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large neutral amino acids transporter small subunit 4 (L-type amino L-acid transporter 4, solute carrier family 43 member 2, SLC43A2, LAT4, PP7664)

Function: - Na+, Cl-, pH-independent high affinity transport of large neutral amino acids Structure: - glycosylated (putative) - belongs to the SLC43A transporter (TC 2.A.1.44) family Compartment: membrane Alternative splicing: named isoforms=3 Expression: - detected in several tissues - higher expression in placenta, kidney & peripheral blood leukocytes - in kidney, detected in epithelial cells of the distal tubule & collecting duct - in the intestine, expressed mainly in crypt cells of the intestinal microvilli & epithelial cells in the base of the villus

General

amino acid transport protein glycoprotein phosphoprotein solute carrier family 43 (SLC43, SLC43A)

Properties

SIZE: entity length = 569 aa MW = 63 kD COMPARTMENT: cellular membrane MOTIF: transmembrane domain {TM1} transmembrane domain {TM2} transmembrane domain {TM3} transmembrane domain {TM4} transmembrane domain {TM5} transmembrane domain {TM6} transmembrane domain {TM7} transmembrane domain {TM8} transmembrane domain {TM9} transmembrane domain {TM10} transmembrane domain {TM11} transmembrane domain {TM12} transmembrane domain {20-40} N-glycosylation site {N55} N-glycosylation site {N58} transmembrane domain {90-110} transmembrane domain {120-140} cytoplasmic domain {N-TERMINAL} exoplasmic loop LOOP#: 1 exoplasmic loop LOOP#: 3 exoplasmic loop LOOP#: 4 exoplasmic loop LOOP#: 5 exoplasmic loop LOOP#: 6 transmembrane domain {143-163} transmembrane domain {177-197} transmembrane domain {203-223} Ser phosphorylation site {S274} transmembrane domain {323-345} transmembrane domain {365-385} lysine-rich region {409-413} MOTIF: lysine residue (SEVERAL) cytoplasmic domain {C-TERMINAL} transmembrane domain {435-455} transmembrane domain {462-482} transmembrane domain {490-510} transmembrane domain {516-536} N-glycosylation site {N560}

Database Correlations

UniProt Q8N370 Pfam PF07690

References

UniProt :accession Q8N370