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lymphocyte function-associated antigen-1 (LFA-1, leukocyte adhesion protein LFA-1, integrin alpha-L/beta-2, CD11a/CD18)

Function: - receptor for ICAMs (ICAM1, ICAM2, ICAM3 & ICAM4) - role in a variety of immune phenomena including: a) leukocyte-endothelial cell interaction (adhesion) b) cytotoxic T-cell mediated killing c) antibody-dependent killing by granulocytes & monocytes - cytoskeletal reorganization (putative) Structure: - consists of: - integrin alpha-L (CD11a) - integrin beta-2 (CD18) Pathology: - defects associated with LFA-1 immunodeficiency disease Pharmacology: - LFA-1 antagonist lifitegrast (Xiidra) ophthalmic FDA-approved for treatment of xerophthalmia

Related

CD102; intercellular adhesion molecule 2; ICAM-2 (ICAM2) intercellular adhesion molecule 1; ICAM-1; major group rhinovirus receptor; CD54 (ICAM1) intercellular adhesion molecule 3; ICAM-3; ICAM-R; CDw50; CD50 (ICAM3) LFA-1 immunodeficiency disease lifitegrast (Xiidra)

General

integrin

Properties

COMPARTMENT: plasma membrane CELL: monocyte macrophage lymphocyte MOTIF: focal adhesion site transmembrane domain SUBUNITS: integrin alpha-L COMPARTMENT: cellular membrane MOTIF: signal sequence {1-25} FG-GAP {42-91} MOTIF: N-glycosylation site {N65} cysteine residue {C73} MODIFICATION: cysteine residue {C80} cysteine residue {C80} MODIFICATION: cysteine residue {C73} N-glycosylation site {N89} FG-GAP {92-149} MOTIF: cysteine residue {C111} MODIFICATION: cysteine residue {C129} cysteine residue {C129} MODIFICATION: cysteine residue {C111} VWFA domain {156-327} MOTIF: N-glycosylation site {N188} FG-GAP {350-400} FG-GAP {401-455} FG-GAP {457-516} MOTIF: Ca+2-binding site SITE: 468-476 FG-GAP {518-575} MOTIF: Ca+2-binding site SITE: 530-538 FG-GAP {578-630} MOTIF: Ca+2-binding site SITE: 590-598 N-glycosylation site {N649} cysteine residue {C653} MODIFICATION: cysteine residue {C707} N-glycosylation site {N670} cysteine residue {C707} MODIFICATION: cysteine residue {C653} N-glycosylation site {N726} N-glycosylation site {N730} cysteine residue {C771} MODIFICATION: cysteine residue {C777} cysteine residue {C777} MODIFICATION: cysteine residue {C771} cysteine residue {C845} MODIFICATION: cysteine residue {C861} cysteine residue {C861} MODIFICATION: cysteine residue {C845} N-glycosylation site {N862} N-glycosylation site {N885} N-glycosylation site {N897} cysteine residue {C998} MODIFICATION: cysteine residue {C1013} cysteine residue {C1013} MODIFICATION: cysteine residue {C998} cysteine residue {C1021} MODIFICATION: cysteine residue {C1052} cysteine residue {C1052} MODIFICATION: cysteine residue {C1021} N-glycosylation site {N1060} N-glycosylation site {N1071} transmembrane domain {1091-1111} GFFKR {1115-1119} integrin beta-2 COMPARTMENT: cellular membrane MOTIF: signal sequence {1-22} cysteine residue {C25} MODIFICATION: cysteine residue {C447} cysteine residue {C33} MODIFICATION: cysteine residue {C43} cysteine residue {C36} MODIFICATION: cysteine residue {C73} cysteine residue {C43} MODIFICATION: cysteine residue {C33} cysteine residue {C46} MODIFICATION: cysteine residue {C62} N-glycosylation site {N50} cysteine residue {C62} MODIFICATION: cysteine residue {C46} cysteine residue {C73} MODIFICATION: cysteine residue {C36} N-glycosylation site {N116} VWFA domain {124-363} MOTIF: cysteine residue {C191} MODIFICATION: cysteine residue {C198} cysteine residue {C198} MODIFICATION: cysteine residue {C191} N-glycosylation site {N212} cysteine residue {C246} MODIFICATION: cysteine residue {C286} N-glycosylation site {N254} cysteine residue {C286} MODIFICATION: cysteine residue {C246} cysteine residue {C386} MODIFICATION: cysteine residue {C400} Cell attachment site {397-399} cysteine residue {C400} MODIFICATION: cysteine residue {C386} cysteine residue {C420} MODIFICATION: cysteine residue {C662} cysteine residue {C445} MODIFICATION: cysteine residue {C449} cysteine residue {C447} MODIFICATION: cysteine residue {C25} Cysteine-rich tandem repeats {449-617} MOTIF: I {449-496} cysteine residue {C449} MODIFICATION: cysteine residue {C445} cysteine residue {C459} MODIFICATION: cysteine residue {C470} cysteine residue {C467} MODIFICATION: cysteine residue {C506} cysteine residue {C470} MODIFICATION: cysteine residue {C459} cysteine residue {C472} MODIFICATION: cysteine residue {C481} cysteine residue {C481} MODIFICATION: cysteine residue {C472} cysteine residue {C483} MODIFICATION: cysteine residue {C497} II {497-540} cysteine residue {C497} MODIFICATION: cysteine residue {C483} N-glycosylation site {N501} cysteine residue {C506} MODIFICATION: cysteine residue {C467} cysteine residue {C512} MODIFICATION: cysteine residue {C517} cysteine residue {C514} MODIFICATION: cysteine residue {C549} cysteine residue {C517} MODIFICATION: cysteine residue {C512} cysteine residue {C519} MODIFICATION: cysteine residue {C534} cysteine residue {C534} MODIFICATION: cysteine residue {C519} cysteine residue {C536} MODIFICATION: cysteine residue {C541} III {541-581} cysteine residue {C541} MODIFICATION: cysteine residue {C536} cysteine residue {C549} MODIFICATION: cysteine residue {C514} cysteine residue {C557} MODIFICATION: cysteine residue {C562} cysteine residue {C559} MODIFICATION: cysteine residue {C590} cysteine residue {C562} MODIFICATION: cysteine residue {C557} cysteine residue {C564} MODIFICATION: cysteine residue {C573} cysteine residue {C573} MODIFICATION: cysteine residue {C564} cysteine residue {C575} MODIFICATION: cysteine residue {C582} IV {582-617} cysteine residue {C582} MODIFICATION: cysteine residue {C575} cysteine residue {C590} MODIFICATION: cysteine residue {C559} cysteine residue {C596} MODIFICATION: cysteine residue {C601} cysteine residue {C598} MODIFICATION: cysteine residue {C643} cysteine residue {C601} MODIFICATION: cysteine residue {C596} cysteine residue {C603} MODIFICATION: cysteine residue {C612} cysteine residue {C612} MODIFICATION: cysteine residue {C603} cysteine residue {C615} MODIFICATION: cysteine residue {C618} cysteine residue {C618} MODIFICATION: cysteine residue {C615} cysteine residue {C622} MODIFICATION: cysteine residue {C631} cysteine residue {C628} MODIFICATION: cysteine residue {C695} cysteine residue {C631} MODIFICATION: cysteine residue {C622} N-glycosylation site {N642} cysteine residue {C643} MODIFICATION: cysteine residue {C598} cysteine residue {C647} MODIFICATION: cysteine residue {C670} cysteine residue {C662} MODIFICATION: cysteine residue {C420} cysteine residue {C670} MODIFICATION: cysteine residue {C647} cysteine residue {C695} MODIFICATION: cysteine residue {C628} transmembrane domain {701-723} Ser phosphorylation site {S745} Ser phosphorylation site {S756} Thr phosphorylation site {T758} Thr phosphorylation site {T759} Thr phosphorylation site {T760} MISC-INFO: LIGAND = ICAM_1 LIGAND = ICAM_2 LIGAND = ICAM_3

References

  1. UniProt :accession P13598
  2. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
  3. Kelleher D, Murphy A, Cullen D. Leukocyte function-associated antigen 1 (LFA-1) is a signaling molecule for cytoskeletal changes in a human T cell line. Eur J Immunol. 1990 Oct;20(10):2351-4. PMID: 2242762
  4. Hibbs ML, Xu H, Stacker SA, Springer TA. Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit. Science. 1991 Mar 29;251(5001):1611-3. PMID: 1672776
  5. FDA News Release. July 12, 2016 FDA approves new medication for dry eye disease http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm510720.htm

Components

CD11a; integrin alpha-L; leukocyte adhesion glycoprotein LFA-1 alpha chain; LFA-1A; leukocyte function-associated molecule 1 alpha chain; CD11 antigen-like family member A (ITGAL, CD11A) CD18 (integrin beta-2, L-CAM beta, ITGB2, CD18, MFI7)