Detail Information for IndEnz0002003697
IED ID IndEnz0002003697
Enzyme Type ID protease003697
Protein Name Aminopeptidase Q
EC 3.4.11.-
Laeverin
Tabulin
Transmembrane Aminopeptidase Q
Gene Name LVRN TAQPEP
Organism Acinonyx jubatus (Cheetah)
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 Feliformia Felidae (cat family) Acinonychinae Acinonyx Acinonyx jubatus (Cheetah)
Enzyme Sequence MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCTAATARLLLHSLFLDCESAEVRGPLSSGPRDGAVGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTITTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSTAEQDDLWRHFQMVVDDQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVKNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSKIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFSNMLEEHQKLTVRAKLQTIKNKNLGNKKLNARMTAWLRKNT
Enzyme Length 992
Uniprot Accession Number A0A6J2ATK2
Absorption
Active Site ACT_SITE 417; /note=Proton acceptor; /evidence=ECO:0000305; ACT_SITE 505; /note=Proton donor; /evidence=ECO:0000305
Activity Regulation
Binding Site BINDING 241; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.11.-
Enzyme Function FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface (By similarity). Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern at or before hair follicle development (PubMed:22997338). {ECO:0000250|UniProtKB:Q6Q4G3, ECO:0000269|PubMed:22997338}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (1); Chain (1); Glycosylation (13); Initiator methionine (1); Metal binding (3); Region (2); Site (1); Topological domain (2); Transmembrane (1)
Keywords Aminopeptidase;Developmental protein;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 113,497
Kinetics
Metal Binding METAL 416; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 420; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 439; /note=Zinc; catalytic; /evidence=ECO:0000305
Rhea ID
Cross Reference Brenda