IED ID | IndEnz0016000116 |
Enzyme Type ID | tyrosinase000116 |
Protein Name |
Cadherin-3 Placental cadherin P-cadherin |
Gene Name | CDH3 CDHP |
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 | MGLPRGPLASLLLLQVCWLQCAASEPCRAVFREAEVTLEAGGAEQEPGQALGKVFMGCPGQEPALFSTDNDDFTVRNGETVQERRSLKERNPLKIFPSKRILRRHKRDWVVAPISVPENGKGPFPQRLNQLKSNKDRDTKIFYSITGPGADSPPEGVFAVEKETGWLLLNKPLDREEIAKYELFGHAVSENGASVEDPMNISIIVTDQNDHKPKFTQDTFRGSVLEGVLPGTSVMQVTATDEDDAIYTYNGVVAYSIHSQEPKDPHDLMFTIHRSTGTISVISSGLDREKVPEYTLTIQATDMDGDGSTTTAVAVVEILDANDNAPMFDPQKYEAHVPENAVGHEVQRLTVTDLDAPNSPAWRATYLIMGGDDGDHFTITTHPESNQGILTTRKGLDFEAKNQHTLYVEVTNEAPFVLKLPTSTATIVVHVEDVNEAPVFVPPSKVVEVQEGIPTGEPVCVYTAEDPDKENQKISYRILRDPAGWLAMDPDSGQVTAVGTLDREDEQFVRNNIYEVMVLAMDNGSPPTTGTGTLLLTLIDVNDHGPVPEPRQITICNQSPVRQVLNITDKDLSPHTSPFQAQLTDDSDIYWTAEVNEEGDTVVLSLKKFLKQDTYDVHLSLSDHGNKEQLTVIRATVCDCHGHVETCPGPWKGGFILPVLGAVLALLFLLLVLLLLVRKKRKIKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPEVVLRNDVAPTIIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEWGSRFKKLADMYGGGEDD |
Enzyme Length | 829 |
Uniprot Accession Number | P22223 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (20); Chain (1); Domain (5); Glycosylation (2); Helix (2); Natural variant (5); Propeptide (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (5) |
Keywords | 3D-structure;Alternative splicing;Calcium;Cell adhesion;Cell membrane;Cleavage on pair of basic residues;Disease variant;Ectodermal dysplasia;Glycoprotein;Hypotrichosis;Membrane;Metal-binding;Reference proteome;Repeat;Sensory transduction;Signal;Transmembrane;Transmembrane helix;Vision |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (18) |
Cross Reference PDB | 4OY9; 4ZML; 4ZMN; 4ZMO; 4ZMP; 4ZMQ; 4ZMT; 4ZMV; 4ZMW; 4ZMX; 4ZMY; 4ZMZ; 5JYL; 5JYM; 6ZTB; 6ZTR; 7CME; 7CMF; |
Mapped Pubmed ID | 11891861; 12021924; 12112590; 12800191; 12919105; 15375751; 15817166; 15967043; 16115928; 17342797; 18074863; 18199584; 18230143; 18329483; 18330089; 18637117; 18637128; 18811693; 18829530; 18927288; 19043399; 19076794; 19528483; 19846933; 19882246; 19901964; 19915572; 20118984; 20140736; 20203473; 20204300; 20338046; 20385540; 20473917; 20621328; 20668551; 20711500; 20844743; 20852590; 20860798; 21317933; 21376238; 21703417; 21781454; 22209340; 22348569; 22389315; 22531681; 22696062; 23180380; 23334344; 23398382; 23405208; 23682078; 23740836; 24139214; 24189400; 24559158; 24636838; 25023983; 25269858; 25322858; 25337260; 25849494; 26285159; 26299056; 26771841; 26885695; 27223886; 27386845; 27399126; 27456782; 27545624; 28045038; 28084338; 28295003; 29338041; 29438669; 29571991; 30006753; 30710256; 31560841; 31621118; 31696509; 31927556; 32156745; 32341236; 32572153; 32816889; 32920119; 32988879; 33413178; 33517284; 33879555; 34216280; 7806582; 9219219; |
Motif | |
Gene Encoded By | |
Mass | 91,418 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |