Detail Information for IndEnz0002005589
IED ID IndEnz0002005589
Enzyme Type ID protease005589
Protein Name Annexin A2
Annexin II
Annexin-2
Calpactin I heavy chain
Calpactin-1 heavy chain
Chromobindin-8
Lipocortin II
Placental anticoagulant protein IV
PAP-IV
Protein I
p36
Gene Name Anxa2 Anx2
Organism Rattus norvegicus (Rat)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELPSAMKSALSGHLETVMLGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGEFRKLLVALAKGKRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYFIQQDTKGDYQKALLYLCGGDD
Enzyme Length 339
Uniprot Accession Number Q07936
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 Alternative sequence (1); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (8); Region (1); Repeat (4); Sequence conflict (4)
Keywords Acetylation;Alternative splicing;Annexin;Basement membrane;Calcium;Calcium/phospholipid-binding;Direct protein sequencing;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 {ECO:0000269|PubMed:1618851}. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000269|Ref.5; 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 10603972; 11423489; 14499952; 14587099; 14734570; 15248295; 15823548; 16396496; 16518874; 18332131; 19193640; 22206666; 23525114; 24819400; 9022675;
Motif
Gene Encoded By
Mass 38,678
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda