u-PAR/Ly-6 domain | |||||||||||
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Identifiers | |||||||||||
Symbol | UPAR_LY6 | ||||||||||
Pfam | PF00021 | ||||||||||
InterPro | IPR001526 | ||||||||||
PROSITE | PDOC00756 | ||||||||||
CATH | 1erg | ||||||||||
SCOP2 | 1erg / SCOPe / SUPFAM | ||||||||||
CDD | cd00117 | ||||||||||
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The LU domain ( Ly-6 antigen/ uPAR) is an evolutionarily conserved protein domain of the three-finger protein superfamily. This domain is found in the extracellular domains of cell-surface receptors and in either GPI-anchored or secreted globular proteins, for example the Ly-6 family, CD59, and Sgp-2. [2] [3]
A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved LU domain of about 100 amino-acid residues. [4] [5] Among these proteins, most contain only a single LU domain, though small numbers of exceptions are known; well-studied family member uPAR has three tandem LU domains. [3]
This domain folds into five antiparallel beta sheets, a structure common to the three-finger protein family. The domain typically contains ten well- conserved cysteine residues involved in five disulfide bonds, though some examples such as two of the three uPAR domains have fewer. [3]
Besides uPAR, other receptors with LU domains include members of the transforming growth factor beta receptor (TGF-beta) superfamily, such as the activin type 2 receptor; [6] and bone morphogenetic protein receptor, type IA. [7] Other LU domain proteins are small globular proteins such as CD59 antigen, LYNX1, SLURP1, and SLURP2. [2] [8]
ARS; CD177; CD59; LY6D; LY6E; LY6H; LYNX1; LYPD2; LYPD3; LYPD4; LYPD5; LYPD6; PLAUR; PSCA; SLURP2; SLURP1; SPACA4; TEX101;
Many LU domain containing proteins are involved in cholinergic signaling and bind acetylcholine receptors, notably linking their function to a common mechanism of 3FTx toxicity. [2] [3] [9] Members of the Ly6/uPAR family are believed to be the evolutionary ancestors of the three-finger toxin (3FTx). [10] Other LU proteins, such as the CD59 antigen, have well-studied functions in regulation of the immune system. [9]
u-PAR/Ly-6 domain | |||||||||||
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Identifiers | |||||||||||
Symbol | UPAR_LY6 | ||||||||||
Pfam | PF00021 | ||||||||||
InterPro | IPR001526 | ||||||||||
PROSITE | PDOC00756 | ||||||||||
CATH | 1erg | ||||||||||
SCOP2 | 1erg / SCOPe / SUPFAM | ||||||||||
CDD | cd00117 | ||||||||||
|
The LU domain ( Ly-6 antigen/ uPAR) is an evolutionarily conserved protein domain of the three-finger protein superfamily. This domain is found in the extracellular domains of cell-surface receptors and in either GPI-anchored or secreted globular proteins, for example the Ly-6 family, CD59, and Sgp-2. [2] [3]
A variety of GPI-linked cell-surface glycoproteins are composed of one or more copies of a conserved LU domain of about 100 amino-acid residues. [4] [5] Among these proteins, most contain only a single LU domain, though small numbers of exceptions are known; well-studied family member uPAR has three tandem LU domains. [3]
This domain folds into five antiparallel beta sheets, a structure common to the three-finger protein family. The domain typically contains ten well- conserved cysteine residues involved in five disulfide bonds, though some examples such as two of the three uPAR domains have fewer. [3]
Besides uPAR, other receptors with LU domains include members of the transforming growth factor beta receptor (TGF-beta) superfamily, such as the activin type 2 receptor; [6] and bone morphogenetic protein receptor, type IA. [7] Other LU domain proteins are small globular proteins such as CD59 antigen, LYNX1, SLURP1, and SLURP2. [2] [8]
ARS; CD177; CD59; LY6D; LY6E; LY6H; LYNX1; LYPD2; LYPD3; LYPD4; LYPD5; LYPD6; PLAUR; PSCA; SLURP2; SLURP1; SPACA4; TEX101;
Many LU domain containing proteins are involved in cholinergic signaling and bind acetylcholine receptors, notably linking their function to a common mechanism of 3FTx toxicity. [2] [3] [9] Members of the Ly6/uPAR family are believed to be the evolutionary ancestors of the three-finger toxin (3FTx). [10] Other LU proteins, such as the CD59 antigen, have well-studied functions in regulation of the immune system. [9]