed on CC capillary endothelia in cerebral cortex. {ECO:0000269|PubMed:10574970, CC ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}. CC -!- DEVELOPMENTAL STAGE: Strong expression in the liver of 14 dpc embryo CC and in brain, spleen, liver, kidney and intestine of an 18 dpc embryo. CC {ECO:0000269|PubMed:9915839}. CC -!- INDUCTION: Expression induced by concanavalin-A stimulation. Induced CC during cell activation but is subsequently maintained at constant CC levels throughout the cell cycle in exponentially growing cells. CC {ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}. CC -!- PTM: Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto- CC protein kinases favors heterotypic cell-cell interactions. CC {ECO:0000250|UniProtKB:P08195}. CC -!- PTM: N-glycosylated; N-glycosylation is crucial for trafficking and CC stability of SLC3A2 to the plasma membrane. CC {ECO:0000250|UniProtKB:P08195}. CC -!- DISRUPTION PHENOTYPE: Embryonically lethal between 3.5 and 9.5 dpc. CC {ECO:0000269|PubMed:12927796}. CC -!- SIMILARITY: Belongs to the SLC3A transporter family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE36291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; X14309; CAA32490.1; -; mRNA. DR EMBL; AB023408; BAA90555.1; -; mRNA. DR EMBL; AK161280; BAE36291.1; ALT_INIT; mRNA. DR EMBL; AK165417; BAE38172.1; -; mRNA. DR EMBL; AC025794; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466612; EDL33352.1; -; Genomic_DNA. DR EMBL; BC065173; AAH65173.1; -; mRNA. DR CCDS; CCDS29540.1; -. [P10852-1] DR CCDS; CCDS50381.1; -. [P10852-2] DR PIR; S03600; S03600. DR RefSeq; NP_001154885.1; NM_001161413.1. [P10852-2] DR RefSeq; NP_032603.3; NM_008577.4. [P10852-1] DR RefSeq; XP_017173567.1; XM_017318078.1. [P10852-1] DR PDB; 6I9Q; X-ray; 2.10 A; A=105-526. DR PDB; 6SUA; X-ray; 2.75 A; B/D=105-526. DR PDBsum; 6I9Q; -. DR PDBsum; 6SUA; -. DR AlphaFoldDB; P10852; -. DR SMR; P10852; -. DR BioGRID; 201377; 19. DR IntAct; P10852; 5. DR MINT; P10852; -. DR STRING; 10090.ENSMUSP00000130194; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR TCDB; 2.A.3.8.5; the amino acid-polyamine-organocation (apc) family. DR GlyConnect; 2098; 7 N-Linked glycans (3 sites). DR GlyCosmos; P10852; 8 sites, 7 glycans. DR GlyGen; P10852; 9 sites, 7 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P10852; -. DR PhosphoSitePlus; P10852; -. DR SwissPalm; P10852; -. DR EPD; P10852; -. DR jPOST; P10852; -. DR MaxQB; P10852; -. DR PaxDb; 10090-ENSMUSP00000130194; -. DR PeptideAtlas; P10852; -. DR ProteomicsDB; 286031; -. [P10852-1] DR ProteomicsDB; 286032; -. [P10852-2] DR Pumba; P10852; -. DR Antibodypedia; 15042; 1216 antibodies from 46 providers. DR DNASU; 17254; -. DR Ensembl; ENSMUST00000010239.6; ENSMUSP00000010239.5; ENSMUSG00000010095.14. [P10852-1] DR Ensembl; ENSMUST00000170157.8; ENSMUSP00000130194.2; ENSMUSG00000010095.14. [P10852-2] DR GeneID; 17254; -. DR KEGG; mmu:17254; -. DR UCSC; uc008gmi.2; mouse. [P10852-2] DR UCSC; uc012bib.1; mouse. [P10852-1] DR AGR; MGI:96955; -. DR CTD; 6520; -. DR MGI; MGI:96955; Slc3a2. DR VEuPathDB; HostDB:ENSMUSG00000010095; -. DR eggNOG; KOG0471; Eukaryota. DR GeneTree; ENSGT00940000156646; -. DR HOGENOM; CLU_006462_9_0_1; -. DR InParanoid; P10852; -. DR OMA; APFMLWD; -. DR OrthoDB; 4266085at2759; -. DR PhylomeDB; P10852; -. DR TreeFam; TF314498; -. DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane. DR Reactome; R-MMU-71240; Tryptophan catabolism. DR BioGRID-ORCS; 17254; 23 hits in 80 CRISPR screens. DR ChiTaRS; Slc3a2; mouse. DR PRO; PR:P10852; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; P10852; Protein. DR Bgee; ENSMUSG00000010095; Expressed in placenta labyrinth and 287 other cell types or tissues. DR ExpressionAtlas; P10852; baseline and differential. DR GO; GO:1990184; C:amino acid transport complex; ISO:MGI. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0044225; C:apical pole of neuron; IDA:MGI. DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; ISO:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0140272; F:exogenous protein binding; ISO:MGI. DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI. DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:MGI. DR GO; GO:0005294; F:neutral L-amino acid secondary active transmembrane transporter activity; ISO:MGI. DR GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0015818; P:isoleucine transport; ISO:MGI. DR GO; GO:1904273; P:L-alanine import across plasma membrane; ISO:MGI. DR GO; GO:1902024; P:L-histidine transport; ISO:MGI. DR GO; GO:1903801; P:L-leucine import across plasma membrane; ISS:UniProtKB. DR GO; GO:0098713; P:leucine import across plasma membrane; ISO:MGI. DR GO; GO:0015820; P:leucine transport; IDA:UniProtKB. DR GO; GO:0015821; P:methionine transport; ISO:MGI. DR GO; GO:0015804; P:neutral amino acid transport; ISO:MGI. DR GO; GO:0015823; P:phenylalanine transport; ISO:MGI. DR GO; GO:0015824; P:proline transport; ISO:MGI. DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:MGI. DR GO; GO:0070327; P:thyroid hormone transport; ISO:MGI. DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB. DR GO; GO:0015828; P:tyrosine transport; ISO:MGI. DR GO; GO:0015829; P:valine transport; ISO:MGI. DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR042280; SLC3A2. DR InterPro; IPR031984; SLC3A2_N. DR PANTHER; PTHR46673; 4F2 CELL-SURFACE ANTIGEN HEAVY CHAIN; 1. DR PANTHER; PTHR46673:SF1; 4F2 CELL-SURFACE ANTIGEN HEAVY CHAIN; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF16028; SLC3A2_N; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR Genevisible; P10852; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amino-acid transport; Cell junction; KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Isopeptide bond; Lysosome; Membrane; Phosphoprotein; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation. FT CHAIN 1..526 FT /note="Amino acid transporter heavy chain SLC3A2" FT /id="PRO_0000064384" FT TOPO_DOM 1..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P08195" FT TRANSMEM 76..99 FT /note="Helical; Signal-anchor for type II membrane protein" FT TOPO_DOM 100..526 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P08195" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08195" FT MOD_RES 5 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q794F9" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08195" FT MOD_RES 302 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08195" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08195" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 263 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250|UniProtKB:P08195" FT CARBOHYD 385 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 399 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973, FT ECO:0000269|PubMed:19656770" FT CARBOHYD 509 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 103 FT /note="Interchain (with C-164 in SLC7A5; C-158 in SLC7A11 FT and C-153 in SLC7A8)" FT /evidence="ECO:0000250|UniProtKB:P08195, FT ECO:0000305|PubMed:9915839" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P08195" FT CROSSLNK 59 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P08195" FT VAR_SEQ 1 FT /note="M -> MDPEPTEHSTDGVSVPRQPPSAQTGLDVQVVSAAGDSGTM (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_054953" FT MUTAGEN 103 FT /note="C->S: Loss of interchain disulfide bond. No effect FT on guidance of SLC7A5 to the plasma membrane." FT /evidence="ECO:0000269|PubMed:9915839" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 123..127 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 133..138 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 141..146 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:6I9Q" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 180..192 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:6I9Q" FT TURN 203..206 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 217..233 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 250..264 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 269..273 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 279..287 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 306..319 FT /evidence="ECO:0007829|PDB:6I9Q" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 335..338 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 354..361 FT /evidence="ECO:0007829|PDB:6I9Q" FT TURN 362..367 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 402..406 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 412..425 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 427..431 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 433..436 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 443..449 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 455..461 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 484..492 FT /evidence="ECO:0007829|PDB:6I9Q" FT HELIX 494..500 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:6I9Q" FT STRAND 517..522 FT /evidence="ECO:0007829|PDB:6I9Q" SQ SEQUENCE 526 AA; 58337 MW; AE6261F11C7D9468 CRC64; MSQDTEVDMK DVELNELEPE KQPMNAADGA AAGEKNGLVK IKVAEDETEA GVKFTGLSKE ELLKVAGSPG WVRTRWALLL LFWLGWLGML AGAVVIIVRA PRCRELPVQR WWHKGALYRI GDLQAFVGRD AGGIAGLKSH LEYLSTLKVK GLVLGPIHKN QKDEINETDL KQINPTLGSQ EDFKDLLQSA KKKSIHIILD LTPNYQGQNA WFLPAQADIV ATKMKEALSS WLQDGVDGFQ FRDVGKLMNA PLYLAEWQNI TKNLSEDRLL IAGTESSDLQ QIVNILESTS DLLLTSSYLS NSTFTGERTE SLVTRFLNAT GSQWCSWSVS QAGLLADFIP DHLLRLYQLL LFTLPGTPVF SYGDELGLQG ALPGQPAKAP LMPWNESSIF HIPRPVSLNM TVKGQNEDPG SLLTQFRRLS DLRGKERSLL HGDFHALSSS PDLFSYIRHW DQNERYLVVL NFRDSGRSAR LGASNLPAGI SLPASAKLLL STDSARQSRE EDTSLKLENL SLNPYEGLLL QFPFVA //