| IED ID | IndEnz0002018779 |
| Enzyme Type ID | protease018779 |
| Protein Name |
Amyloid beta precursor like protein 2 APPH Amyloid beta A4 precursor-like protein 2 Amyloid protein homolog Amyloid-like protein 2 APLP-2 CDEI box-binding protein CDEBP Sperm membrane protein YWK-II |
| Gene Name | APLP2 APPL2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAATGTAAAAATGRLLLLLLVGLTAPALALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCFETKEEVLQYCQEMYPELQITNVMEANQRVSIDNWCRRDKKQCKSRFVTPFKCLVGEFVSDVLLVPEKCQFFHKERMEVCENHQHWHTVVKEACLTQGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKIIGSVSKEEEEEDEEEEEEEDEEEDYDVYKSEFPTEADLEDFTEAAVDEDDEDEEEGEEVVEDRDYYYDTFKGDDYNEENPTEPGSDGTMSDKEITHDVKAVCSQEAMTGPCRAVMPRWYFDLSKGKCVRFIYGGCGGNRNNFESEDYCMAVCKAMIPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKAERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRMALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTASISETPVDVRVSSEESEEIPPFHPFHPFPALPENEDTQPELYHPMKKGSGVGEQDGGLIGAEEKVINSKNKVDENMVIDETLDVKEMIFNAERVGGLEEERESVGPLREDFSLSSSALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQMQI |
| Enzyme Length | 763 |
| Uniprot Accession Number | Q06481 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity). {ECO:0000250, ECO:0000269|PubMed:8307156}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (5); Beta strand (3); Chain (1); Compositional bias (3); Disulfide bond (9); Domain (3); Frameshift (1); Helix (10); Metal binding (3); Modified residue (1); Motif (1); Natural variant (1); Region (4); Sequence conflict (4); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Alternative splicing;Cell membrane;Copper;DNA-binding;Disulfide bond;Glycoprotein;Membrane;Metal-binding;Nucleus;Phosphoprotein;Protease inhibitor;Reference proteome;Serine protease inhibitor;Signal;Transmembrane;Transmembrane helix |
| Interact With | P51693; Itself; P05067-4; O75618; P14921; P05412; Q93074; P02649; P05067; Q96GW7; Q13867; Q9BS26; Q06787-7; P06241; P14136; Q14114-3; Q96L34; P17252; P23443; P04271; Q8IUQ4-2; P84022; Q13190; P43405-2; Q13428-5; Q9BX74; Q9BVJ6 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000305}. |
| Modified Residue | MOD_RES 590; /note=Phosphoserine; by FAM20C; /evidence=ECO:0000269|PubMed:26091039 |
| Post Translational Modification | PTM: The BPTI/Kunitz inhibitor domain is O-glycosylated. {ECO:0000269|PubMed:8307156}. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5JBT; 5TPT; |
| Mapped Pubmed ID | 12228233; 12595709; 14597230; 14699153; 14970211; 14970212; 14983046; 15208260; 15231748; 15584916; 16193067; 16279945; 16645641; 17405931; 17452623; 17709753; 18452037; 18641335; 19126676; 19808674; 20195357; 20379614; 20711500; 20732423; 20936779; 20953506; 21178287; 21293490; 21695060; 21826533; 21952790; 21988832; 22641691; 22797723; 23430252; 25683482; 26085104; 26313004; 26496610; 27796194; 27810896; 29663738; 30608876; 30810435; 32716039; 8467233; 9109675; 9461550; |
| Motif | MOTIF 750..755; /note=NPXY motif |
| Gene Encoded By | |
| Mass | 86,956 |
| Kinetics | |
| Metal Binding | METAL 163; /note=Copper; /evidence=ECO:0000255|PROSITE-ProRule:PRU01217; METAL 167; /note=Copper; /evidence=ECO:0000255|PROSITE-ProRule:PRU01217; METAL 184; /note=Copper; /evidence=ECO:0000255|PROSITE-ProRule:PRU01217 |
| Rhea ID | |
| Cross Reference Brenda |