Mutant lesions in daf-2 alleles
| Allele | Classa | Mutation location location (domain) | DNA change | Amino acid change | Reference | Predicted outcome of mutationb |
|---|---|---|---|---|---|---|
| e979 | 2D | L1 | TGC-TAC | C146Y | This study | a |
| m631 | NC | L1 | CGA-TGA | R281STOP | This study | b |
| m41 | 1B | Cys-Rich | GGA-GAA | G383E | Yu et al. (2002) | c |
| mg43c | NC | Cys-Rich | TGT-TAT | C401Y | Kimura et al. (1998) | a |
| m579 | 2B | Cys-Rich | CGT-TGT | R437C | Scott et al. (2002) | d, h, i |
| sa187 | 2C | Cys-Rich | TGT-AGT | C469S | Kimura et al. (1998) | a |
| mg43c | NC | Cys-Rich | CCC-CTC | P470L | Kimura et al. (1998) | d |
| m596d | 1E | L2 | GGC-AGC | G547S | Scott et al. (2002) | e, h |
| e1368 | 1A | L2 | TCA-TTA | S573L | Kimura et al. (1998) | e |
| e1365/sa193e,f | 1A | L2 | TGC-TAC | A580T | Kimura et al. (1998); this study | f |
| sa229 | 1A | FnIII1 | GAT-AAT | D648N | Kimura et al. (1998) | g |
| mu150 | 1A | FnIII1 | GGC-GAC | G682D | This study | f |
| e1371 | 1A | FnIII2α | GGA-GAA | G803E | This study | d |
| m212 | 1D | FnIII2ID | TGT-TAT | C883Y | This study | a, h |
| m577f | 1C | FnIII2β | TGC-TAC | C1045Y | This study | a, h |
| m646 | NC | Prekinase | CAA-TAA | Q1223STOP | This study; K. Kimura and G. Ruvkun (personal communication) | b |
| sa219 | 2C | Kinase | GAT-AAT | D1374N | Kimura et al. (1998) | d |
| sa223 | 2E | Kinase | CGA-CAA | R1430Q | This study | d, h, i |
| e1391 | 2D | Kinase | CCC-CTC | P1434L | Kimura et al. (1998) | d, i |
| m65 | NC | Kinase | TGG-TAG | W1449STOP | This study | b |
| e1370 | 2C | Kinase | CCA-TCA | P1465S | Kimura et al. (1998) | d |
| m633 | NC | Kinase | CGT-CAT | R1510H | K. Kimura and G. Ruvkun (personal communication) | d |
| tm1236 | NC | Kinase | Deletion (see text) | This study |
↵a Classes as defined in Gems et al. (1998). NC, nonconditional Daf-c.
↵b a: Residue affected is a disulfide-bonded cysteine. Substitution is likely to disrupt fold stability. b: Nonsense mutation implying truncation of the polypeptide chain. Mutant protein is expected not to be functional. c: Residue affected is in a part of the sequence present only in nematodes. We were unable to predict the effect of substitution on the basis of homology to mammalian receptors. d: Residue affected is highly conserved in all phyla. Substitution is likely to affect stability of the structure or aspects of the receptor mechanism. e: Residue affected is solvent inaccessible and not highly conserved across phyla. The conservative nature of the substitution means that it is not predicted to have major detrimental effects. f: Residue affected is solvent inaccessible and not highly conserved across phyla. The nonconservative nature of the substitution suggests that it is likely to disrupt fold stability. g: Residue affected is solvent accessible and not highly conserved across phyla. Currently unable to predict effect of substitution. h: A nonidentical, naturally occurring, or engineered mutation in the equivalent hInsR position has been reported. i: An identical, naturally occurring, or engineered mutation in the equivalent hInsR position has been reported. For further details, see http://www.biochem.ucl.ac.uk/rilm.
↵c The mg43 allele has two lesions, both affecting the CR domain.
↵d Previously defined as class 2A (Gems et al. 1998). Given that this allele is suppressed by daf-12(m20), we have redesignated it as a class 1 allele.
↵e The e1365 and sa193 alleles were isolated in different labs but contain identical sequence changes.
↵f Sequence analysis revealed that the allele identified as e1365 in Gems et al. (1998) was in fact daf-2(m577). The real e1365 (Kimura et al. 1997) is a class 1A allele.