4F2_MOUSE
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 03-AUG-2022, entry version 194.
DE RecName: 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 SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 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 [12]
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 [13]
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 [14]
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, Pancreas,
RC 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 [15]
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: Component of several heterodimeric complexes involved in
CC amino acid transport (PubMed:9915839). The precise substrate
CC specificity depends on the other subunit in the heterodimer
CC (PubMed:9915839). The complexes function as amino acid exchangers (By
CC similarity). The homodimer functions as sodium-independent, high-
CC affinity transporter that mediates uptake of large neutral amino acids
CC such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine
CC and tryptophan (PubMed:9915839). The heterodimer formed by SLC3A2 and
CC SLC7A6 or SLC3A2 and SLC7A7 mediates the uptake of dibasic amino acids
CC (By similarity). The heterodimer with SLC7A5/LAT1 mediates the
CC transport of thyroid hormones triiodothyronine (T3) and thyroxine (T4)
CC across the cell membrane (By similarity). The heterodimer with
CC SLC7A5/LAT1 is involved in the uptake of toxic methylmercury (MeHg)
CC when administered as the L-cysteine or D,L-homocysteine complexes (By
CC similarity). The heterodimer with SLC7A5/LAT1 is involved in the uptake
CC of leucine (By similarity). When associated with LAPTM4B, the
CC heterodimer with SLC7A5/LAT1 is recruited to lysosomes to promote
CC leucine uptake into these organelles, and thereby mediates mTORC1
CC activation (By similarity). The heterodimer with SLC7A5/LAT1 may play a
CC role in the transport of L-DOPA across the blood-brain barrier
CC (Probable). The heterodimer formed by SLC3A2 and SLC7A5/LAT1 or SLC3A2
CC and SLC7A8/LAT2 is involved in the cellular activity of small molecular
CC weight nitrosothiols, via the stereoselective transport of L-
CC nitrosocysteine (L-CNSO) across the transmembrane (By similarity).
CC Together with ICAM1, regulates the transport activity of SLC7A8/LAT2 in
CC polarized intestinal cells by generating and delivering intracellular
CC signals (By similarity). Required for targeting of SLC7A5/LAT1 and
CC SLC7A8/LAT2 to the plasma membrane and for channel activity
CC (PubMed:9915839). Plays a role in nitric oxide synthesis in human
CC umbilical vein endothelial cells (HUVECs) via transport of L-arginine
CC (By similarity). May mediate blood-to-retina L-leucine transport across
CC the inner blood-retinal barrier (By similarity).
CC {ECO:0000250|UniProtKB:P08195, ECO:0000250|UniProtKB:Q794F9,
CC ECO:0000269|PubMed:9915839, ECO:0000305|PubMed:11011012}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with a non-glycosylated light
CC chain (SLC7A5, SLC7A6, SLCA7A7, SLC7A8, SLC7A10 or SLCA7A11)
CC (PubMed:9915839, PubMed:10574970, PubMed:11011012). Interacts with
CC TLCD3A/CT120 and ICAM1. Constitutively and specifically associates with
CC beta-1 integrins (alpha-2/beta-1, alpha-3/beta-1, alpha-5/beta-1 and
CC alpha-6/beta-1), but minimally with alpha-4/beta-1. Interacts with
CC LAPTM4B; recruits SLC3A2 and SLC7A5 to lysosomes to promote leucine
CC uptake into these organelles and is required for mTORC1 activation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08195,
CC ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11011012,
CC ECO:0000269|PubMed:9915839}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P08195}. Cell membrane
CC {ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:9915839}; Single-pass
CC type II membrane protein {ECO:0000250|UniProtKB:P08195}. Cell junction
CC {ECO:0000269|PubMed:9915839}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P08195}. Melanosome
CC {ECO:0000250|UniProtKB:P08195}. 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,
CC ECO:0000250|UniProtKB:P08195, 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 -!- MISCELLANEOUS: Leucine uptake was inhibited by ileum, valine histidine
CC and phenylalanine as well as by 2-aminobicyclo-(2,2,1)-heptane-2-
CC carboxylic acid (BCH) (a specific inhibitor of system L transport).
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};
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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; 13.
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 GlyGen; P10852; 8 sites, 7 N-linked glycans (3 sites).
DR iPTMnet; P10852; -.
DR PhosphoSitePlus; P10852; -.
DR SwissPalm; P10852; -.
DR EPD; P10852; -.
DR jPOST; P10852; -.
DR MaxQB; P10852; -.
DR PaxDb; P10852; -.
DR PeptideAtlas; P10852; -.
DR PRIDE; P10852; -.
DR ProteomicsDB; 286031; -. [P10852-1]
DR ProteomicsDB; 286032; -. [P10852-2]
DR Antibodypedia; 15042; 1043 antibodies from 46 providers.
DR DNASU; 17254; -.
DR Ensembl; ENSMUST00000010239; ENSMUSP00000010239; ENSMUSG00000010095. [P10852-1]
DR Ensembl; ENSMUST00000170157; ENSMUSP00000130194; ENSMUSG00000010095. [P10852-2]
DR GeneID; 17254; -.
DR KEGG; mmu:17254; -.
DR UCSC; uc008gmi.2; mouse. [P10852-2]
DR UCSC; uc012bib.1; mouse. [P10852-1]
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; SHWCSWS; -.
DR OrthoDB; 1384693at2759; -.
DR PhylomeDB; P10852; -.
DR TreeFam; TF314498; -.
DR Reactome; R-MMU-210991; Basigin interactions.
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 75 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 283 other tissues.
DR ExpressionAtlas; P10852; baseline and differential.
DR Genevisible; P10852; MM.
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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISS: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:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904273; P:L-alanine import across plasma membrane; 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; ISS:UniProtKB.
DR GO; GO:0015804; P:neutral amino acid transport; ISO:MGI.
DR GO; GO:0015823; P:phenylalanine transport; ISO:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR Gene3D; 2.60.40.1180; -; 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; PTHR46673; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16028; SLC3A2_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
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="4F2 cell-surface antigen heavy chain"
FT /id="PRO_0000064384"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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:0000255"
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:0000255"
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)"
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
