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Myocilin (Myocilin 55 kDa subunit) (Trabecular meshwork-induced glucocorticoid response protein) [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)]

 MYOC_HUMAN              Reviewed;         504 AA.
Q99972; B2RD84; O00620; Q7Z6Q9;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
25-OCT-2017, entry version 166.
RecName: Full=Myocilin {ECO:0000303|PubMed:9169133};
AltName: Full=Myocilin 55 kDa subunit;
AltName: Full=Trabecular meshwork-induced glucocorticoid response protein {ECO:0000303|PubMed:9497363};
Contains:
RecName: Full=Myocilin, N-terminal fragment;
AltName: Full=Myocilin 20 kDa N-terminal fragment;
Contains:
RecName: Full=Myocilin, C-terminal fragment;
AltName: Full=Myocilin 35 kDa N-terminal fragment;
Flags: Precursor;
Name=MYOC; Synonyms=GLC1A, TIGR {ECO:0000303|PubMed:9280311};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9280311; DOI=10.1016/S0014-5793(97)00934-4;
Ortego J., Escribano J., Coca-Prados M.;
"Cloning and characterization of subtracted cDNAs from a human ciliary
body library encoding TIGR, a protein involved in juvenile open angle
glaucoma with homology to myosin and olfactomedin.";
FEBS Lett. 413:349-353(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Retina;
PubMed=9169133; DOI=10.1006/geno.1997.4682;
Kubota R., Noda S., Wang Y., Minoshima S., Asakawa S., Kudoh J.,
Mashima Y., Oguchi Y., Shimizu N.;
"A novel myosin-like protein (myocilin) expressed in the connecting
cilium of the photoreceptor: molecular cloning, tissue expression, and
chromosomal mapping.";
Genomics 41:360-369(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLC1A ARG-246;
LEU-370; SER-477; LYS-480 AND PHE-499.
TISSUE=Leukocyte;
PubMed=9328473; DOI=10.1093/hmg/6.12.2091;
Adam M.F., Belmouden A., Binisti P., Brezin A.P., Valtot F.,
Bechetoille A., Dascotte J.-C., Copin B., Gomez L., Chaventre A.,
Bach J.-F., Garchon H.-J.;
"Recurrent mutations in a single exon encoding the evolutionarily
conserved olfactomedin-homology domain of TIGR in familial open-angle
glaucoma.";
Hum. Mol. Genet. 6:2091-2097(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS GLC1A VAL-364
AND HIS-437.
PubMed=9005853; DOI=10.1126/science.275.5300.668;
Stone E.M., Fingert J.H., Alward W.L.M., Nguyen T.D., Polansky J.R.,
Sunden S.L.F., Nishimura D., Clark A.F., Nystuen A., Nichols B.E.,
Mackey D.A., Ritch R., Kalenak J.W., Craven E.R., Sheffield V.C.;
"Identification of a gene that causes primary open angle glaucoma.";
Science 275:668-670(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9446806; DOI=10.1006/bbrc.1997.7972;
Kubota R., Kudoh J., Mashima Y., Asakawa S., Minoshima S.,
Hejtmancik J.F., Oguchi Y., Shimizu N.;
"Genomic organization of the human myocilin gene (MYOC) responsible
for primary open angle glaucoma (GLC1A).";
Biochem. Biophys. Res. Commun. 242:396-400(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9548973;
Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C.,
Alward W.L.M., Sheffield V.C., Stone E.M.;
"Characterization and comparison of the human and mouse GLC1A glaucoma
genes.";
Genome Res. 8:377-384(1998).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 1-6 AND 33-37, SEQUENCE REVISION, OLIGOMERIZATION,
SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION BY GLUCOCORTICOIDS.
PubMed=9497363; DOI=10.1074/jbc.273.11.6341;
Nguyen T.D., Chen P., Huang W.D., Chen H., Johnson D., Polansky J.R.;
"Gene structure and properties of TIGR, an olfactomedin-related
glycoprotein cloned from glucocorticoid-induced trabecular meshwork
cells.";
J. Biol. Chem. 273:6341-6350(1998).
[12]
PROTEIN SEQUENCE OF 33-37, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=19287508;
Sohn S., Joe M.K., Kim T.E., Im J.E., Choi Y.R., Park H., Kee C.;
"Dual localization of wild-type myocilin in the endoplasmic reticulum
and extracellular compartment likely occurs due to its incomplete
secretion.";
Mol. Vis. 15:545-556(2009).
[13]
PROTEIN SEQUENCE OF 227-233, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
CHARACTERIZATION OF VARIANTS GLC1A LYS-323; LEU-370 AND GLY-380, AND
PROTEOLYTIC PROCESSING.
PubMed=15795224; DOI=10.1074/jbc.M501340200;
Aroca-Aguilar J.D., Sanchez-Sanchez F., Ghosh S., Coca-Prados M.,
Escribano J.;
"Myocilin mutations causing glaucoma inhibit the intracellular
endoproteolytic cleavage of myocilin between amino acids Arg226 and
Ile227.";
J. Biol. Chem. 280:21043-21051(2005).
[14]
SUBCELLULAR LOCATION.
PubMed=11053284;
O'Brien E.T., Ren X., Wang Y.;
"Localization of myocilin to the golgi apparatus in Schlemm's canal
cells.";
Invest. Ophthalmol. Vis. Sci. 41:3842-3849(2000).
[15]
SUBCELLULAR LOCATION, INDUCTION BY GLUCOCORTICOIDS, GLYCOSYLATION, AND
TISSUE SPECIFICITY.
PubMed=11431441;
Clark A.F., Steely H.T., Dickerson J.E. Jr., English-Wright S.,
Stropki K., McCartney M.D., Jacobson N., Shepard A.R., Clark J.I.,
Matsushima H., Peskind E.R., Leverenz J.B., Wilkinson C.W.,
Swiderski R.E., Fingert J.H., Sheffield V.C., Stone E.M.;
"Glucocorticoid induction of the glaucoma gene MYOC in human and
monkey trabecular meshwork cells and tissues.";
Invest. Ophthalmol. Vis. Sci. 42:1769-1780(2001).
[16]
INTERACTION WITH OLFM3.
PubMed=12019210; DOI=10.1093/hmg/11.11.1291;
Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.;
"Optimedin: a novel olfactomedin-related protein that interacts with
myocilin.";
Hum. Mol. Genet. 11:1291-1301(2002).
[17]
INTERACTION WITH FN1, AND SUBCELLULAR LOCATION.
PubMed=11773026;
Filla M.S., Liu X., Nguyen T.D., Polansky J.R., Brandt C.R.,
Kaufman P.L., Peters D.M.;
"In vitro localization of TIGR/MYOC in trabecular meshwork
extracellular matrix and binding to fibronectin.";
Invest. Ophthalmol. Vis. Sci. 43:151-161(2002).
[18]
INTERACTION WITH MYL2.
PubMed=11773029;
Wentz-Hunter K., Ueda J., Yue B.Y.;
"Protein interactions with myocilin.";
Invest. Ophthalmol. Vis. Sci. 43:176-182(2002).
[19]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11923248;
Ueda J., Wentz-Hunter K., Yue B.Y.;
"Distribution of myocilin and extracellular matrix components in the
juxtacanalicular tissue of human eyes.";
Invest. Ophthalmol. Vis. Sci. 43:1068-1076(2002).
[20]
DISULFIDE BOND AT 245-CYS--CYS-433.
PubMed=12615070; DOI=10.1016/S0006-291X(03)00198-0;
Nagy I., Trexler M., Patthy L.;
"Expression and characterization of the olfactomedin domain of human
myocilin.";
Biochem. Biophys. Res. Commun. 302:554-561(2003).
[21]
CHARACTERIZATION OF VARIANT SER-57, GLYCOSYLATION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
PubMed=12697062; DOI=10.1186/1471-2156-4-5;
Shepard A.R., Jacobson N., Sui R., Steely H.T., Lotery A.J.,
Stone E.M., Clark A.F.;
"Characterization of rabbit myocilin: implications for human myocilin
glycosylation and signal peptide usage.";
BMC Genet. 4:5-5(2003).
[22]
SUBCELLULAR LOCATION.
PubMed=15944158; DOI=10.1074/jbc.M504803200;
Hardy K.M., Hoffman E.A., Gonzalez P., McKay B.S., Stamer W.D.;
"Extracellular trafficking of myocilin in human trabecular meshwork
cells.";
J. Biol. Chem. 280:28917-28926(2005).
[23]
CLEAVAGE BY CAPN2, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
MUTAGENESIS OF 226-ARG--GLU-230; ARG-226; ILE-227; LYS-229 AND
GLU-230.
PubMed=17650508; DOI=10.1074/jbc.M609608200;
Sanchez-Sanchez F., Martinez-Redondo F., Aroca-Aguilar J.D.,
Coca-Prados M., Escribano J.;
"Characterization of the intracellular proteolytic cleavage of
myocilin and identification of calpain II as a myocilin-processing
protease.";
J. Biol. Chem. 282:27810-27824(2007).
[24]
FUNCTION IN MITOCHONDRIAL DEPOLARIZATION, AND SUBCELLULAR LOCATION.
PubMed=17516541; DOI=10.1002/jcp.21147;
Sakai H., Shen X., Koga T., Park B.C., Noskina Y., Tibudan M.,
Yue B.Y.;
"Mitochondrial association of myocilin, product of a glaucoma gene, in
human trabecular meshwork cells.";
J. Cell. Physiol. 213:775-784(2007).
[25]
FUNCTION IN CELL-MATRIX ADHESION.
PubMed=17984096; DOI=10.1074/jbc.M708250200;
Shen X., Koga T., Park B.C., SundarRaj N., Yue B.Y.;
"Rho GTPase and cAMP/protein kinase A signaling mediates myocilin-
induced alterations in cultured human trabecular meshwork cells.";
J. Biol. Chem. 283:603-612(2008).
[26]
FUNCTION IN CELL ADHESION.
PubMed=18855004; DOI=10.1007/s00418-008-0518-4;
Goldwich A., Scholz M., Tamm E.R.;
"Myocilin promotes substrate adhesion, spreading and formation of
focal contacts in podocytes and mesangial cells.";
Histochem. Cell Biol. 131:167-180(2009).
[27]
FUNCTION IN STRESS FIBER ASSEMBLY, INTERACTION WITH FRZB; FZD7; FZD10;
FZD1 AND WIF1, AND CHARACTERIZATION OF VARIANT ASN-477.
PubMed=19188438; DOI=10.1128/MCB.01274-08;
Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
"Myocilin is a modulator of Wnt signaling.";
Mol. Cell. Biol. 29:2139-2154(2009).
[28]
FUNCTION IN NEURITE OUTGROWTH.
PubMed=19959812; DOI=10.2353/ajpath.2010.090194;
Koga T., Shen X., Park J.S., Qiu Y., Park B.C., Shyam R., Yue B.Y.;
"Differential effects of myocilin and optineurin, two glaucoma genes,
on neurite outgrowth.";
Am. J. Pathol. 176:343-352(2010).
[29]
FUNCTION IN CELL MIGRATION.
PubMed=21656515; DOI=10.1002/jcp.22701;
Kwon H.S., Tomarev S.I.;
"Myocilin, a glaucoma-associated protein, promotes cell migration
through activation of integrin-focal adhesion kinase-serine/threonine
kinase signaling pathway.";
J. Cell. Physiol. 226:3392-3402(2011).
[30]
FUNCTION IN OSTEOBLAST DIFFERENTIATION.
PubMed=23629661; DOI=10.1074/jbc.M112.422972;
Kwon H.S., Johnson T.V., Tomarev S.I.;
"Myocilin stimulates osteogenic differentiation of mesenchymal stem
cells through mitogen-activated protein kinase signaling.";
J. Biol. Chem. 288:16882-16894(2013).
[31]
FUNCTION IN MYELINATION, AND INTERACTION WITH NFASC; GLDN AND NRCAM.
PubMed=23897819; DOI=10.1074/jbc.M112.446138;
Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
Tomarev S.I.;
"Myocilin mediates myelination in the peripheral nervous system
through ErbB2/3 signaling.";
J. Biol. Chem. 288:26357-26371(2013).
[32]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 228-504 IN COMPLEX WITH
CALCIUM, DISULFIDE BONDS, CHARACTERIZATION OF VARIANTS GLC1A LYS-293;
ILE-353 AND VAL-445, AND CHARACTERIZATION OF VARIANTS MET-329;
CYS-422; PRO-425 AND CYS-473.
PubMed=25524706; DOI=10.1093/hmg/ddu730;
Donegan R.K., Hill S.E., Freeman D.M., Nguyen E., Orwig S.D.,
Turnage K.C., Lieberman R.L.;
"Structural basis for misfolding in myocilin-associated glaucoma.";
Hum. Mol. Genet. 24:2111-2124(2015).
[33]
VARIANTS GLC1A ARG-367 AND LEU-370.
PubMed=9345106; DOI=10.1086/301612;
Suzuki Y., Shirato S., Taniguchi F., Ohara K., Nishimaki K., Ohta S.;
"Mutations in the TIGR gene in familial primary open-angle glaucoma in
Japan.";
Am. J. Hum. Genet. 61:1202-1204(1997).
[34]
VARIANT GLC1A PRO-341.
PubMed=9510647; DOI=10.3341/kjo.1997.11.2.75;
Kee C., Ahn B.-H.;
"TIGR gene in primary open-angle glaucoma and steroid-induced
glaucoma.";
Korean J. Ophthalmol. 11:75-78(1997).
[35]
VARIANT GLC1A ARG-337.
PubMed=9361308; DOI=10.3109/13816819709057124;
Stoilova D., Child A., Brice G., Crick R.P., Fleck B.W., Sarfarazi M.;
"Identification of a new 'TIGR' mutation in a family with juvenile-
onset primary open angle glaucoma.";
Ophthalmic Genet. 18:109-118(1997).
[36]
VARIANTS GLC1A LYS-352; LEU-370; MET-377 AND HIS-437.
PubMed=9792882; DOI=10.1086/302098;
Wiggs J.L., Allingham R.R., Vollrath D., Jones K.H., De La Paz M.,
Kern J., Patterson K., Babb V.L., Del Bono E.A., Broomer B.W.,
Pericak-Vance M.A., Haines J.L.;
"Prevalence of mutations in TIGR/Myocilin in patients with adult and
juvenile primary open-angle glaucoma.";
Am. J. Hum. Genet. 63:1549-1552(1998).
[37]
VARIANTS GLC1A ARG-367 AND LEU-370.
PubMed=9490287; DOI=10.1007/s004390050661;
Michels-Rautenstrauss K.G., Mardin C.Y., Budde W.M., Liehr T.,
Polansky J.R., Nguyen T., Timmerman V., van Broeckhoven C.,
Naumann G.O.H., Pfeiffer R.A., Rautenstrauss B.W.;
"Juvenile open angle glaucoma: fine mapping of the TIGR gene to
1q24.3-q25.2 and mutation analysis.";
Hum. Genet. 102:103-106(1998).
[38]
VARIANTS GLC1A ARG-367 AND PHE-426.
PubMed=9521427;
DOI=10.1002/(SICI)1098-1004(1998)11:3<244::AID-HUMU10>3.0.CO;2-Z;
Mansergh F.C., Kenna P.F., Ayuso C., Kiang A.-S., Humphries P.,
Farrar G.J.;
"Novel mutations in the TIGR gene in early and late onset open angle
glaucoma.";
Hum. Mutat. 11:244-251(1998).
[39]
VARIANTS GLC1A LEU-370; ALA-380 AND PRO-502, AND VARIANT LYS-76.
PubMed=9863594; DOI=10.1136/jmg.35.12.989;
Stoilova D., Child A., Brice G., Desai T., Barsoum-Homsy M.,
Ozdemir N., Chevrette L., Adam M.F., Garchon H.-J., Pitts Crick R.,
Sarfarazi M.;
"Novel TIGR/MYOC mutations in families with juvenile onset primary
open angle glaucoma.";
J. Med. Genet. 35:989-992(1998).
[40]
VARIANT GLC1A GLU-423.
PubMed=9697688; DOI=10.1038/1203;
Morissette J., Clepet C., Moisan S., Dubois S., Winstall E.,
Vermeeren D., Nguyen T.D., Polansky J.R., Cote G., Anctil J.-L.,
Amyot M., Plante M., Falardeau P., Raymond V.;
"Homozygotes carrying an autosomal dominant TIGR mutation do not
manifest glaucoma.";
Nat. Genet. 19:319-321(1998).
[41]
VARIANTS GLC1A, AND VARIANTS.
PubMed=9535666; DOI=10.1056/NEJM199804093381503;
Alward W.L.M., Fingert J.H., Coote M.A., Johnson A.T., Lerner S.F.,
Junqua D., Durcan F.J., McCartney P.J., Mackey D.A., Sheffield V.C.,
Stone E.M.;
"Clinical features associated with mutations in the chromosome 1 open-
angle glaucoma gene.";
N. Engl. J. Med. 338:1022-1027(1998).
[42]
VARIANT GLC1A ILE-353.
PubMed=10330365; DOI=10.1086/302407;
Yoon S.-J.K., Kim H.-S., Moon J.-I., Lim J.M., Joo C.-K.;
"Mutations of the TIGR/MYOC gene in primary open-angle glaucoma in
Korea.";
Am. J. Hum. Genet. 64:1775-1778(1999).
[43]
VARIANTS GLC1A, AND VARIANTS.
PubMed=10196380; DOI=10.1093/hmg/8.5.899;
Fingert J.H., Heon E., Liebmann J.M., Yamamoto T., Craig J.E.,
Rait J., Kawase K., Hoh S.-T., Buys Y.M., Dickinson J., Hockey R.R.,
Williams-Lyn D., Trope G., Kitazawa Y., Ritch R., Mackey D.A.,
Alward W.L.M., Sheffield V.C., Stone E.M.;
"Analysis of myocilin mutations in 1703 glaucoma patients from five
different populations.";
Hum. Mol. Genet. 8:899-905(1999).
[44]
VARIANT GLC1A PRO-448.
PubMed=10340788; DOI=10.1016/S0021-5155(98)00077-X;
Yokoyama A., Nao-i N., Date Y., Nakazato M., Chumann H., Chihara E.,
Sawada A., Matsukura S.;
"Detection of a new TIGR gene mutation in a Japanese family with
primary open angle glaucoma.";
Jpn. J. Ophthalmol. 43:85-88(1999).
[45]
VARIANTS GLC1A ARG-252; GLY-272; LYS-323; LEU-370; MET-377; PHE-426;
ASN-477 AND SER-499, VARIANTS ASP-57; LYS-76; MET-329 AND ARG-398,
CHARACTERIZATION OF VARIANTS GLC1A ARG-252; GLY-272; LYS-323; LEU-370;
MET-377; PHE-426; ASN-477 AND SER-499, AND CHARACTERIZATION OF
VARIANTS ASP-57; LYS-76; MET-329 AND ARG-398.
PubMed=11004290; DOI=10.1016/S0002-9394(00)00536-5;
Shimizu S., Lichter P.R., Johnson A.T., Zhou Z., Higashi M.,
Gottfredsdottir M., Othman M., Moroi S.E., Rozsa F.W., Schertzer R.M.,
Clarke M.S., Schwartz A.L., Downs C.A., Vollrath D., Richards J.E.;
"Age-dependent prevalence of mutations at the GLC1A locus in primary
open-angle glaucoma.";
Am. J. Ophthalmol. 130:165-177(2000).
[46]
VARIANT GLC1A ARG-252.
PubMed=10873982; DOI=10.1136/bjo.84.7.722;
Booth A.P., Anwar R., Chen H., Churchill A.J., Jay J., Polansky J.,
Nguyen T., Markham A.F.;
"Genetic screening in a large family with juvenile onset primary open
angle glaucoma.";
Br. J. Ophthalmol. 84:722-726(2000).
[47]
VARIANT GLC1A ALA-53.
PubMed=10644174;
DOI=10.1002/(SICI)1098-1004(200001)15:1<122::AID-HUMU38>3.0.CO;2-O;
Pang C.P., Leung Y.F., Chua J.K.H., Baum L., Fan D.S.P., Lam D.S.;
"Novel TIGR sequence alteration Val53Ala.";
Hum. Mutat. 15:122-122(2000).
[48]
VARIANTS GLC1A GLN-158; ASN-360 AND THR-363, AND VARIANTS HIS-19;
LYS-76; GLU-208 AND HIS-470.
PubMed=10980537;
DOI=10.1002/1098-1004(200009)16:3<270::AID-HUMU13>3.0.CO;2-M;
Kubota R., Mashima Y., Ohtake Y., Tanino T., Kimura T., Hotta Y.,
Kanai A., Tokuoka S., Azuma I., Tanihara H., Inatani M., Inoue Y.,
Kudoh J., Oguchi Y., Shimizu N.;
"Novel mutations in the myocilin gene in Japanese glaucoma patients.";
Hum. Mutat. 16:270-270(2000).
[49]
VARIANTS GLC1A GLU-208 AND ILE-353, AND VARIANTS ARG-12 AND LYS-76.
PubMed=10798654;
Lam D.S.C., Leung Y.F., Chua J.K.H., Baum L., Fan D.S.P., Choy K.W.,
Pang C.P.;
"Truncations in the TIGR gene in individuals with and without primary
open-angle glaucoma.";
Invest. Ophthalmol. Vis. Sci. 41:1386-1391(2000).
[50]
VARIANT GLC1A ARG-433.
PubMed=10819638; DOI=10.1136/jmg.37.4.301;
Vasconcellos J.P.C., Melo M.B., Tsukumo D.M.L., Basseres D.S.,
Bordin S., Saad S.T.O., Costa F.F.;
"Novel mutation in the MYOC gene in primary open glaucoma patients.";
J. Med. Genet. 37:301-303(2000).
[51]
VARIANTS GLC1A LYS-261 AND GLU-337, AND VARIANT ARG-398.
PubMed=10916185; DOI=10.1076/1381-6810(200006)2121-8FT109;
Vazquez C.M., Herrero O.M.V., Bastus B.M., Perez V.D.;
"Mutations in the third exon of the MYOC gene in Spanish patients with
primary open angle glaucoma.";
Ophthalmic Genet. 21:109-115(2000).
[52]
VARIANTS GLC1A ARG-252; LYS-293; ARG-367; LEU-370; LYS-377; VAL-399
AND VAL-445, AND VARIANT ARG-398.
PubMed=11774072; DOI=10.1086/338709;
Vincent A.L., Billingsley G., Buys Y., Levin A.V., Priston M.,
Trope G., Williams-Lyn D., Heon E.;
"Digenic inheritance of early-onset glaucoma: CYP1B1, a potential
modifier gene.";
Am. J. Hum. Genet. 70:448-460(2002).
[53]
VARIANTS GLC1A TRP-126; LYS-293; LYS-352; ARG-367; GLU-423; THR-427;
VAL-445 AND LEU-481, AND VARIANTS LYS-76; GLU-77 AND ARG-398.
PubMed=12189160; DOI=10.1093/hmg/11.18.2077;
The Quebec glaucoma network;
Faucher M., Anctil J.-L., Rodrigue M.-A., Duchesne A., Bergeron D.,
Blondeau P., Cote G., Dubois S., Bergeron J., Arseneault R.,
Morissette J., Raymond V.;
"Founder TIGR/myocilin mutations for glaucoma in the Quebec
population.";
Hum. Mol. Genet. 11:2077-2090(2002).
[54]
VARIANTS GLC1A ALA-251; MET-345; ARG-367; LEU-370; ASN-393; SER-434;
ASP-450 AND CYS-470, AND VARIANT LYS-76.
PubMed=12442283; DOI=10.1002/humu.9092;
Michels-Rautenstrauss K., Mardin C., Wakili N., Juenemann A.M.,
Villalobos L., Mejia C., Soley G.C., Azofeifa J., Oezbey S.,
Naumann G.O.H., Reis A., Rautenstrauss B.;
"Novel mutations in the MYOC/GLC1A gene in a large group of glaucoma
patients.";
Hum. Mutat. 20:479-480(2002).
[55]
VARIANTS GLC1A LYS-300 AND CYS-471, AND VARIANTS ARG-12; LEU-16;
SER-17; LYS-76; PRO-95; GLU-208; PRO-215; ILE-353 AND LYS-414.
PubMed=12356829;
Pang C.P., Leung Y.F., Fan B., Baum L., Tong W.C., Lee W.S.,
Chua J.K.H., Fan D.S.P., Liu Y., Lam D.S.C.;
"TIGR/MYOC gene sequence alterations in individuals with and without
primary open-angle glaucoma.";
Invest. Ophthalmol. Vis. Sci. 43:3231-3235(2002).
[56]
VARIANTS GLC1A LYS-342 AND ASN-380.
PubMed=12362081; DOI=10.1097/00061198-200210000-00008;
Challa P., Herndon L.W., Hauser M.A., Broomer B.W.,
Pericak-Vance M.A., Ababio-Danso B., Allingham R.R.;
"Prevalence of myocilin mutations in adults with primary open-angle
glaucoma in Ghana, West Africa.";
J. Glaucoma 11:416-420(2002).
[57]
VARIANTS GLC1A ARG-25 AND GLU-423.
PubMed=12860809; DOI=10.1001/archopht.121.7.1034;
Bruttini M., Longo I., Frezzotti P., Ciappetta R., Randazzo A.,
Orzalesi N., Fumagalli E., Caporossi A., Frezzotti R., Renieri A.;
"Mutations in the myocilin gene in families with primary open-angle
glaucoma and juvenile open-angle glaucoma.";
Arch. Ophthalmol. 121:1034-1038(2003).
[58]
VARIANTS GLC1A ARG-367; ILE-438; LYS-480 AND PHE-499, AND VARIANTS
SER-57; LYS-76 AND ARG-398.
PubMed=12872267; DOI=10.1002/humu.9165;
Melki R., Belmouden A., Brezin A., Garchon H.-J.;
"Myocilin analysis by DHPLC in French POAG patients: increased
prevalence of Q368X mutation.";
Hum. Mutat. 22:179-179(2003).
[59]
VARIANT GLC1A HIS-48, AND VARIANT LYS-76.
PubMed=15025728; DOI=10.1111/j.1399-0004.2004.00232.x;
Sripriya S., Uthra S., Sangeetha R., George R.J., Hemamalini A.,
Paul P.G., Amali J., Vijaya L., Kumaramanickavel G.;
"Low frequency of myocilin mutations in Indian primary open-angle
glaucoma patients.";
Clin. Genet. 65:333-337(2004).
[60]
VARIANTS GLC1A ASN-360; THR-363; LEU-369 AND PRO-448.
PubMed=15534471; DOI=10.1097/0.ijg.0000138204.6d;
Ishikawa K., Funayama T., Ohtake Y., Tanino T., Kurosaka D.,
Suzuki K., Ideta H., Fujimaki T., Tanihara H., Asaoka R., Naoi N.,
Yasuda N., Iwata T., Mashima Y.;
"Novel MYOC gene mutation, Phe369Leu, in Japanese patients with
primary open-angle glaucoma detected by denaturing high-performance
liquid chromatography.";
J. Glaucoma 13:466-471(2004).
[61]
VARIANT GLC1A ARG-274.
PubMed=15255110; DOI=10.1076/opge.25.1.11.28995;
Markandaya M., Ramesh T.K., Selvaraju V., Dorairaj S.K., Prakash R.,
Shetty J., Kumar A.;
"Genetic analysis of an Indian family with members affected with
juvenile-onset primary open-angle glaucoma.";
Ophthalmic Genet. 25:11-23(2004).
[62]
VARIANT GLC3A HIS-48.
PubMed=15733270; DOI=10.1111/j.1399-0004.2005.00411.x;
Kaur K., Reddy A.B.M., Mukhopadhyay A., Mandal A.K., Hasnain S.E.,
Ray K., Thomas R., Balasubramanian D., Chakrabarti S.;
"Myocilin gene implicated in primary congenital glaucoma.";
Clin. Genet. 67:335-340(2005).
[63]
VARIANT GLC1A TYR-245, AND CHARACTERIZATION OF VARIANT GLC1A TYR-245.
PubMed=16401791; DOI=10.1001/archopht.124.1.102;
Fan B.J., Leung D.Y.L., Wang D.Y., Gobeil S., Raymond V., Tam P.O.S.,
Lam D.S.C., Pang C.P.;
"Novel myocilin mutation in a Chinese family with juvenile-onset open-
angle glaucoma.";
Arch. Ophthalmol. 124:102-106(2006).
[64]
VARIANT GLC1A HIS-380.
PubMed=17499207; DOI=10.1016/j.ajo.2007.03.037;
Wirtz M.K., Samples J.R., Choi D., Gaudette N.D.;
"Clinical features associated with an Asp380His Myocilin mutation in a
US family with primary open-angle glaucoma.";
Am. J. Ophthalmol. 144:75-80(2007).
[65]
VARIANTS GLC1A VAL-244 AND ARG-252.
PubMed=17210859; DOI=10.1001/archopht.125.1.98;
Hewitt A.W., Bennett S.L., Richards J.E., Dimasi D.P., Booth A.P.,
Inglehearn C., Anwar R., Yamamoto T., Fingert J.H., Heon E.,
Craig J.E., Mackey D.A.;
"Myocilin Gly252Arg mutation and glaucoma of intermediate severity in
Caucasian individuals.";
Arch. Ophthalmol. 125:98-104(2007).
-!- 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}.
-!- SUBUNIT: Homodimer (via N-terminus). Can also form higher
oligomers (PubMed:9497363). Interacts with OLFM3, FN1, NRCAM, GLDN
and NFASC (PubMed:12019210, PubMed:11773026, PubMed:23897819).
Interacts (via N-terminus) with MYL2 (PubMed:11773029). Interacts
with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt
signaling (PubMed:19188438). Interacts with SNTA1; regulates
muscle hypertrophy. Interacts with ERBB2 and ERBB3; acivates
ERBB2-ERBB3 signaling pathway. Interacts with SNCG; affects its
secretion and its aggregation (By similarity).
{ECO:0000250|UniProtKB:O70624, ECO:0000269|PubMed:11773026,
ECO:0000269|PubMed:11773029, ECO:0000269|PubMed:12019210,
ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:23897819,
ECO:0000269|PubMed:9497363}.
-!- INTERACTION:
P10916:MYL2; NbExp=7; IntAct=EBI-11692272, EBI-725770;
P09486:SPARC; NbExp=3; IntAct=EBI-11692272, EBI-2800983;
Q14515:SPARCL1; NbExp=2; IntAct=EBI-11692272, EBI-2682673;
-!- 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, 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.
-!- TISSUE SPECIFICITY: Detected in aqueous humor (PubMed:12697062).
Detected in the eye (at protein level) (PubMed:11431441). Widely
expressed. Highly expressed in various types of muscle, ciliary
body, papillary sphincter, skeletal muscle, heart, and bone
marrow-derived mesenchymal stem cells. Expressed predominantly in
the retina. In normal eyes, found in the inner uveal meshwork
region and the anterior portion of the meshwork. In contrast, in
many glaucomatous eyes, it is found in more regions of the
meshwork and seems to be expressed at higher levels than in normal
eyes, regardless of the type or clinical severity of glaucoma. The
myocilin 35 kDa fragment is detected in aqueous humor and to a
lesser extent in iris and ciliary body.
{ECO:0000269|PubMed:11431441, ECO:0000269|PubMed:12697062,
ECO:0000269|PubMed:15795224}.
-!- INDUCTION: Up-regulated by dexamethasone, a glucocorticoid.
{ECO:0000269|PubMed:11431441, ECO:0000269|PubMed:9497363}.
-!- 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}.
-!- 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 mutations 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
mutations 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}.
-!- SEQUENCE CAUTION:
Sequence=BAA24532.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF001620; AAC51725.1; -; mRNA.
EMBL; D88214; BAA23531.1; -; mRNA.
EMBL; Z97171; CAB09899.1; -; Genomic_DNA.
EMBL; Z97177; CAB09899.1; JOINED; Genomic_DNA.
EMBL; Z97174; CAB09899.1; JOINED; Genomic_DNA.
EMBL; U85257; AAC52051.1; -; mRNA.
EMBL; AB006688; BAA24532.1; ALT_INIT; Genomic_DNA.
EMBL; AF049793; AAC14264.1; -; Genomic_DNA.
EMBL; AF049791; AAC14264.1; JOINED; Genomic_DNA.
EMBL; AF049792; AAC14264.1; JOINED; Genomic_DNA.
EMBL; AK315443; BAG37831.1; -; mRNA.
EMBL; Z98750; CAD92590.2; -; Genomic_DNA.
EMBL; CH471067; EAW90903.1; -; Genomic_DNA.
EMBL; BC029261; AAH29261.1; -; mRNA.
CCDS; CCDS1297.1; -.
PIR; JC5830; JC5830.
RefSeq; NP_000252.1; NM_000261.1.
UniGene; Hs.436037; -.
PDB; 4WXQ; X-ray; 2.15 A; A=228-504.
PDB; 4WXS; X-ray; 1.90 A; A=228-504.
PDB; 4WXU; X-ray; 2.09 A; A=228-504.
PDBsum; 4WXQ; -.
PDBsum; 4WXS; -.
PDBsum; 4WXU; -.
ProteinModelPortal; Q99972; -.
SMR; Q99972; -.
BioGrid; 110736; 43.
IntAct; Q99972; 3.
STRING; 9606.ENSP00000037502; -.
iPTMnet; Q99972; -.
PhosphoSitePlus; Q99972; -.
BioMuta; MYOC; -.
DMDM; 3024209; -.
EPD; Q99972; -.
PaxDb; Q99972; -.
PeptideAtlas; Q99972; -.
PRIDE; Q99972; -.
DNASU; 4653; -.
Ensembl; ENST00000037502; ENSP00000037502; ENSG00000034971.
GeneID; 4653; -.
KEGG; hsa:4653; -.
UCSC; uc001ghu.4; human.
CTD; 4653; -.
DisGeNET; 4653; -.
EuPathDB; HostDB:ENSG00000034971.14; -.
GeneCards; MYOC; -.
HGNC; HGNC:7610; MYOC.
HPA; HPA027364; -.
MalaCards; MYOC; -.
MIM; 137750; phenotype.
MIM; 231300; phenotype.
MIM; 601652; gene.
neXtProt; NX_Q99972; -.
OpenTargets; ENSG00000034971; -.
Orphanet; 98976; Congenital glaucoma.
Orphanet; 98977; Juvenile glaucoma.
PharmGKB; PA31415; -.
eggNOG; ENOG410INPA; Eukaryota.
eggNOG; ENOG410YBJJ; LUCA.
GeneTree; ENSGT00760000119005; -.
HOGENOM; HOG000059654; -.
HOVERGEN; HBG105662; -.
InParanoid; Q99972; -.
OMA; RYKYSSM; -.
OrthoDB; EOG091G05HN; -.
PhylomeDB; Q99972; -.
TreeFam; TF315964; -.
GeneWiki; MYOC; -.
GenomeRNAi; 4653; -.
PRO; PR:Q99972; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000034971; -.
CleanEx; HS_MYOC; -.
ExpressionAtlas; Q99972; baseline and differential.
Genevisible; Q99972; HS.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0033268; C:node of Ranvier; ISS:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB.
GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032027; F:myosin light chain binding; IPI:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:UniProtKB.
GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISS:UniProtKB.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IMP:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0014734; P:skeletal muscle hypertrophy; ISS:UniProtKB.
InterPro; IPR031213; Myocilin.
InterPro; IPR003112; Olfac-like_dom.
PANTHER; PTHR23192:SF33; PTHR23192:SF33; 1.
Pfam; PF02191; OLF; 1.
SMART; SM00284; OLF; 1.
PROSITE; PS51132; OLF; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell projection; Cilium; Coiled coil;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
Disease mutation; Disulfide bond; Endoplasmic reticulum;
Extracellular matrix; Glaucoma; Glycoprotein; Golgi apparatus;
Lipoprotein; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Mitochondrion outer membrane; Palmitate;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 32 {ECO:0000269|PubMed:19287508,
ECO:0000269|PubMed:9497363}.
CHAIN 33 504 Myocilin.
/FTId=PRO_0000020084.
CHAIN 33 226 Myocilin, N-terminal fragment.
/FTId=PRO_0000428749.
CHAIN 227 504 Myocilin, C-terminal fragment.
/FTId=PRO_0000428750.
DOMAIN 244 503 Olfactomedin-like. {ECO:0000255|PROSITE-
ProRule:PRU00446}.
COILED 74 184 {ECO:0000255}.
MOTIF 502 504 Microbody targeting signal.
{ECO:0000255}.
METAL 380 380 Calcium. {ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU}.
METAL 428 428 Calcium. {ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU}.
METAL 429 429 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU}.
METAL 477 477 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU}.
METAL 478 478 Calcium. {ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU}.
SITE 226 227 Cleavage; by CAPN2.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:17650508}.
DISULFID 245 433 {ECO:0000244|PDB:4WXQ,
ECO:0000244|PDB:4WXS,
ECO:0000244|PDB:4WXU,
ECO:0000255|PROSITE-ProRule:PRU00446,
ECO:0000269|PubMed:12615070}.
VARIANT 4 4 F -> S.
/FTId=VAR_009665.
VARIANT 9 9 C -> S.
/FTId=VAR_009666.
VARIANT 12 12 G -> R (in dbSNP:rs199752860).
{ECO:0000269|PubMed:10798654,
ECO:0000269|PubMed:12356829}.
/FTId=VAR_009667.
VARIANT 16 16 P -> L (in dbSNP:rs745439002).
{ECO:0000269|PubMed:12356829}.
/FTId=VAR_054269.
VARIANT 17 17 A -> S. {ECO:0000269|PubMed:12356829}.
/FTId=VAR_054270.
VARIANT 19 19 Q -> H (in dbSNP:rs2234925).
{ECO:0000269|PubMed:10980537}.
/FTId=VAR_009668.
VARIANT 25 25 C -> R (in GLC1A; dbSNP:rs755246983).
{ECO:0000269|PubMed:12860809}.
/FTId=VAR_054271.
VARIANT 48 48 Q -> H (in GLC1A and GLC3A; the GLC3A
patient also carries mutation H-368 in
CYP1B1 suggesting digenic inheritance;
dbSNP:rs74315339).
{ECO:0000269|PubMed:15025728,
ECO:0000269|PubMed:15733270}.
/FTId=VAR_054272.
VARIANT 53 53 V -> A (in GLC1A; dbSNP:rs200208925).
{ECO:0000269|PubMed:10644174}.
/FTId=VAR_008969.
VARIANT 57 57 N -> D. {ECO:0000269|PubMed:11004290}.
/FTId=VAR_054273.
VARIANT 57 57 N -> S (loss of higher molecular weight
isoform; dbSNP:rs561439247).
{ECO:0000269|PubMed:12697062,
ECO:0000269|PubMed:12872267}.
/FTId=VAR_054274.
VARIANT 73 73 N -> S.
/FTId=VAR_009669.
VARIANT 76 76 R -> K (in dbSNP:rs2234926).
{ECO:0000269|PubMed:10798654,
ECO:0000269|PubMed:10980537,
ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:12356829,
ECO:0000269|PubMed:12442283,
ECO:0000269|PubMed:12872267,
ECO:0000269|PubMed:15025728,
ECO:0000269|PubMed:9863594}.
/FTId=VAR_009670.
VARIANT 77 77 D -> E. {ECO:0000269|PubMed:12189160}.
/FTId=VAR_054275.
VARIANT 82 82 R -> C (in GLC1A; dbSNP:rs764005392).
/FTId=VAR_009671.
VARIANT 82 82 R -> H (in dbSNP:rs201552559).
/FTId=VAR_009672.
VARIANT 95 95 L -> P. {ECO:0000269|PubMed:12356829}.
/FTId=VAR_054276.
VARIANT 126 126 R -> W (in GLC1A; dbSNP:rs200120115).
{ECO:0000269|PubMed:12189160}.
/FTId=VAR_054277.
VARIANT 158 158 R -> Q (in GLC1A; dbSNP:rs199746824).
{ECO:0000269|PubMed:10980537}.
/FTId=VAR_054278.
VARIANT 189 189 R -> Q (in dbSNP:rs144579767).
/FTId=VAR_009673.
VARIANT 203 203 S -> F.
/FTId=VAR_009674.
VARIANT 208 208 D -> E (in GLC1A; unknown pathological
significance; dbSNP:rs2234927).
{ECO:0000269|PubMed:10798654,
ECO:0000269|PubMed:10980537,
ECO:0000269|PubMed:12356829}.
/FTId=VAR_014943.
VARIANT 215 215 L -> P (in dbSNP:rs531050114).
{ECO:0000269|PubMed:12356829}.
/FTId=VAR_054279.
VARIANT 244 244 G -> V (in GLC1A; unknown pathological
significance; dbSNP:rs757769997).
{ECO:0000269|PubMed:17210859}.
/FTId=VAR_054280.
VARIANT 245 245 C -> Y (in GLC1A; forms homomultimeric
complexes that migrate at molecular
weights larger than their wild-type
counterparts; these mutant complexes
remain sequestered intracellularly;
dbSNP:rs74315340).
{ECO:0000269|PubMed:16401791}.
/FTId=VAR_054281.
VARIANT 246 246 G -> R (in GLC1A).
{ECO:0000269|PubMed:9328473}.
/FTId=VAR_005468.
VARIANT 251 251 V -> A (in GLC1A).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_054282.
VARIANT 252 252 G -> R (in GLC1A; dbSNP:rs74315341).
{ECO:0000269|PubMed:10873982,
ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:17210859}.
/FTId=VAR_054283.
VARIANT 261 261 E -> K (in GLC1A).
{ECO:0000269|PubMed:10916185}.
/FTId=VAR_054284.
VARIANT 272 272 R -> G (in GLC1A; unknown pathological
significance).
{ECO:0000269|PubMed:11004290}.
/FTId=VAR_054285.
VARIANT 274 274 P -> R (in GLC1A).
{ECO:0000269|PubMed:15255110}.
/FTId=VAR_054286.
VARIANT 286 286 W -> R (in GLC1A).
/FTId=VAR_009675.
VARIANT 293 293 T -> K (in GLC1A; no effect on protein
stability; dbSNP:rs139122673).
{ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:25524706}.
/FTId=VAR_009676.
VARIANT 300 300 E -> K (in GLC1A; unknown pathological
significance; dbSNP:rs748621461).
{ECO:0000269|PubMed:12356829}.
/FTId=VAR_054287.
VARIANT 323 323 E -> K (in GLC1A; inhibits
endoproteolytic processing; mainly
accumulates as insoluble aggregates
inside the endoplasmic reticulum).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:15795224}.
/FTId=VAR_054288.
VARIANT 329 329 V -> M (slightly decreased protein
stability; dbSNP:rs146391864).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:25524706}.
/FTId=VAR_009677.
VARIANT 337 337 Q -> E (in GLC1A).
{ECO:0000269|PubMed:10916185}.
/FTId=VAR_054289.
VARIANT 337 337 Q -> R (in GLC1A; dbSNP:rs74315335).
{ECO:0000269|PubMed:9361308}.
/FTId=VAR_005469.
VARIANT 341 341 S -> P (in GLC1A).
{ECO:0000269|PubMed:9510647}.
/FTId=VAR_054290.
VARIANT 342 342 R -> K (in GLC1A).
{ECO:0000269|PubMed:12362081}.
/FTId=VAR_054291.
VARIANT 345 345 I -> M (in GLC1A).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_054292.
VARIANT 352 352 E -> K (in GLC1A; unknown pathological
significance; dbSNP:rs61745146).
{ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:9792882}.
/FTId=VAR_009678.
VARIANT 353 353 T -> I (in GLC1A; unknown pathological
significance; no significant effect on
protein stability; dbSNP:rs137853277).
{ECO:0000269|PubMed:10330365,
ECO:0000269|PubMed:10798654,
ECO:0000269|PubMed:12356829,
ECO:0000269|PubMed:25524706}.
/FTId=VAR_009679.
VARIANT 360 360 I -> N (in GLC1A).
{ECO:0000269|PubMed:10980537,
ECO:0000269|PubMed:15534471}.
/FTId=VAR_054293.
VARIANT 361 361 P -> S (in GLC1A).
/FTId=VAR_009680.
VARIANT 363 363 A -> T (in GLC1A).
{ECO:0000269|PubMed:10980537,
ECO:0000269|PubMed:15534471}.
/FTId=VAR_054294.
VARIANT 364 364 G -> V (in GLC1A; dbSNP:rs121909193).
{ECO:0000269|PubMed:9005853}.
/FTId=VAR_005470.
VARIANT 367 367 G -> R (in GLC1A; dbSNP:rs74315334).
{ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:12442283,
ECO:0000269|PubMed:12872267,
ECO:0000269|PubMed:9345106,
ECO:0000269|PubMed:9490287,
ECO:0000269|PubMed:9521427}.
/FTId=VAR_005471.
VARIANT 369 369 F -> L (in GLC1A).
{ECO:0000269|PubMed:15534471}.
/FTId=VAR_054295.
VARIANT 370 370 P -> L (in GLC1A; severe form; inhibits
endoproteolytic processing; produced the
highest inhibition of the endoproteolytic
processing; mainly accumulates as
insoluble aggregates inside the
endoplasmic reticulum; inhibits neurite
outgrowth; dbSNP:rs74315330).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:12442283,
ECO:0000269|PubMed:15795224,
ECO:0000269|PubMed:9328473,
ECO:0000269|PubMed:9345106,
ECO:0000269|PubMed:9490287,
ECO:0000269|PubMed:9792882,
ECO:0000269|PubMed:9863594}.
/FTId=VAR_005472.
VARIANT 377 377 T -> K (in GLC1A).
{ECO:0000269|PubMed:11774072}.
/FTId=VAR_054296.
VARIANT 377 377 T -> M (in GLC1A; dbSNP:rs566289099).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:9792882}.
/FTId=VAR_009681.
VARIANT 380 380 D -> A (in GLC1A; incomplete penetrance;
inhibits endoproteolytic processing;
mainly accumulates as insoluble
aggregates inside the endoplasmic
reticulum). {ECO:0000269|PubMed:9863594}.
/FTId=VAR_009682.
VARIANT 380 380 D -> G (in GLC1A).
{ECO:0000269|PubMed:15795224}.
/FTId=VAR_009683.
VARIANT 380 380 D -> H (in GLC1A; dbSNP:rs121909194).
{ECO:0000269|PubMed:17499207}.
/FTId=VAR_054297.
VARIANT 380 380 D -> N (in GLC1A).
{ECO:0000269|PubMed:12362081}.
/FTId=VAR_054298.
VARIANT 393 393 S -> N (in GLC1A).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_054299.
VARIANT 393 393 S -> R (in GLC1A).
/FTId=VAR_009684.
VARIANT 398 398 K -> R (in dbSNP:rs56314834).
{ECO:0000269|PubMed:10916185,
ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:12872267}.
/FTId=VAR_009685.
VARIANT 399 399 G -> V (in GLC1A; dbSNP:rs28936694).
{ECO:0000269|PubMed:11774072}.
/FTId=VAR_054300.
VARIANT 402 402 V -> I.
/FTId=VAR_009686.
VARIANT 414 414 E -> K. {ECO:0000269|PubMed:12356829}.
/FTId=VAR_054301.
VARIANT 422 422 R -> C (no effect on protein stability;
dbSNP:rs751113505).
{ECO:0000269|PubMed:25524706}.
/FTId=VAR_009687.
VARIANT 422 422 R -> H (in GLC1A; dbSNP:rs201573718).
/FTId=VAR_009688.
VARIANT 423 423 K -> E (in GLC1A; heterozygote specific
phenotype; dbSNP:rs74315336).
{ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:12860809,
ECO:0000269|PubMed:9697688}.
/FTId=VAR_009689.
VARIANT 425 425 S -> P (decreases protein stability).
{ECO:0000269|PubMed:25524706}.
/FTId=VAR_009690.
VARIANT 426 426 V -> F (in GLC1A).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:9521427}.
/FTId=VAR_005473.
VARIANT 427 427 A -> T (in GLC1A; dbSNP:rs754237376).
{ECO:0000269|PubMed:12189160}.
/FTId=VAR_054302.
VARIANT 433 433 C -> R (in GLC1A; severe form;
dbSNP:rs74315338).
{ECO:0000269|PubMed:10819638}.
/FTId=VAR_008970.
VARIANT 434 434 G -> S (in GLC1A).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_054303.
VARIANT 437 437 Y -> H (in GLC1A; dbSNP:rs74315328).
{ECO:0000269|PubMed:9005853,
ECO:0000269|PubMed:9792882}.
/FTId=VAR_005474.
VARIANT 438 438 T -> I (in GLC1A).
{ECO:0000269|PubMed:12872267}.
/FTId=VAR_054304.
VARIANT 445 445 A -> V (in GLC1A; no effect on protein
stability; dbSNP:rs140967767).
{ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:12189160,
ECO:0000269|PubMed:25524706}.
/FTId=VAR_009691.
VARIANT 448 448 T -> P (in GLC1A).
{ECO:0000269|PubMed:10340788,
ECO:0000269|PubMed:15534471}.
/FTId=VAR_054305.
VARIANT 450 450 N -> D (in GLC1A).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_054306.
VARIANT 465 465 I -> M (in GLC1A).
/FTId=VAR_009692.
VARIANT 470 470 R -> C (in GLC1A; dbSNP:rs771122834).
{ECO:0000269|PubMed:12442283}.
/FTId=VAR_009693.
VARIANT 470 470 R -> H (in dbSNP:rs750791099).
{ECO:0000269|PubMed:10980537}.
/FTId=VAR_054307.
VARIANT 471 471 Y -> C (in GLC1A; unknown pathological
significance; dbSNP:rs554235897).
{ECO:0000269|PubMed:12356829}.
/FTId=VAR_054308.
VARIANT 473 473 Y -> C (no effect on protein stability).
{ECO:0000269|PubMed:25524706}.
/FTId=VAR_009694.
VARIANT 477 477 I -> N (in GLC1A; induces stress fiber
formation in only 5% of cells;
dbSNP:rs74315331).
{ECO:0000269|PubMed:11004290,
ECO:0000269|PubMed:19188438}.
/FTId=VAR_009695.
VARIANT 477 477 I -> S (in GLC1A; dbSNP:rs74315331).
{ECO:0000269|PubMed:9328473}.
/FTId=VAR_005475.
VARIANT 480 480 N -> K (in GLC1A; dbSNP:rs74315332).
{ECO:0000269|PubMed:12872267,
ECO:0000269|PubMed:9328473}.
/FTId=VAR_005476.
VARIANT 481 481 P -> L (in GLC1A).
{ECO:0000269|PubMed:12189160}.
/FTId=VAR_009696.
VARIANT 481 481 P -> T (in GLC1A).
/FTId=VAR_009697.
VARIANT 495 495 V -> I.
/FTId=VAR_009698.
VARIANT 499 499 I -> F (in GLC1A).
{ECO:0000269|PubMed:12872267,
ECO:0000269|PubMed:9328473}.
/FTId=VAR_005477.
VARIANT 499 499 I -> S (in GLC1A).
{ECO:0000269|PubMed:11004290}.
/FTId=VAR_054309.
VARIANT 500 500 K -> R (in dbSNP:rs145977437).
/FTId=VAR_009699.
VARIANT 502 502 S -> P (in GLC1A).
{ECO:0000269|PubMed:9863594}.
/FTId=VAR_009700.
MUTAGEN 226 230 Missing: Impairs endoproteolytic
processing.
{ECO:0000269|PubMed:17650508}.
MUTAGEN 226 226 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.
{ECO:0000269|PubMed:17650508}.
MUTAGEN 226 226 R->Q: Slightly increases endoproteolytic
processing.
{ECO:0000269|PubMed:17650508}.
MUTAGEN 227 227 I->G: Reduced processing.
{ECO:0000269|PubMed:17650508}.
MUTAGEN 229 229 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. {ECO:0000269|PubMed:17650508}.
MUTAGEN 230 230 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.
{ECO:0000269|PubMed:17650508}.
STRAND 248 251 {ECO:0000244|PDB:4WXS}.
STRAND 255 259 {ECO:0000244|PDB:4WXS}.
HELIX 263 265 {ECO:0000244|PDB:4WXS}.
STRAND 266 272 {ECO:0000244|PDB:4WXS}.
STRAND 285 289 {ECO:0000244|PDB:4WXS}.
STRAND 292 303 {ECO:0000244|PDB:4WXS}.
HELIX 304 309 {ECO:0000244|PDB:4WXS}.
STRAND 313 322 {ECO:0000244|PDB:4WXS}.
STRAND 328 330 {ECO:0000244|PDB:4WXS}.
STRAND 333 338 {ECO:0000244|PDB:4WXS}.
STRAND 341 348 {ECO:0000244|PDB:4WXS}.
TURN 349 352 {ECO:0000244|PDB:4WXS}.
STRAND 353 359 {ECO:0000244|PDB:4WXS}.
STRAND 366 369 {ECO:0000244|PDB:4WXS}.
TURN 375 378 {ECO:0000244|PDB:4WXU}.
STRAND 380 384 {ECO:0000244|PDB:4WXS}.
STRAND 387 392 {ECO:0000244|PDB:4WXS}.
TURN 395 399 {ECO:0000244|PDB:4WXS}.
STRAND 400 406 {ECO:0000244|PDB:4WXS}.
TURN 408 410 {ECO:0000244|PDB:4WXS}.
STRAND 413 422 {ECO:0000244|PDB:4WXS}.
HELIX 423 425 {ECO:0000244|PDB:4WXS}.
STRAND 426 432 {ECO:0000244|PDB:4WXS}.
STRAND 435 454 {ECO:0000244|PDB:4WXS}.
TURN 455 457 {ECO:0000244|PDB:4WXS}.
STRAND 460 468 {ECO:0000244|PDB:4WXS}.
STRAND 474 480 {ECO:0000244|PDB:4WXS}.
TURN 481 484 {ECO:0000244|PDB:4WXS}.
STRAND 485 490 {ECO:0000244|PDB:4WXS}.
STRAND 493 497 {ECO:0000244|PDB:4WXS}.
STRAND 499 501 {ECO:0000244|PDB:4WXS}.
SEQUENCE 504 AA; 56972 MW; 9588C04F1D227623 CRC64;
MRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT FSVASPNESS
CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QETQEGLQRE
LGTLRRERDQ LETQTRELET AYSNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL
RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE
GDTGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE
YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI
PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPEN LELEQTWETN
IRKQSVANAF IICGTLYTVS SYTSADATVN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN
PLEKKLFAWD NLNMVTYDIK LSKM


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MYOD1 MYOC Gene myocilin, trabecular meshwork inducible glucocorticoid response
201-20-3602 MYOC{myocilin, trabecular meshwork inducible glucocorticoid response}rabbit.pAb 0.2ml
GWB-BB1B9C Myocilin Trabecular Meshwork Inducible Glucocorticoid Response Rabbit anti-Human Polyclonal (aa69-85) Antibody
CSB-EL015356DO Dog myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL015356RA Rat myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL015356CA Cat myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Cat, Sample Type serum, plasma 96T
CSB-EL015356BO Bovine myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL015356MO Mouse myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL015356HU Human myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015356RB Rabbit myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-PA015356GA01HU Rabbit anti-human myocilin, trabecular meshwork inducible glucocorticoid response polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA015356GA01HU Rabbit anti-human myocilin, trabecular meshwork inducible glucocorticoid response polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
13090-H08H MYOC _ Myocilin Protein (His Tag) 20
49-806 Myocilin Antibody 0.05 mg
C491 Myocilin 500
C491 Myocilin lmg
E0260d Rat ELISA Kit FOR Myocilin 96T
PC-Myo Myocilin Antibody, WB control 100-150ul
YF-MA14364 anti-Myocilin (2B4) 100 ug
CH087_HUMAN Rat ELISA Kit FOR Myocilin 96T


 

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