Detail Information for IndEnz0002007276
IED ID IndEnz0002007276
Enzyme Type ID protease007276
Protein Name Pannexin-1
Gene Name PANX1 MRS1 UNQ2529/PRO6028
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 MAIAQLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPPLFWRFAAAPHICSDLKFIMEELDKVYNRAIKAAKSARDLDMRDGACSVPGVTENLGQSLWEVSESHFKYPIVEQYLKTKKNSNNLIIKYISCRLLTLIIILLACIYLGYYFSLSSLSDEFVCSIKSGILRNDSTVPDQFQCKLIAVGIFQLLSVINLVVYVLLAPVVVYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISEVKSYKCLKVLENIKSSGQGIDPMLLLTNLGMIKMDVVDGKTPMSAEMREEQGNQTAELQGMNIDSETKANNGEKNARQRLLDSSC
Enzyme Length 426
Uniprot Accession Number Q96RD7
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Structural component of the gap junctions and the hemichannels involved in the ATP release and nucleotide permeation (PubMed:16908669, PubMed:20829356, PubMed:30918116). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (PubMed:16908669). Plays a critical role in oogenesis (PubMed:30918116). {ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:20829356, ECO:0000269|PubMed:30918116}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (9); Chain (1); Glycosylation (1); Helix (19); Modified residue (2); Mutagenesis (3); Natural variant (7); Region (1); Sequence conflict (2); Topological domain (5); Transmembrane (4); Turn (4)
Keywords 3D-structure;Alternative splicing;Calcium;Calcium channel;Calcium transport;Cell junction;Cell membrane;Differentiation;Disease variant;Endoplasmic reticulum;Gap junction;Glycoprotein;Ion channel;Ion transport;Membrane;Oogenesis;Reference proteome;S-nitrosylation;Transmembrane;Transmembrane helix;Transport
Interact With P02652; Q9BQE5; P41181; Q92843; Q9BXR6; Q96IV6; P37268; Q9NVC3; Q8NBD8; P01375; O95183; Q14508; Itself
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30918116}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:17715132}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
Modified Residue MOD_RES 40; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:Q9JIP4; MOD_RES 347; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:Q9JIP4
Post Translational Modification PTM: S-nitrosylation inhibits channel currents and ATP release. {ECO:0000250|UniProtKB:Q9JIP4}.; PTM: N-glycosylation may play a role in cell surface targeting (By similarity). Exists in three glycosylation states: non-glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated (GLY2) (PubMed:30918116). {ECO:0000250|UniProtKB:Q9JIP4, ECO:0000269|PubMed:30918116}.
Signal Peptide
Structure 3D Electron microscopy (15)
Cross Reference PDB 6LTN; 6LTO; 6M02; 6M66; 6M67; 6M68; 6V6D; 6WBF; 6WBG; 6WBI; 6WBK; 6WBL; 6WBM; 6WBN; 7DWB;
Mapped Pubmed ID 12958598; 14597722; 16682648; 16690868; 17036048; 17240370; 17925379; 18596211; 19056988; 19150332; 19213873; 20086016; 20516070; 20622111; 20628624; 20660288; 20884646; 20944749; 21606493; 21659516; 21791690; 2182768; 21865551; 22311122; 22753409; 22947051; 22972801; 23033481; 23456773; 23549611; 23594276; 23700432; 23798685; 23918924; 23936165; 24146091; 24418937; 24531690; 24646995; 24655807; 24671093; 25008946; 25112874; 25170954; 25301060; 25947940; 26009197; 26009198; 26054298; 26098574; 26223428; 26242575; 26385361; 26496610; 26638075; 26755773; 26823467; 27025600; 27109381; 27518505; 27720686; 27741412; 27883084; 28036289; 28134257; 28142297; 28389204; 28735901; 29222846; 29357945; 29393654; 29676177; 29802622; 29848662; 29882918; 29932112; 30061676; 30377218; 30814251; 31110238; 31211503; 31242494; 31278290; 31410978; 31694915; 31698505; 32023876; 32203128; 32231289; 32246089; 32284561; 32312847; 32494015; 32639715; 32931038; 33050989; 33052098; 33345473; 33394272; 33405952; 33499026; 33564071; 33647315; 33947837; 34067798; 34301959; 34380770; 34796785; 450099;
Motif
Gene Encoded By
Mass 48,050
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda