MYOC
entrez
4653
canonical
uniprot
Q99972
canonical
ensembl
ENSG00000034971
resolver
ensp
ENSP00000037502
resolver
enst
ENST00000037502
resolver
genesymbol
MYOC
resolver
genesymbol_syn
GLC1A
resolver
genesymbol_syn
TIGR
resolver
hgnc
HGNC:7610
resolver
uniprot
A0A0S2Z421
resolver
uniprot
B2RD84
resolver
uniprot
O00620
resolver
uniprot
Q7Z6Q9
resolver
uniprot_entry
A0A0S2Z421_HUMAN
resolver
uniprot_entry
MYOC_HUMAN
resolver
uniprot_sec
B2RD84
resolver
uniprot_sec
O00620
resolver
uniprot_sec
Q7Z6Q9
resolver
amino_acid_sequence
MRFFCARCCSFGPEMPAVQLLLLACLVWDVGARTAQLRKANDQSGRCQYTFSVASPNESSCPEQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVPPGSREVSTWNLDTLAFQELKSELTEVPASRILKESPSGYLRSGEGDTGCGELVWVGEPLTLRTAETITGKYGVWMRDPKPTYPYTQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGAVVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSKLNPENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKKLFAWDNLNMVTYDIKLSKM
uniprot
proteins
disease_involvement
DISEASE: Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. {ECO:0000269|PubMed:10196380, ECO:0000269|PubMed:10330365, ECO:0000269|PubMed:10340788, ECO:0000269|PubMed:10644174, ECO:0000269|PubMed:10798654, ECO:0000269|PubMed:10819638, ECO:0000269|PubMed:10873982, ECO:0000269|PubMed:10916185, ECO:0000269|PubMed:10980537, ECO:0000269|PubMed:11004290, ECO:0000269|PubMed:11774072, ECO:0000269|PubMed:12189160, ECO:0000269|PubMed:12356829, ECO:0000269|PubMed:12362081, ECO:0000269|PubMed:12442283, ECO:0000269|PubMed:12860809, ECO:0000269|PubMed:12872267, ECO:0000269|PubMed:15025728, ECO:0000269|PubMed:15255110, ECO:0000269|PubMed:15534471, ECO:0000269|PubMed:15795224, ECO:0000269|PubMed:16401791, ECO:0000269|PubMed:17210859, ECO:0000269|PubMed:17499207, ECO:0000269|PubMed:25524706, ECO:0000269|PubMed:9005853, ECO:0000269|PubMed:9328473, ECO:0000269|PubMed:9345106, ECO:0000269|PubMed:9361308, ECO:0000269|PubMed:9490287, ECO:0000269|PubMed:9510647, ECO:0000269|PubMed:9521427, ECO:0000269|PubMed:9535666, ECO:0000269|PubMed:9697688, ECO:0000269|PubMed:9792882, ECO:0000269|PubMed:9863594}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. {ECO:0000269|PubMed:15733270}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. MYOC mutations may contribute to GLC3A via digenic inheritance with CYP1B1 and/or another locus associated with the disease (PubMed:15733270). {ECO:0000269|PubMed:15733270}.
uniprot
proteins
function
FUNCTION: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork. {ECO:0000250|UniProtKB:O70624, ECO:0000269|PubMed:17516541, ECO:0000269|PubMed:17984096, ECO:0000269|PubMed:18855004, ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:19959812, ECO:0000269|PubMed:21656515, ECO:0000269|PubMed:23629661, ECO:0000269|PubMed:23897819}.
uniprot
proteins
mass_dalton
56972
uniprot
proteins
mutagenesis
MUTAGEN 226..230; /note="Missing: Impairs endoproteolytic processing."; /evidence="ECO:0000269|PubMed:17650508"; MUTAGEN 226; /note="R->A: Reduced processing. Impairs endoproteolytic processing; when associated with A-229 or A-230. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-229 or A-230."; /evidence="ECO:0000269|PubMed:17650508"; MUTAGEN 226; /note="R->Q: Slightly increases endoproteolytic processing."; /evidence="ECO:0000269|PubMed:17650508"; MUTAGEN 227; /note="I->G: Reduced processing."; /evidence="ECO:0000269|PubMed:17650508"; MUTAGEN 229; /note="K->A: Completely blocks endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226."; /evidence="ECO:0000269|PubMed:17650508"; MUTAGEN 230; /note="E->A: Impairs endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and released a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226."; /evidence="ECO:0000269|PubMed:17650508
uniprot
proteins
post_translational_modification
PTM: Different isoforms may arise by post-translational modifications. {ECO:0000269|PubMed:9497363}.; PTM: Glycosylated. {ECO:0000269|PubMed:11431441, ECO:0000269|PubMed:12697062, ECO:0000269|PubMed:17650508, ECO:0000269|PubMed:19287508}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.; PTM: Undergoes a calcium-dependent proteolytic cleavage at Arg-226 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain. {ECO:0000269|PubMed:15795224, ECO:0000269|PubMed:17650508}.
uniprot
proteins
pubmed
10196380
uniprot
proteins
pubmed
10330365
uniprot
proteins
pubmed
10340788
uniprot
proteins
pubmed
10644174
uniprot
proteins
pubmed
10798654
uniprot
proteins
pubmed
10819638
uniprot
proteins
pubmed
10873982
uniprot
proteins
pubmed
10916185
uniprot
proteins
pubmed
10980537
uniprot
proteins
pubmed
11004290
uniprot
proteins
pubmed
11053284
uniprot
proteins
pubmed
11431441
uniprot
proteins
pubmed
11773026
uniprot
proteins
pubmed
11773029
uniprot
proteins
pubmed
11774072
uniprot
proteins
pubmed
11923248
uniprot
proteins
pubmed
12019210
uniprot
proteins
pubmed
12189160
uniprot
proteins
pubmed
12356829
uniprot
proteins
pubmed
12362081
uniprot
proteins
pubmed
12442283
uniprot
proteins
pubmed
12615070
uniprot
proteins
pubmed
12697062
uniprot
proteins
pubmed
12860809
uniprot
proteins
pubmed
12872267
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15025728
uniprot
proteins
pubmed
15255110
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15534471
uniprot
proteins
pubmed
15733270
uniprot
proteins
pubmed
15795224
uniprot
proteins
pubmed
15944158
uniprot
proteins
pubmed
16401791
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17210859
uniprot
proteins
pubmed
17499207
uniprot
proteins
pubmed
17516541
uniprot
proteins
pubmed
17650508
uniprot
proteins
pubmed
17984096
uniprot
proteins
pubmed
18855004
uniprot
proteins
pubmed
19188438
uniprot
proteins
pubmed
19287508
uniprot
proteins
pubmed
19959812
uniprot
proteins
pubmed
21656515
uniprot
proteins
pubmed
23629661
uniprot
proteins
pubmed
23897819
uniprot
proteins
pubmed
25524706
uniprot
proteins
pubmed
9005853
uniprot
proteins
pubmed
9169133
uniprot
proteins
pubmed
9280311
uniprot
proteins
pubmed
9328473
uniprot
proteins
pubmed
9345106
uniprot
proteins
pubmed
9361308
uniprot
proteins
pubmed
9446806
uniprot
proteins
pubmed
9490287
uniprot
proteins
pubmed
9497363
uniprot
proteins
pubmed
9510647
uniprot
proteins
pubmed
9521427
uniprot
proteins
pubmed
9535666
uniprot
proteins
pubmed
9548973
uniprot
proteins
pubmed
9697688
uniprot
proteins
pubmed
9792882
uniprot
proteins
pubmed
9863594
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11431441, ECO:0000269|PubMed:12697062, ECO:0000269|PubMed:19287508, ECO:0000269|PubMed:9497363}. Golgi apparatus {ECO:0000269|PubMed:11053284}. Cytoplasmic vesicle {ECO:0000269|PubMed:11431441}. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:11773026, ECO:0000305|PubMed:11431441}. Secreted, extracellular exosome {ECO:0000269|PubMed:15944158}. Mitochondrion {ECO:0000269|PubMed:17516541}. Mitochondrion intermembrane space {ECO:0000269|PubMed:17516541}. Mitochondrion inner membrane {ECO:0000269|PubMed:17516541}. Mitochondrion outer membrane {ECO:0000269|PubMed:17516541}. Rough endoplasmic reticulum {ECO:0000269|PubMed:19287508}. Cell projection. Cell projection, cilium {ECO:0000269|PubMed:9169133}. Note=Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum (PubMed:9169133). It is only imported to mitochondria in the trabecular meshwork (PubMed:17516541). Localizes to the Golgi apparatus in Schlemm's canal endothelial cells (PubMed:11053284). Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles (PubMed:15944158). Localizes in trabecular meshwork extracellular matrix (PubMed:15944158). {ECO:0000269|PubMed:11053284, ECO:0000269|PubMed:15944158, ECO:0000269|PubMed:17516541, ECO:0000269|PubMed:9169133}.; SUBCELLULAR LOCATION: [Myocilin, C-terminal fragment]: Secreted.; SUBCELLULAR LOCATION: [Myocilin, N-terminal fragment]: Endoplasmic reticulum. Note=Remains retained in the endoplasmic reticulum.
uniprot
proteins