| IED ID | IndEnz0001000891 |
| Enzyme Type ID | amylase000891 |
| Protein Name |
4F2 cell-surface antigen heavy chain 4F2hc Solute carrier family 3 member 2 CD antigen CD98 |
| Gene Name | Slc3a2 Mdu1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSQDTEVDMKDVELNELEPEKQPMNAADGAAAGEKNGLVKIKVAEDETEAGVKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPVQRWWHKGALYRIGDLQAFVGRDAGGIAGLKSHLEYLSTLKVKGLVLGPIHKNQKDEINETDLKQINPTLGSQEDFKDLLQSAKKKSIHIILDLTPNYQGQNAWFLPAQADIVATKMKEALSSWLQDGVDGFQFRDVGKLMNAPLYLAEWQNITKNLSEDRLLIAGTESSDLQQIVNILESTSDLLLTSSYLSNSTFTGERTESLVTRFLNATGSQWCSWSVSQAGLLADFIPDHLLRLYQLLLFTLPGTPVFSYGDELGLQGALPGQPAKAPLMPWNESSIFHIPRPVSLNMTVKGQNEDPGSLLTQFRRLSDLRGKERSLLHGDFHALSSSPDLFSYIRHWDQNERYLVVLNFRDSGRSARLGASNLPAGISLPASAKLLLSTDSARQSREEDTSLKLENLSLNPYEGLLLQFPFVA |
| Enzyme Length | 526 |
| Uniprot Accession Number | P10852 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of several heterodimeric complexes involved in amino acid transport (PubMed:9915839). The precise substrate specificity depends on the other subunit in the heterodimer (PubMed:9915839). The complexes function as amino acid exchangers (By similarity). The homodimer functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine and tryptophan (PubMed:9915839). The heterodimer formed by SLC3A2 and SLC7A6 or SLC3A2 and SLC7A7 mediates the uptake of dibasic amino acids (By similarity). The heterodimer with SLC7A5/LAT1 mediates the transport of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane (By similarity). The heterodimer with SLC7A5/LAT1 is involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes (By similarity). The heterodimer with SLC7A5/LAT1 is involved in the uptake of leucine (By similarity). When associated with LAPTM4B, the heterodimer with SLC7A5/LAT1 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (By similarity). The heterodimer with SLC7A5/LAT1 may play a role in the transport of L-DOPA across the blood-brain barrier (Probable). The heterodimer formed by SLC3A2 and SLC7A5/LAT1 or SLC3A2 and SLC7A8/LAT2 is involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane (By similarity). Together with ICAM1, regulates the transport activity of SLC7A8/LAT2 in polarized intestinal cells by generating and delivering intracellular signals (By similarity). Required for targeting of SLC7A5/LAT1 and SLC7A8/LAT2 to the plasma membrane and for channel activity (PubMed:9915839). Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine (By similarity). May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier (By similarity). {ECO:0000250|UniProtKB:P08195, ECO:0000250|UniProtKB:Q794F9, ECO:0000269|PubMed:9915839, ECO:0000305|PubMed:11011012}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (22); Chain (1); Compositional bias (1); Cross-link (2); Disulfide bond (1); Erroneous initiation (1); Glycosylation (8); Helix (22); Modified residue (6); Mutagenesis (1); Region (1); Topological domain (2); Transmembrane (1); Turn (4) |
| Keywords | 3D-structure;Alternative splicing;Amino-acid transport;Cell junction;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Isopeptide bond;Lysosome;Membrane;Phosphoprotein;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Transport;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: Expression induced by concanavalin-A stimulation. Induced during cell activation but is subsequently maintained at constant levels throughout the cell cycle in exponentially growing cells. {ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}. |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P08195}. Cell membrane {ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:9915839}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08195}. Cell junction {ECO:0000269|PubMed:9915839}. Lysosome membrane {ECO:0000250|UniProtKB:P08195}. Melanosome {ECO:0000250|UniProtKB:P08195}. Note=Localized at the plasma membrane when associated with SLC7A5 or SLC7A8. Localized to the apical membrane of placental syncytiotrophoblastic cells. Recruited to lysosomes by LAPTM4B (By similarity). Located selectively at cell-cell adhesion sites (PubMed:9915839). Colocalized with SLC7A8/LAT2 at the basolateral membrane of kidney proximal tubules and small intestine epithelia. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08195, ECO:0000269|PubMed:9915839}. |
| Modified Residue | MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P08195"; MOD_RES 5; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q794F9"; MOD_RES 58; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"; MOD_RES 300; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P08195"; MOD_RES 302; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P08195"; MOD_RES 420; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P08195" |
| Post Translational Modification | PTM: Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-protein kinases favors heterotypic cell-cell interactions. {ECO:0000250|UniProtKB:P08195}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6I9Q; 6SUA; |
| Mapped Pubmed ID | 10101682; 10734121; 11167010; 11751410; 12466851; 12520002; 12904583; 12927796; 1358795; 14517553; 14527684; 14610273; 14681479; 15522208; 15625115; 15713750; 15880135; 16399997; 16615898; 16707844; 1676980; 17273864; 17597067; 17682053; 17967808; 18799693; 19270713; 1959604; 1970801; 19841087; 2004789; 20340160; 20522643; 21266579; 21267068; 21490400; 21670318; 21677750; 21711689; 22457928; 22499850; 22588539; 22624878; 22641098; 22768207; 23055941; 23296466; 24491544; 24534009; 25002078; 25267066; 2531187; 26493331; 26836475; 27687603; 27908736; 28012647; 28320871; 29141216; 29906411; 30451822; 30696773; 31396687; 31789450; 32188932; 32463547; 3356451; 33665549; 33907288; 3476959; 6321791; 6402449; 6984005; 7719025; 7894154; 8358177; 8499657; 8554532; 8589516; 9027487; 9341170; 9501310; 9730611; 9763662; |
| Motif | |
| Gene Encoded By | |
| Mass | 58,337 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |