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Literature summary extracted from

  • Mukai, H.
    The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC (2003), J. Biochem., 133, 17-27.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Drosophila melanogaster
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Homo sapiens
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Xenopus laevis
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Caenorhabditis elegans
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminal C2-domain Asteroidea
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Mus musculus
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Rattus norvegicus
2.7.11.1 arachidonic acid activates in vitro, binds at the autoinhibitory site at the C-terminus Bos taurus
2.7.11.1 cardiolipin activates isozyme PKNalpha Homo sapiens
2.7.11.1 cardiolipin activates isozyme PKNalpha Rattus norvegicus
2.7.11.1 linoleic acid
-
 Homo sapiens
2.7.11.1 lysophosphatidic acid activates isozyme PKNalpha Mus musculus
2.7.11.1 lysophosphatidic acid activates isozyme PKNalpha Homo sapiens
2.7.11.1 lysophosphatidic acid activates isozyme PKNalpha Rattus norvegicus
2.7.11.1 lysophosphatidylinositol activates isozyme PKNalpha Homo sapiens
2.7.11.1 lysophosphatidylinositol activates isozyme PKNalpha Rattus norvegicus
2.7.11.1 additional information no activation by calcium/phosphatidylserine/diolein, phosphorylation of PKN is required for full activation Homo sapiens
2.7.11.1 additional information no activation by calcium/phosphatidylserine/diolein, phosphorylation of PKN is required for full activation Rattus norvegicus
2.7.11.1 additional information phosphorylation of PKN is required for full activation Drosophila melanogaster
2.7.11.1 additional information phosphorylation of PKN is required for full activation Mus musculus
2.7.11.1 additional information phosphorylation of PKN is required for full activation Bos taurus
2.7.11.1 additional information phosphorylation of PKN is required for full activation Xenopus laevis
2.7.11.1 additional information phosphorylation of PKN is required for full activation Caenorhabditis elegans
2.7.11.1 additional information phosphorylation of PKN is required for full activation Asteroidea
2.7.11.1 phosphatidylinositol 3,4,5-trisphosphate activates isozyme PKNalpha Homo sapiens
2.7.11.1 phosphatidylinositol 3,4,5-trisphosphate activates isozyme PKNalpha Rattus norvegicus
2.7.11.1 phosphatidylinositol 4,5-bisphosphate activates isozyme PKNalpha Homo sapiens
2.7.11.1 phosphatidylinositol 4,5-bisphosphate activates isozyme PKNalpha Rattus norvegicus
2.7.11.1 Rac1 GTPase, binds and activates PKN Drosophila melanogaster
2.7.11.1 Rac2 GTPase, binds and activates PKN Drosophila melanogaster
2.7.11.1 Rho small GTPase, binds and activates PKN Caenorhabditis elegans
2.7.11.1 Rho small GTPase, binds and activates PKN Asteroidea
2.7.11.1 Rho1 small GTPase, binds GTP-dependently and activates PKN Drosophila melanogaster
2.7.11.1 RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Mus musculus
2.7.11.1 RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Homo sapiens
2.7.11.1 RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Rattus norvegicus
2.7.11.1 RhoA small GTPase, binds to the ACC domain and activates isozymes PKNalpha and PRK2/PKNgamma/PAK-2 Bos taurus
2.7.11.1 RhoA small GTPase, binds to the ACC domain of PKNalpha forming a catalytic active site Drosophila melanogaster
2.7.11.1 small GTPase Rho small GTPase, binds and activates PKN Xenopus laevis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.1 DNA sequence determination of isozyme PKNbeta Homo sapiens
2.7.11.1 gene mapping, DNA sequence determination and analysis of multiple isozymes Rattus norvegicus
2.7.11.1 PKNalpha gene mapps to 19p12-p13.1 of chromosome 8 situated at the prostanoid receptor gene locus Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Asteroidea
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Bos taurus
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Caenorhabditis elegans
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Drosophila melanogaster
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Homo sapiens
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Mus musculus
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Rattus norvegicus
2.7.11.1 additional information PKN possesses an autoinhibitory site at the C-terminal C2 domain, which also binds activating arachidonic acid Xenopus laevis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.11.1 cytosol
-
 Rattus norvegicus 5829
-
2.7.11.1 cytosol
-
 Asteroidea 5829
-
2.7.11.1 cytosol juxtanuclear, isozyme PKNalpha, no isozyme PKNbeta Homo sapiens 5829
-
2.7.11.1 endoplasmic reticulum isozyme PKNalpha Homo sapiens 5783
-
2.7.11.1 endosome isozyme PKNalpha Homo sapiens 5768
-
2.7.11.1 membrane
-
 Bos taurus 16020
-
2.7.11.1 membrane isozyme PKNalpha Homo sapiens 16020
-
2.7.11.1 membrane postnuclear fraction Rattus norvegicus 16020
-
2.7.11.1 additional information PKNalpha translocates from the cytosol to the nucleus in response to various stresses, PRK2/PKNgamma/PAK-2 translocates from the cytosol to germinal vesicles during meiotic maturation in oocytes Asteroidea
-
-
2.7.11.1 nucleus
-
 Asteroidea 5634
-
2.7.11.1 nucleus isozyme PKNbeta Homo sapiens 5634
-
2.7.11.1 perinuclear space isozyme PKNbeta Homo sapiens
-
-
2.7.11.1 vesicle isozyme PKNalpha Homo sapiens 31982
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.1 additional information Drosophila melanogaster regulation mechanism and biological function of PKN ?
-
 ?
2.7.11.1 additional information Bos taurus regulation mechanism and biological function of PKN ?
-
 ?
2.7.11.1 additional information Caenorhabditis elegans regulation mechanism and biological function of PKN ?
-
 ?
2.7.11.1 additional information Asteroidea regulation mechanism and biological function of PKN ?
-
 ?
2.7.11.1 additional information Mus musculus regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, isozyme PKNalpha is involved in glucose transport in 3T3/L1 cells ?
-
 ?
2.7.11.1 additional information Homo sapiens regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, PKNalpha is involved in vesicle transport in the endoplasmic reticulum, PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction, PKN interacts with papillomaviral oncoproteins being involved in tumorigenesis, overview ?
-
 ?
2.7.11.1 additional information Rattus norvegicus regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization, overview ?
-
 ?
2.7.11.1 additional information Xenopus laevis regulation mechanism and biological function of PKN, the enzyme is involved in cell cycle control ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Asteroidea
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Bos taurus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Caenorhabditis elegans
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Drosophila melanogaster
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Homo sapiens
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Mus musculus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Rattus norvegicus
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-
2.7.11.1 Xenopus laevis
-
 at least 3 different isozymes PKNalpha/PKN-1/PAK-1, PKNbeta, and PRK2/PKNgamma/PAK-2
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.1 phosphoprotein e.g. phosphorylation of isozyme PRK2/PKNgamma/PAK-2 at Ser473 and Thr308, phosphorylation is required for full activation Homo sapiens
2.7.11.1 phosphoprotein phosphorylation is required for full activation Drosophila melanogaster
2.7.11.1 phosphoprotein phosphorylation is required for full activation Mus musculus
2.7.11.1 phosphoprotein phosphorylation is required for full activation Rattus norvegicus
2.7.11.1 phosphoprotein phosphorylation is required for full activation Bos taurus
2.7.11.1 phosphoprotein phosphorylation is required for full activation Xenopus laevis
2.7.11.1 phosphoprotein phosphorylation is required for full activation Caenorhabditis elegans
2.7.11.1 phosphoprotein phosphorylation is required for full activation Asteroidea
2.7.11.1 proteolytic modification PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.1 isozyme PKNalpha from brain membrane Bos taurus
2.7.11.1 PKN from testis to homogeneity by immuno affinity Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Drosophila melanogaster
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Mus musculus
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Homo sapiens
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Rattus norvegicus
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Bos taurus
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Xenopus laevis
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Caenorhabditis elegans
a
2.7.11.1 ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate catalytic mechanism and regulation of PKN Asteroidea
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.1 3T3-L1 cell isozyme PKNalpha Mus musculus
-
2.7.11.1 A2780-DX3 cell lymphoid cell line, specific expression of isozyme PRK2/PKNgamma/PAK-2 Homo sapiens
-
2.7.11.1 brain isozyme PKNalpha Homo sapiens
-
2.7.11.1 brain isozyme PKNalpha Rattus norvegicus
-
2.7.11.1 brain isozyme PKNalpha Bos taurus
-
2.7.11.1 embryo
-
 Xenopus laevis
-
2.7.11.1 epithelium
-
 Homo sapiens
-
2.7.11.1 fibroblast IR fibroblasts Rattus norvegicus
-
2.7.11.1 HeLa cell isozymes PRK2/PKNgamma/PAK-2, and PKNbeta Homo sapiens
-
2.7.11.1 hippocampus
-
 Homo sapiens
-
2.7.11.1 JURKAT cell isozyme PRK2/PKNgamma/PAK-2 Homo sapiens
-
2.7.11.1 K-562 cell chromic myelogenous leukemia cell line, isozyme PKNbeta Homo sapiens
-
2.7.11.1 keratinocyte
-
 Homo sapiens
-
2.7.11.1 keratinocyte isozyme PRK2/PKNgamma/PAK-2 Mus musculus
-
2.7.11.1 liver isozyme PRK2/PKNgamma/PAK-2 Rattus norvegicus
-
2.7.11.1 additional information isozymes show different tissue distribution Drosophila melanogaster
-
2.7.11.1 additional information isozymes show different tissue distribution Mus musculus
-
2.7.11.1 additional information isozymes show different tissue distribution Bos taurus
-
2.7.11.1 additional information isozymes show different tissue distribution Xenopus laevis
-
2.7.11.1 additional information isozymes show different tissue distribution Caenorhabditis elegans
-
2.7.11.1 additional information isozymes show different tissue distribution Asteroidea
-
2.7.11.1 additional information ubiquitous expression of isozyme PKNalpha, isozymes show different tissue distribution Rattus norvegicus
-
2.7.11.1 additional information ubiquitous expression of isozyme PKNalpha, isozymes show different tissue distribution, PKNbeta is mainly expressed in cancer cells in adults Homo sapiens
-
2.7.11.1 neuron isozyme PKNalpha Homo sapiens
-
2.7.11.1 NIH-3T3 cell isozyme PKNalpha Mus musculus
-
2.7.11.1 oocyte isozyme PRK2/PKNgamma/PAK-2 Asteroidea
-
2.7.11.1 spleen
-
 Homo sapiens
-
2.7.11.1 spleen
-
 Rattus norvegicus
-
2.7.11.1 SW-480 cell colorectal adenocarcinoma cell line, isozyme PKNbeta Homo sapiens
-
2.7.11.1 testis
-
 Homo sapiens
-
2.7.11.1 testis
-
 Rattus norvegicus
-
2.7.11.1 thymus
-
 Homo sapiens
-
2.7.11.1 thymus
-
 Rattus norvegicus
-
2.7.11.1 U-937 cell isozyme PKNalpha Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + MARCKS protein isozyme PKNalpha Homo sapiens ADP + MARCKS phosphoprotein
-
 ?
2.7.11.1 ATP + MB protein
-
 Homo sapiens ADP + MB phosphoprotein
-
 ?
2.7.11.1 ATP + protein kinase C isozyme PKNalpha Homo sapiens ADP + phosphorylated protein kinase C
-
 ?
2.7.11.1 ATP + vimentin isozyme PKNalpha Homo sapiens ADP + phosphorylated vimentin
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN Drosophila melanogaster ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN Bos taurus ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN Caenorhabditis elegans ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN Asteroidea ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, isozyme PKNalpha is involved in glucose transport in 3T3/L1 cells Mus musculus ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization and cell adhesion, overview, PKNalpha is involved in vesicle transport in the endoplasmic reticulum, PKNalpha is cleaved by caspase-3 or related proteases in apoptotic Jurkat and U-937 cells contributing to signal transduction, PKN interacts with papillomaviral oncoproteins being involved in tumorigenesis, overview Homo sapiens ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN, PKNalpha is involved in insulin-induced actin cytoskeleton reorganization, overview Rattus norvegicus ?
-
 ?
2.7.11.1 additional information regulation mechanism and biological function of PKN, the enzyme is involved in cell cycle control Xenopus laevis ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Xenopus laevis ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Caenorhabditis elegans ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain Asteroidea ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Mus musculus ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Homo sapiens ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Rattus norvegicus ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site Bos taurus ?
-
 ?
2.7.11.1 additional information enzyme performs autophosphorylation, PKN binds several associated proteins via its ACC domain, i.e. RhoA, a small GTPase, which binds to the ACC domain of PKNalpha forming a catalytic active site, isozyme PRK2/PKNgamma/PAK-2 binds to the large non-transmembrane protein Tyr phosphatase PTP-BL involved in the modulation of cytoskeleton, mediated by PSD-95 Drosophila melanogaster ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Drosophila melanogaster
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Mus musculus
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Homo sapiens
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Rattus norvegicus
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Bos taurus
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Xenopus laevis
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Caenorhabditis elegans
2.7.11.1 More isozyme structure analysis, PKN kinase contains a catalytic domain homologous to that of protein kinase C, as well as a unique regulatory region containing antiparallel coiled-coil domain, the ACC domain, and an autoinhibitory C2 domain binding activators Asteroidea

Synonyms

EC Number Synonyms Comment Organism
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Drosophila melanogaster
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Mus musculus
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Homo sapiens
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Rattus norvegicus
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Bos taurus
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Xenopus laevis
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Caenorhabditis elegans
2.7.11.1 More PKN belongs to the AGC subfamily of protein kinases Asteroidea
2.7.11.1 PKN
-
 Drosophila melanogaster
2.7.11.1 PKN
-
 Mus musculus
2.7.11.1 PKN
-
 Homo sapiens
2.7.11.1 PKN
-
 Rattus norvegicus
2.7.11.1 PKN
-
 Bos taurus
2.7.11.1 PKN
-
 Xenopus laevis
2.7.11.1 PKN
-
 Caenorhabditis elegans
2.7.11.1 PKN
-
 Asteroidea

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.1 ATP
-
 Drosophila melanogaster
2.7.11.1 ATP
-
 Mus musculus
2.7.11.1 ATP
-
 Homo sapiens
2.7.11.1 ATP
-
 Rattus norvegicus
2.7.11.1 ATP
-
 Bos taurus
2.7.11.1 ATP
-
 Xenopus laevis
2.7.11.1 ATP
-
 Caenorhabditis elegans
2.7.11.1 ATP
-
 Asteroidea