aap-1 encodes the C. elegans ortholog of the phosphoinositide 3-kinase (PI3K) p50/p55 adaptor/regulatory subunit; AAP-1 negatively regulates lifespan and dauer development, and likely functions as the sole adaptor subunit for the AGE-1/p110 PI3K catalytic subunit to which it binds in vitro; although AAP-1 potentiates insulin-like signaling, it is not absolutely required for insulin-like signaling under most conditions.
aat-1 encodes an amino acid transporter catalytic subunit; when co-expressed in Xenopus oocytes with the ATG-2 glycoprotein subunit, AAT-1 is able to facilitate amino acid uptake and exchange, showing a relatively high affinity for small and some large neutral amino acids; in addition, AAT-1 is able to covalently associate with ATG-2 or ATG-1 to form heterodimers in the Xenopus expression system; when co-expressed with ATG-2, AAT-1 localizes to the cell surface of oocytes, but when expressed alone or with ATG-1, AAT-1 localizes intracellularly.
aat-2 encodes a predicted amino acid transporter catalytic subunit; when co-expressed in Xenopus oocytes with a glycoprotein subunit, however, AAT-2 is not able to induce amino acid uptake.
aat-3 encodes an amino acid transporter catalytic subunit; when co-expressed in Xenopus oocytes with the ATG-2 glycoprotein subunit, AAT-3 is able to facilitate amino acid uptake and exchange, showing a relatively high affinity for small and some large neutral amino acids; in addition, AAT-3 is able to covalently associate with ATG-2 or ATG-1 to form heterodimers in the Xenopus expression system; when co-expressed with ATG-2, AAT-3 localizes to the cell surface of oocytes, but when expressed alone, or with ATG-1, AAT-3 localizes intracellularly.
aat-4 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-4 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-4 does not require this residue for heterodimer formation or, alternatively, does not require the glycoprotein subunit for function.
aat-5 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-5 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-5 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-5 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-5 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-5 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-5 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-5 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-5 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-6 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-6 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-6 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-6 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-6 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-6 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-8 encodes a predicted amino acid transporter catalytic subunit; unlike catalytic subunits in other organisms, however, AAT-8 does not contain the highly conserved cysteine residue known to facilitate covalent interaction with a glycoprotein subunit, suggesting that AAT-8 does not require this residue for heterodimer formation or alternatively, does not require the glycoprotein subunit for function.
aat-9 encodes an amino acid transporter catalytic subunit; AAT-9 lacks the conserved cysteine residue proposed to be essential for association with a glycoprotein subunit, and when expressed alone in Xenopus ooctyes, AAT-9 can localize to the cell surface and function as an aromatic amino acid exchanger that displays substrate-activated anion conductance; nevertheless, AAT-9 activity is enhanced by co-expression with the ATG-1 and ATG-2 glycoprotein subunits; an aat-9::gfp promoter fusion directs expression in anterior neurons, including some chemosensory neurons, as well as in some anterior body wall muscles.
aat-9 encodes an amino acid transporter catalytic subunit; AAT-9 lacks the conserved cysteine residue proposed to be essential for association with a glycoprotein subunit, and when expressed alone in Xenopus ooctyes, AAT-9 can localize to the cell surface and function as an aromatic amino acid exchanger that displays substrate-activated anion conductance; nevertheless, AAT-9 activity is enhanced by co-expression with the ATG-1 and ATG-2 glycoprotein subunits; an aat-9::gfp promoter fusion directs expression in anterior neurons, including some chemosensory neurons, as well as in some anterior body wall muscles.
abf-4 encodes a homolog of the antibacterial factor ASABF from Ascaris suum; ABF-4 may play a role in innate immunity, though at present the only evidence for its having an antimicrobial humoral function is its sequence similarity.
abf-6 encodes a homolog of the antibacterial factor ASABF from Ascaris suum; ABF-6 may play a role in innate immunity, though at present the only evidence for its having an antimicrobial humoral function is its sequence similarity.
abl-1 encodes, by alternative splicing, three isoforms of a Src homology (SH) 2 and 3 domain-containing non-receptor tyrosine kinase orthologous to human ABL1 (OMIM:189980, mutated in chronic myeloid leukemia) and ABL2 (OMIM:164690); ABL-1 inhibits germline apoptosis induced by radiation or by natural aging, but it has no effect on apoptosis induced by starvation or by chemical mutagens (ethylnitrosourea, ethylmethanesulfonate, cisplatin, etoposide), or on constitutive ('physiological') germline apoptosis; at the same time, ABL-1 is required for germline apoptosis induced by oxidative, osmotic or heat-shock stress, and is also required for pathogenesis by Shigella flexneri infecting the intestine; ABL-1-inhibited apoptosis is confined to a single gonad arm undergoing radiation, having no nonautonomous effect on the unirradiated arm; abl-1 is expressed in the germline, in most or all cells of early embryos, and in postembryonic pharynx, tail ganglia and ventral nerve cord; abl-1(ok171) mutants are hypersensitive to germline apoptosis and resistant to S. flexneri infection; both abl-1(ok171) phenotypes are phenocopied by c-ABL inhibitors such as STI-571 (Gleevec); ABL-1-inhibited apoptosis requires active CED-3 and EGL-1, inactive CED-9, and active AKT-1, CEP-1, CLK-1, HUS-1, and MRT-2; abl-1(ok171) has no effect on somatic apoptosis, and abl-1(ok171) mutants are generally normal; abl-1 transcripts are enriched in cultured unc-4::GFP neurons.
abl-1 encodes, by alternative splicing, three isoforms of a Src homology (SH) 2 and 3 domain-containing non-receptor tyrosine kinase orthologous to human ABL1 (OMIM:189980, mutated in chronic myeloid leukemia) and ABL2 (OMIM:164690); ABL-1 inhibits germline apoptosis induced by radiation or by natural aging, but it has no effect on apoptosis induced by starvation or by chemical mutagens (ethylnitrosourea, ethylmethanesulfonate, cisplatin, etoposide), or on constitutive ('physiological') germline apoptosis; at the same time, ABL-1 is required for germline apoptosis induced by oxidative, osmotic or heat-shock stress, and is also required for pathogenesis by Shigella flexneri infecting the intestine; ABL-1-inhibited apoptosis is confined to a single gonad arm undergoing radiation, having no nonautonomous effect on the unirradiated arm; abl-1 is expressed in the germline, in most or all cells of early embryos, and in postembryonic pharynx, tail ganglia and ventral nerve cord; abl-1(ok171) mutants are hypersensitive to germline apoptosis and resistant to S. flexneri infection; both abl-1(ok171) phenotypes are phenocopied by c-ABL inhibitors such as STI-571 (Gleevec); ABL-1-inhibited apoptosis requires active CED-3 and EGL-1, inactive CED-9, and active AKT-1, CEP-1, CLK-1, HUS-1, and MRT-2; abl-1(ok171) has no effect on somatic apoptosis, and abl-1(ok171) mutants are generally normal; abl-1 transcripts are enriched in cultured unc-4::GFP neurons.
abt-1 encodes a predicted ATP-binding cassette (ABC) transporter that is a member of the ABCA subfamily of transport proteins; ABT-1 is predicted to function as a transmembrane protein that couples energy to transport of various molecules across membranes, but as loss of abt-1 activity via RNAi results in no obvious defects, the precise role of abt-1 in C. elegans development and/or behavior is not yet known.
abt-2 encodes a predicted ATP-binding cassette (ABC) transporter that is a member of the ABCA subfamily of transport proteins; ABT-2 is predicted to function as a transmembrane protein that couples energy to transport of various molecules across membranes, but as loss of abt-2 activity via RNAi results in no obvious defects, the precise role of abt-2 in C. elegans development and/or behavior is not yet known.
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