| IED ID |
IndEnz0002018479 |
| Enzyme Type ID |
protease018479 |
| Protein Name |
Growth/differentiation factor 8
GDF-8
Myostatin
|
| Gene Name |
Mstn Gdf8 |
| 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 |
MMQKLQMYVYIYLFMLIAAGPVDLNEGSEREENVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS |
| Enzyme Length |
376 |
| Uniprot Accession Number |
O08689 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000269|PubMed:14671324, ECO:0000269|PubMed:24076600, ECO:0000269|PubMed:9139826}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (8); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (2); Mutagenesis (2); Propeptide (1); Signal peptide (1); Site (1); Turn (1) |
| Keywords |
3D-structure;Cleavage on pair of basic residues;Cytokine;Disulfide bond;Glycoprotein;Growth factor;Heparin-binding;Reference proteome;Secreted;Signal |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14671324}. |
| Modified Residue |
|
| Post Translational Modification |
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase (PubMed:14671324). {ECO:0000269|PubMed:14671324}. |
| Signal Peptide |
SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D |
X-ray crystallography (3) |
| Cross Reference PDB |
3HH2;
3SEK;
5JI1;
|
| Mapped Pubmed ID |
10444569;
10508689;
10962344;
11459935;
11599046;
11641715;
11855847;
11877467;
11940514;
12029139;
12054591;
12115949;
12194980;
12222823;
12242286;
12244043;
12388123;
12447939;
12459784;
12546816;
12559964;
12559968;
12618358;
12704695;
12717734;
12749855;
12761853;
12824080;
12963705;
14504233;
14517293;
14973295;
14976141;
15342483;
15466422;
15468312;
15567067;
15681832;
15699335;
15822605;
15878958;
15973171;
15975431;
16003464;
16054590;
16077203;
16078270;
16079293;
16110473;
16141072;
16182246;
16219664;
16330774;
16404405;
16423875;
16491296;
16602821;
16709649;
16723712;
16763166;
16837207;
16916601;
16972257;
17030820;
17038559;
17039257;
17148752;
17267614;
17336525;
17383950;
17551508;
17592022;
17596894;
17597062;
17726519;
17878677;
17881772;
17949710;
17959898;
18038928;
18049864;
18162552;
18163379;
18175804;
18252947;
18255059;
18286185;
18316481;
18334608;
18339631;
18389502;
18391535;
18453534;
18535106;
18596030;
18621057;
18795097;
18852073;
19086062;
19129464;
19141683;
19208906;
19295913;
19298661;
19342595;
19351500;
19357233;
19406121;
19435857;
19477958;
19509018;
19509079;
19591015;
19654287;
19663901;
19715499;
19725775;
19726871;
19736304;
19759331;
19899116;
20010628;
20036643;
20065166;
20079729;
20161803;
20171187;
20233748;
20412806;
20419100;
20544938;
20568119;
20592178;
20595537;
20595541;
20623149;
20624929;
20810712;
20877574;
20884321;
20980549;
21054789;
21082689;
21147879;
21204650;
21266502;
21267068;
21347623;
21390326;
21406613;
21416223;
21421824;
21427410;
21507246;
21565991;
21618442;
21677277;
21689628;
21732194;
21756198;
21927895;
21964591;
22056524;
22058168;
22079083;
22079631;
22125316;
22155110;
22202673;
22205678;
22277753;
22318951;
22393251;
22431133;
22439337;
22640741;
22682244;
22685331;
22711460;
22711699;
22791505;
22869749;
22906226;
22910409;
22941030;
22995402;
23129614;
23178301;
23201547;
23295128;
23297411;
23324137;
23362117;
23465590;
23485710;
23516508;
23632633;
23752591;
23770987;
23868854;
23918385;
23979839;
24011072;
24019467;
24145431;
24333131;
24342526;
24344126;
24438338;
24445322;
24498167;
24504412;
24517228;
24575400;
24671706;
24680839;
24718581;
24807786;
24952961;
24965795;
25147795;
25179606;
25277978;
25304272;
25336187;
25528587;
25657005;
25695746;
25695797;
25725788;
25807490;
25808276;
25810521;
25869071;
25878062;
25958325;
25959011;
26075897;
26198127;
26219865;
26236992;
26252892;
26275053;
26304113;
26340892;
26372181;
26489925;
26549246;
26580671;
26644908;
26769954;
26923583;
26944368;
27015310;
27076790;
27129272;
27148972;
27214824;
27297797;
27312354;
27494364;
27549031;
27559042;
27581061;
27647997;
27821779;
27965203;
28073155;
28074479;
28170423;
28257634;
28270449;
28334989;
28465350;
28533420;
28676454;
28852138;
28870245;
28928419;
28956216;
29024627;
29192067;
29348202;
30078553;
30121012;
30129974;
30139748;
30222937;
30576242;
30726112;
30777303;
30808964;
30814254;
30888862;
30998775;
31073529;
31187730;
31200956;
31657476;
31751423;
31830002;
31960486;
32071240;
32156541;
32432932;
32459523;
32710883;
32900939;
33003470;
33034787;
33219121;
33220490;
33284091;
33295877;
33348054;
33554779;
34080650;
34131275;
34239010;
34359850;
34440852;
9335610;
9356471;
9680391;
9988218;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
42,921 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|