Detail Information for IndEnz0002016646
IED ID IndEnz0002016646
Enzyme Type ID protease016646
Protein Name Annexin A2
Annexin-2
Gene Name ANXA2 ANX2
Organism Canis lupus familiaris (Dog) (Canis familiaris)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
Enzyme Length 339
Uniprot Accession Number Q6TEQ7
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. {ECO:0000250|UniProtKB:P07355}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (8); Region (1); Repeat (4)
Keywords Acetylation;Annexin;Basement membrane;Calcium;Calcium/phospholipid-binding;Extracellular matrix;Isopeptide bond;Phosphoprotein;Reference proteome;Repeat;Secreted;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=In the lamina beneath the plasma membrane. {ECO:0000250}.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:P04272; MOD_RES 24; /note=Phosphotyrosine; by SRC; /evidence=ECO:0000250|UniProtKB:P07355; MOD_RES 26; /note=Phosphoserine; by PKC; /evidence=ECO:0000250|UniProtKB:P07355; MOD_RES 49; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P07356; MOD_RES 152; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P07356; MOD_RES 184; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P07355; MOD_RES 199; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P07356; MOD_RES 227; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P07356
Post Translational Modification PTM: ISGylated. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17022977;
Motif
Gene Encoded By
Mass 38,654
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda