Tag | Content |
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EKPD ID | EKS-MUM-00185 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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AGC/PKA | 484.1 | 2.2E-145 | 44 | 298 | 255 |
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Status | Reviewed |
Ensembl Protein | ENSMUSP00000005606 |
UniProt Accession | P05132; Q9JID0; |
Protein Name | cAMP-dependent protein kinase catalytic subunit alpha |
Protein Synonyms/Alias | PKA C-alpha; |
Gene Name | Prkaca |
Gene Synonyms/Alias | Prkaca; Pkaca; |
Ensembl Information | |
Organism | Mus musculus |
Functional Description | Phosphorylates a large number of substrates in thecytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, TRPC1 and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B- alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha- difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). TRPC1 activation by phosphorylation promotes Ca(2+) influx, essential for the increase in permeability induced by thrombin in confluent endothelial monolayers. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Regulates negatively tight junction (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. Prevents meiosis redumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). |
Protein Length | 351 |
Protein Sequence (FASTA) | MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL GTGSFGRVML 60 | VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV 120 | MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY 180 | IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF 240 | ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 300 | TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F 351 |
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Nucleotide Sequence (FASTA) | ATGGGCAACG CCGCCGCCGC CAAGAAGGGC AGCGAGCAGG AGAGCGTGAA AGAGTTCCTA 60 | GCCAAAGCCA AGGAAGATTT CCTGAAAAAA TGGGAGACCC CTTCTCAGAA TACAGCCCAG 120 | TTGGATCAGT TTGATAGAAT CAAGACCCTT GGCACCGGCT CCTTTGGGCG AGTGATGCTG 180 | GTGAAGCACA AGGAGAGTGG GAACCACTAC GCCATGAAGA TCTTAGACAA GCAGAAGGTG 240 | GTGAAGCTAA AGCAGATCGA GCACACTCTG AATGAGAAGC GCATCCTGCA GGCCGTCAAC 300 | TTCCCGTTCC TGGTCAAACT TGAATTCTCC TTCAAGGACA ACTCAAACCT GTACATGGTC 360 | ATGGAGTATG TAGCTGGTGG CGAGATGTTC TCCCACCTAC GGCGGATTGG AAGGTTCAGC 420 | GAGCCCCATG CCCGTTTCTA CGCGGCGCAG ATCGTCCTGA CCTTTGAGTA TCTGCACTCC 480 | CTGGACCTCA TCTACCGGGA CCTGAAGCCC GAGAATCTTC TCATCGACCA GCAGGGCTAT 540 | ATTCAGGTGA CAGACTTCGG TTTTGCCAAG CGTGTGAAAG GCCGTACTTG GACCTTGTGT 600 | GGGACCCCTG AGTACTTGGC CCCCGAGATT ATCCTGAGCA AAGGCTACAA CAAGGCTGTG 660 | GACTGGTGGG CTCTCGGAGT CCTCATCTAC GAGATGGCTG CTGGTTACCC ACCCTTCTTC 720 | GCTGACCAGC CTATCCAGAT CTATGAGAAA ATCGTCTCTG GGAAGGTGCG GTTCCCATCC 780 | CACTTCAGCT CTGACTTGAA GGACCTGCTG CGGAACCTTC TGCAGGTGGA TCTCACCAAG 840 | CGCTTTGGGA ACCTCAAGAA CGGGGTCAAT GACATCAAGA ACCACAAGTG GTTTGCCACG 900 | ACTGACTGGA TTGCCATCTA TCAGAGAAAG GTGGAAGCTC CCTTCATACC AAAGTTTAAA 960 | GGCCCTGGGG ACACGAGTAA CTTTGACGAC TATGAGGAGG AAGAGATCCG GGTCTCCATC 1020 | AATGAGAAGT GTGGCAAGGA GTTTACTGAG TTTTAG 1056 |
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Domain Profile | S: 1 ferlktlGtGsfGrvelvrekeskkyyalkvlskekvvklkqvehvknekrvlkavefpf 60 | f+r+ktlGtGsfGrv+lv++kes+++ya+k+l+k+kvvklkq+eh+ nekr+l+av+fpf | Q: 44 FDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPF 103 | 789********************************************************* |
| S: 61 lvkllasfkdesnlylvleyveGGelfsylrkvrrfsekaarfyaaeivlaleylhsldl 120 | lvkl++sfkd+snly+v+eyv+GGe+fs+lr+++rfse++arfyaa+ivl++eylhsldl | Q: 104 LVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDL 163 | ************************************************************ |
| S: 121 iyrdlkpenllldkeGyikvtdfGfakkvkdrtwtlcGtpeylapeiiqskgynkavdww 180 | iyrdlkpenll+d++Gyi+vtdfGfak+vk+rtwtlcGtpeylapeii skgynkavdww | Q: 164 IYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWW 223 | ************************************************************ |
| S: 181 alGvliyellaGyppffddqpikiyekivsgklkfpsklssdlkdllkkllqvdltkrlg 240 | alGvliye++aGyppff+dqpi+iyekivsgk++fps++ssdlkdll++llqvdltkr+g | Q: 224 ALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG 283 | ************************************************************ |
| S: 241 nlkngvedikehkwf 255 | nlkngv+dik+hkwf | Q: 284 NLKNGVNDIKNHKWF 298 | **************9 |
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Domain Sequence (FASTA) | FDRIKTLGTG SFGRVMLVKH KESGNHYAMK ILDKQKVVKL KQIEHTLNEK RILQAVNFPF 60 | LVKLEFSFKD NSNLYMVMEY VAGGEMFSHL RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL 120 | IYRDLKPENL LIDQQGYIQV TDFGFAKRVK GRTWTLCGTP EYLAPEIILS KGYNKAVDWW 180 | ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG 240 | NLKNGVNDIK NHKWF 255 |
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Keyword | 3D-structure; Alternative splicing; ATP-binding; cAMP; Cell membrane; Complete proteome; Cytoplasm; Kinase; Lipoprotein; Membrane; Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |