AKT1

Potassium channel AKT1

935 amino acids

Highly selective inward-rectifying potassium channel that mediates potassium uptake by plant roots.

Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily.

104.465 kDa

MARWGAARMAACGPWGRNRRVGAGDAFEASEVRRDGRSRMMPACGPWGAGHGGGDPALERELSRDGSHYSISSAILPSLGARSNRRIKLRRFIISPYDRRYRIWETFLIVLVVYSAWVSPFEFGFIPKPTGALATADNVVNAFFAVDIILTFFVAYLDKMSYMLEDDPKKIAWRYSTTWLVLDVASTIPSEFARRILPSKLRSYGFFNMLRLWRLRRVSSLFSRLEKDRHFNYFWVRCAKLICVTLFAVHCAACFYYLLADRYPVPTSTWIGNYMADFHERSLWIRYVTSVYWSITTLTTVGYGDLHAENTREMIFNIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNYRDTIQAATSFGVRNQLPPRLQDQMISHISLKYRTDSEGLQQQEILDSLPKAIKSSISQYLFFHLVQNVYLFQGVSNDLIFQLVSEMKAEYFPPREDVILQNEAPTDFYILVSGSVELVEQQNGADQVIQVATSGEVVGEIGVLCYRPQLFTVRTRSLCQLLRLNRTAFLSIVQSNVGDGTIIMNNLIQFLKEQKENSVMAGVVKEIESMLARGNLDLPITLCFAVTRGDDFLLHQLLKRGMDPNESDNDGHTALHIAASKGNEQCVRLLLEYGADPNARDSEGKVPLWEALCEKHAAVVQLLVEGGADLSSGDTGLYACIAVEESDTELLNDIIHYGGDVNRARRDGTTALHRAVCDGNVQMAELLLEHGADIDKQDGNGWTPRALAEQQGHDDIQLLFRSRKAATASGHHHVPSSTTTRVAPAAAAASLIGRFNSEPMMKNMIHEDADLPSRVLPEKLRRKRVTFQNSLFGVISSSQAQRETDHPLSRGGLAATGSPNPSSGSRNAVIRVTISCPEKGNTAGKLVLLPQTLDMLLELGAKKFDFAPTKVLTVEGAEVDEVELIRDGDHLVLVSDEWDAEKMKGKS

AKT1

Potassium channel AKT1

935 amino acids

Highly selective inward-rectifying potassium channel that mediates potassium uptake by plant roots. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May be a major salt-sensitive potassium channel in roots.

Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily.

104.464 kDa

MARWGAARMAACGPWGRNRRVGAGDAFEASEVRRDGRSRMMPACGPWGAGHGGGDPALERELSRDGSHYSISSAILPSLGARSNRRIKLRRFIISPYDRRYRIWETFLIVLVVYSAWVSPFEFGFIPKPTGALATADNVVNAFFAVDIILTFFVAYLDKMSYMLEDDPKKIAWRYSTTWLVLDVASTIPSEFARRILPSKLRSYGFFNMLRLWRLRRVSSLFSRLEKDRHFNYFWVRCAKLICVTLFAVHCAACFYYLLADRYPVPTSTWIGNYMADFHERSLWIRYVTSVYWSITTLTTVGYGDLHAENTREMIFNIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNYRDTIQAATSFGVRNQLPPRLQDQMISHISLKYRTDSEGLQQQEILDSLPKAIKSSISQYLFFHLVQNVYLFQGVSNDLIFQLVSEMKAEYFPPREDVILQNEAPTDFYILVSGSVELVEQQNGADQVIQVATSGEVVGEIGVLCYRPQLFTVRTRSLCQLLRLNRTAFLSIVQSNVGDGTIIMNNLIQFLKEQKENSVMAGVVKEIESMLARGNLDLPITLCFAVTRGDDFLLHQLLKRGMDPNESDNDGHTALHIAASKGNEQCVRLLLEYGADPNARDSEGKVPLWEALCEKHAAVVQLLVEGGADLSSGDTGLYACIAVEESDTELLNDIIHYGGDVNRARRDGTTALHRAVCDGNVQMAELLLEHGADIDKQDGNGWTPRALAEQQGHDDIQLLFRSRKAATASGHHHVPSSTTTRVAPAAAAASLIGRFNSEPMMKNMIHEDADLPSRVLPEKLRRKRVTFQNSLFGVISSSQAQRETDHPLSRGGLAATGSPNPSSGSRNAVIRVTISCPEKGNTAGKLVLLPQTLDMLLELGAKKFDFAPTKVLTVEGAEVDEVELIRDGDHLVLVSNEWDAEKMKGKS

AKT1

Potassium channel AKT1

857 amino acids

Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins (PubMed:12678562, PubMed:16814720, PubMed:16895985, PubMed:17898163, PubMed:9572739). Is essential with POT5/HAK5 for high-affinity potassium uptake in roots during seedling establishment and postgermination growth under low potassium conditions (PubMed:20413648).

Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily.

96.99 kDa

MRGGALLCGQVQDEIEQLSRESSHFSLSTGILPSLGARSNRRVKLRRFVVSPYDHKYRIWEAFLVVLVVYTAWVSPFEFGFLRKPRPPLSITDNIVNAFFAIDIIMTFFVGYLDKSTYLIVDDRKQIAFKYLRSWFLLDLVSTIPSEAAMRISSQSYGLFNMLRLWRLRRVGALFARLEKDRNFNYFWVRCAKLVCVTLFAVHCAACFYYLIAARNSNPAKTWIGANVANFLEESLWMRYVTSMYWSITTLTTVGYGDLHPVNTKEMIFDIFYMLFNLGLTAYLIGNMTNLVVHGTSRTRNFRDTIQAASNFAHRNHLPPRLQDQMLAHLCLKYRTDSEGLQQQETLDALPKAIRSSISHFLFYSLMDKVYLFRGVSNDLLFQLVSEMKAEYFPPKEDVILQNEAPTDFYILVNGTADLVDVDTGTESIVREVKAGDIIGEIGVLCYRPQLFTVRTKRLCQLLRMNRTTFLNIIQANVGDGTIIMNNLLQHLKEMNDPVMTNVLLEIENMLARGKMDLPLNLCFAAIREDDLLLHQLLKRGLDPNESDNNGRTPLHIAASKGTLNCVLLLLEYHADPNCRDAEGSVPLWEAMVEGHEKVVKVLLEHGSTIDAGDVGHFACTAAEQGNLKLLKEIVLHGGDVTRPRATGTSALHTAVCEENIEMVKYLLEQGADVNKQDMHGWTPRDLAEQQGHEDIKALFREKLHERRVHIETSSSVPILKTGIRFLGRFTSEPNIRPASREVSFRIRETRARRKTNNFDNSLFGILANQSVPKNGLATVDEGRTGNPVRVTISCAEKDDIAGKLVLLPGSFKELLELGSNKFGIVATKVMNKDNNAEIDDVDVIRDGDHLIFATDS

Akt1

RAC serine/threonine-protein kinase

611 amino acids

Serine/threonine kinase involved in various developmental processes (PubMed:9601646, PubMed:10587646, PubMed:10962553, PubMed:11740943, PubMed:12172554, PubMed:11872800, PubMed:14525946, PubMed:12893776, PubMed:15466161, PubMed:15712201). During early embryogenesis, acts as a survival protein (PubMed:9601646, PubMed:10962553). During mid-embryogenesis, phosphorylates and activates trh, a transcription factor required for tracheal cell fate determination (PubMed:11740943). Also regulates tracheal cell migration (PubMed:11740943, PubMed:14525946). Later in development, acts downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and antagonizing FOXO transcription factor (PubMed:10587646, PubMed:10962553, PubMed:11752451, PubMed:12893776, PubMed:25329475, PubMed:29025897, PubMed:24603715). Controls follicle cell size during oogenesis (PubMed:15712201). May also stimulate cell growth by phosphorylating Gig/Tsc2 and inactivating the Tsc complex (PubMed:12172554, PubMed:15466161). Dephosphorylation of 'Ser-586' by Phlpp triggers apoptosis and suppression of tumor growth (PubMed:10962553).

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

68.485 kDa

MNYLPFVLQRRSTVVASAPAPGSASRIPESPTTTGSNIINIIYSQSTHPNSSPTSGSAEKFSWQQSWPSRTSAAPTHDSGTMSINTTFDLSSPSVTSGHALTEQTQVVKEGWLMKRGEHIKNWRQRYFVLHSDGRLMGYRSKPADSASTPSDFLLNNFTVRGCQIMTVDRPKPFTFIIRGLQWTTVIERTFAVESELERQQWTEAIRNVSSRLIDVGEVAMTPSEQTDMTDVDMATIAEDELSEQFSVQGTTCNSSGVKKVTLENFEFLKVLGKGTFGKVILCREKATAKLYAIKILKKEVIIQKDEVAHTLTESRVLKSTNHPFLISLKYSFQTNDRLCFVMQYVNGGELFWHLSHERIFTEDRTRFYGAEIISALGYLHSQGIIYRDLKLENLLLDKDGHIKVADFGLCKEDITYGRTTKTFCGTPEYLAPEVLDDNDYGQAVDWWGTGVVMYEMICGRLPFYNRDHDVLFTLILVEEVKFPRNITDEAKNLLAGLLAKDPKKRLGGGKDDVKEIQAHPFFASINWTDLVLKKIPPPFKPQVTSDTDTRYFDKEFTGESVELTPPDPTGPLGSIAEEPLFPQFSYQGDMASTLGTSSHISTSTSLASMQ

AKT1

Acyl-CoA ligase AKT1

578 amino acids

Acyl-CoA ligase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype (PubMed:10432635, PubMed:20348386). AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) (PubMed:22846083). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment (PubMed:22846083). The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety (PubMed:10432635, PubMed:10975654, PubMed:22846083). Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes (PubMed:20348386). The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated (PubMed:10432635, PubMed:10975654, PubMed:22846083). The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalyzis of a side reaction of EDA or its precursor (PubMed:24611558).

63.348 kDa

MVFAAPCWVPPLPSDLPDSTTLEEFIFCQVKDSQTRSELDRSILICGTQGKEYTVQESMERTGRLAQGLSAWLDWPQKPSEEDWKVAAIFNINCVEFFSISHAIHRLGGTVSAINASSTADELEAQLRLSNAQAIFTCNTLLKIAMKASQKVGIPLANIFLTDAPGSYRPDDVYPFQEIDNIVRTARSSLPLLQLGRGQGSSTPAYICFSSGTSGAQKPVLLSHQGIIANIVQINTFEKFRQKGPNVSLCILPLAHSYGLVCVAYNALYRGDRLAVLPSSDVEDLLSIVEKLRINTLYLVPTLLSRILSGGKAGGHDLSCVKEVYTGGAPLHPMLGEHILRHHPTWKTKQCYGATEAGTAVSVTSDCDLWPGSVGCLLPGVQAKIIRSDGSETTKHDESGELWVSSPSLAIGYLSNPLATEATFTVDNTGRTWLRTGDEAKICLSPNGNEHLFIVDRIKDIIKVKGFQVAPVELEQLLLSNDFVEEVAITSRQDKRGEERPQAFVVRTHEGLKEPQDAVSESLQALVKARKARYKWLHPHVIFVDSLPKTTSGKIMRRALRNMCPANSEVNGRLSSKI

akt1

RAC-alpha serine/threonine-protein kinase

481 amino acids

AKT1 is one of several closely related serine/threonine-protein kinases known as the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase (By similarity). Required for insulin-stimulated meiotic reinitiation during oocyte maturation.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

56.042 kDa

MNEVAIVKEGWLHKRGEYIKTWRPRYFLLKSDGTFIGYKERPQDVDQLETPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDSPEEREEWIQVIQHVADNLKKQEEEMMEVRSGDSPSDNSGAEEMEVSHSKPKHKVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERIFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLLPEAKSLLSGLLKKDPKQRLGGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDNFEFVDNERRPHFPQFSYSASGNA

AKT1

RAC-alpha serine/threonine-protein kinase

480 amino acids

AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation (By similarity).

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

55.748 kDa

MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDLEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPGENSGAEEMEVSLAKPKHRVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKEVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFASIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMEGVDSERRPHFPQFSYSASATA

AKT1

RAC-alpha serine/threonine-protein kinase

480 amino acids

AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

55.686 kDa

MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA

Akt1

RAC-alpha serine/threonine-protein kinase

480 amino acids

AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

55.707 kDa

MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWATAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA

Akt1

RAC-alpha serine/threonine-protein kinase

480 amino acids

AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation.

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

55.735 kDa

MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVALAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA