| IED ID |
IndEnz0002007839 |
| Enzyme Type ID |
protease007839 |
| Protein Name |
Pannexin-1
|
| Gene Name |
Panx1 |
| Organism |
Mus musculus (Mouse) |
| 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
Mus
Mus
Mus musculus (Mouse)
|
| Enzyme Sequence |
MAIAHLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKSSLQSESGNLPLWLHKFFPYILLLFAILLYLPALFWRFSAAPHLCSDLKFIMEELDKVYNRAIKAAKSARDLDLRDGPGPPGVTENVGQSLWEISESHFKYPIVEQYLKTKKNSSHLIMKYISCRLVTFVVILLACIYLSYYFSLSSLSDEFLCSIKSGVLKNDSTIPDRFQCKLIAVGIFQLLSLINLIVYALLIPVVVYTFFIPFRQKTDILKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISELKSYKCLKVLENIKSNGQGIDPMLLLTNLGMIKMDIIDGKIPTSLQTKGEDQGSQRVEFKDLDLSSEAAANNGEKNSRQRLLNPSC |
| Enzyme Length |
426 |
| Uniprot Accession Number |
Q9JIP4 |
| 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. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity). {ECO:0000250}.; FUNCTION: Structural component of the gap junctions and the hemichannels involved in the ATP release and nucleotide permeation. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis. Plays a critical role in oogenesis. {ECO:0000250|UniProtKB:Q96RD7}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Glycosylation (1); Modified residue (2); Mutagenesis (4); Sequence conflict (3); Topological domain (5); Transmembrane (4) |
| Keywords |
Calcium;Calcium channel;Calcium transport;Cell junction;Cell membrane;Endoplasmic reticulum;Gap junction;Glycoprotein;Ion channel;Ion transport;Membrane;Reference proteome;S-nitrosylation;Transmembrane;Transmembrane helix;Transport |
| Interact With |
P97382 |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96RD7}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250|UniProtKB:Q96RD7}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. |
| Modified Residue |
MOD_RES 40; /note=S-nitrosocysteine; /evidence=ECO:0000269|PubMed:23033481; MOD_RES 346; /note=S-nitrosocysteine; /evidence=ECO:0000269|PubMed:23033481 |
| Post Translational Modification |
PTM: S-nitrosylation inhibits channel currents and ATP release. {ECO:0000269|PubMed:23033481}.; PTM: N-glycosylation may play a role in cell surface targeting (PubMed:17925379). Exists in three glycosylation states: non-glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated (GLY2) (By similarity). {ECO:0000250|UniProtKB:Q96RD7, ECO:0000269|PubMed:17925379}. |
| Signal Peptide |
|
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
11217851;
12466851;
14597722;
15028292;
15661370;
16026466;
16143426;
16616526;
17009242;
17149368;
17379420;
17389364;
17433728;
18322214;
18490713;
18596211;
18649185;
18695503;
18945939;
19009624;
19047635;
19056988;
19130485;
19213873;
19416975;
19474335;
19692571;
19780818;
20086016;
20332104;
20664064;
20829356;
21267068;
21505260;
21508259;
21546608;
21606493;
21677750;
21865551;
21949881;
21983290;
22002608;
22147915;
22235111;
22267745;
22311983;
22384122;
22426419;
22458943;
22499153;
22707207;
22753409;
22768083;
22785119;
22797941;
22915101;
22945868;
22952282;
22956545;
22956847;
22965528;
22982782;
23111424;
23284764;
23390418;
23449592;
23549611;
23583931;
23659289;
23675350;
23742824;
23827947;
23885286;
23964896;
24194600;
24522432;
24531690;
24590064;
24646995;
24668173;
24694658;
24751934;
24839011;
24860098;
24885326;
25056878;
25070895;
25080488;
25100586;
25170954;
25309319;
25327779;
25360084;
25605289;
25637780;
25690012;
25796110;
25819435;
25947940;
25987548;
26002464;
26035172;
26109673;
26126730;
26136251;
26163370;
26195825;
26242575;
26386583;
26413467;
26453396;
26553756;
26572062;
26573818;
26596404;
26792207;
26818508;
26828725;
26839965;
27076682;
27099931;
27159053;
27255725;
27548819;
27626380;
27769744;
27784763;
27797339;
27910899;
28134928;
28158679;
28195232;
28445139;
28705898;
28751666;
28780469;
28855161;
29057961;
29087614;
29098296;
29221793;
29234270;
29246445;
29563335;
29643381;
29710868;
29744875;
29745255;
29848662;
29866797;
29952014;
29987408;
30077007;
30377218;
30385873;
30655582;
30745457;
30814251;
30862176;
30902848;
30918989;
30930743;
30952430;
31033038;
31118206;
31202174;
31202927;
31400255;
31411729;
31554905;
31818976;
31849935;
32070042;
32132172;
32238926;
32241676;
32260308;
32446934;
32819386;
33248294;
33449849;
33525532;
33635784;
33641341;
33653920;
33910381;
34067798;
34283971;
34380770;
34489419;
34490843;
34639052;
34676213;
34694360;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
48,167 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|