Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myocilin

Gene

Myoc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling (PubMed:23629661). Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling (PubMed:23897819). Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex (PubMed:22371502). 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 (By similarity).By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi366 – 3661CalciumBy similarity
Metal bindingi414 – 4141CalciumBy similarity
Metal bindingi415 – 4151Calcium; via carbonyl oxygenBy similarity
Metal bindingi463 – 4631Calcium; via carbonyl oxygenBy similarity
Metal bindingi464 – 4641CalciumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myocilin
Alternative name(s):
Trabecular meshwork-induced glucocorticoid response protein
Cleaved into the following 2 chains:
Alternative name(s):
Myocilin 20 kDa N-terminal fragment
Alternative name(s):
Myocilin 35 kDa N-terminal fragment
Gene namesi
Name:Myoc
Synonyms:Tigr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1202864. Myoc.

Subcellular locationi

  • Secreted 1 Publication
  • Golgi apparatus 1 Publication
  • Cytoplasmic vesicle By similarity
  • Secretedextracellular space By similarity
  • Secretedextracellular spaceextracellular matrix By similarity
  • Secretedexosome By similarity
  • Mitochondrion By similarity
  • Mitochondrion intermembrane space By similarity
  • Mitochondrion inner membrane By similarity
  • Mitochondrion outer membrane By similarity
  • Rough endoplasmic reticulum 1 Publication
  • Cell projection By similarity
  • Cell projectioncilium By similarity

  • Note: Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum. It is only imported to mitochondria in the trabecular meshwork. Localizes to the Golgi apparatus in Schlemm's canal endothelial cells. Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles. Localizes in trabecular meshwork extracellular matrix.By similarity
Myocilin, N-terminal fragment :

GO - Cellular componenti

  • cilium Source: UniProtKB-SubCell
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • node of Ranvier Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • rough endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasmic vesicle, Endoplasmic reticulum, Extracellular matrix, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice lacking Myoc are viable, fertile and show no significant differences in intraocular pressure or clinical signs of glaucoma. They also show a reduction in cortical bone thickness as well as trabecular volume.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 490472MyocilinPRO_0000020086Add
BLAST
Chaini19 – 212194Myocilin, N-terminal fragmentBy similarityPRO_0000428743Add
BLAST
Chaini213 – 490278Myocilin, C-terminal fragmentBy similarityPRO_0000428744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi231 ↔ 419PROSITE-ProRule annotationBy similarity

Post-translational modificationi

Palmitoylated.By similarity
Undergoes a calcium-dependent proteolytic cleavage at Gln-212 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 (By similarity).By similarity
Glycosylated.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei212 – 2132Cleavage; by CAPN2By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiO70624.
PRIDEiO70624.

PTM databases

PhosphoSiteiO70624.

Expressioni

Tissue specificityi

Expressed in ciliary body, iris, retina, trabecular network and sclera but not in lens or cornea. Also expressed strongly in skeletal muscle and weakly in heart, brain, testis, liver, kidney, thyroid and epididymis. No expression detected in embryo. Expressed in sciatic nerve.4 Publications

Gene expression databases

BgeeiO70624.
CleanExiMM_MYOC.
ExpressionAtlasiO70624. baseline and differential.
GenevisibleiO70624. MM.

Interactioni

Subunit structurei

Homodimer (via N-terminus). Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC. Interacts (via N-terminus) with MYL2. Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates Wnt signaling. Interacts with SNTA1; regulates muscle hypertrophy (PubMed:22371502). Interacts with ERBB2 and ERBB3; acivates ERBB2-ERBB3 signaling pathway (PubMed:23897819). Interacts with SNCG; affects its secretion and its aggregation (PubMed:16392033).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028020.

Structurei

3D structure databases

ProteinModelPortaliO70624.
SMRiO70624. Positions 230-487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini230 – 489260Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili69 – 170102Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG410INPA. Eukaryota.
ENOG410YBJJ. LUCA.
HOGENOMiHOG000059654.
HOVERGENiHBG105662.
InParanoidiO70624.
OMAiRYKYSSM.
OrthoDBiEOG75F4CZ.
PhylomeDBiO70624.
TreeFamiTF315964.

Family and domain databases

InterProiIPR031213. Myocilin.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF33. PTHR23192:SF33. 1 hit.
PfamiPF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70624-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALHLLFLA CLVWGMGART AQFRKANDRS GRCQYTFTVA SPNESSCPRE
60 70 80 90 100
DQAMSAIQDL QRDSSIQHAD LESTKARVRS LESLLHQMTL GRVTGTQEAQ
110 120 130 140 150
EGLQGQLGAL RRERDQLETQ TRDLEAAYNN LLRDKSALEE EKRQLEQENE
160 170 180 190 200
DLARRLESSS EEVTRLRRGQ CPSTQYPSQD MLPGSREVSQ WNLDTLAFQE
210 220 230 240 250
LKSELTEVPA SQILKENPSG RPRSKEGDKG CGALVWVGEP VTLRTAETIA
260 270 280 290 300
GKYGVWMRDP KPTHPYTQES TWRIDTVGTE IRQVFEYSQI SQFEQGYPSK
310 320 330 340 350
VHVLPRALES TGAVVYAGSL YFQGAESRTV VRYELDTETV KAEKEIPGAG
360 370 380 390 400
YHGHFPYAWG GYTDIDLAVD ESGLWVIYST EEAKGAIVLS KLNPANLELE
410 420 430 440 450
RTWETNIRKQ SVANAFVICG ILYTVSSYSS AHATVNFAYD TKTGTSKTLT
460 470 480 490
IPFTNRYKYS SMIDYNPLER KLFAWDNFNM VTYDIKLLEM
Length:490
Mass (Da):55,314
Last modified:August 1, 1998 - v1
Checksum:i2F090571E97B0425
GO

Polymorphismi

Variant Ala-164 is found in strain BALB/cJ which has a low intraocular pressure (PubMed:9588210, PubMed:9675094). Variant Thr-164 is found in strains C3H/HeJ and C57BL/6J, two strains which have a relatively high intraocular pressure (PubMed:9588210, PubMed:9548973, PubMed:9680392).4 Publications

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641T → A in strain: BALB/cJ. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041335, AF041333, AF041334 Genomic DNA. Translation: AAC32805.1.
AF049796, AF049795, AF049794 Genomic DNA. Translation: AAC14265.1.
AF039869 mRNA. Translation: AAC40112.1.
AB013592 mRNA. Translation: BAA32031.1.
CCDSiCCDS15422.1.
PIRiJE0096.
RefSeqiNP_034995.3. NM_010865.3.
UniGeneiMm.10694.

Genome annotation databases

EnsembliENSMUST00000028020; ENSMUSP00000028020; ENSMUSG00000026697.
GeneIDi17926.
KEGGimmu:17926.
UCSCiuc007dgm.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041335, AF041333, AF041334 Genomic DNA. Translation: AAC32805.1.
AF049796, AF049795, AF049794 Genomic DNA. Translation: AAC14265.1.
AF039869 mRNA. Translation: AAC40112.1.
AB013592 mRNA. Translation: BAA32031.1.
CCDSiCCDS15422.1.
PIRiJE0096.
RefSeqiNP_034995.3. NM_010865.3.
UniGeneiMm.10694.

3D structure databases

ProteinModelPortaliO70624.
SMRiO70624. Positions 230-487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028020.

PTM databases

PhosphoSiteiO70624.

Proteomic databases

PaxDbiO70624.
PRIDEiO70624.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028020; ENSMUSP00000028020; ENSMUSG00000026697.
GeneIDi17926.
KEGGimmu:17926.
UCSCiuc007dgm.2. mouse.

Organism-specific databases

CTDi4653.
MGIiMGI:1202864. Myoc.

Phylogenomic databases

eggNOGiENOG410INPA. Eukaryota.
ENOG410YBJJ. LUCA.
HOGENOMiHOG000059654.
HOVERGENiHBG105662.
InParanoidiO70624.
OMAiRYKYSSM.
OrthoDBiEOG75F4CZ.
PhylomeDBiO70624.
TreeFamiTF315964.

Miscellaneous databases

PROiO70624.
SOURCEiSearch...

Gene expression databases

BgeeiO70624.
CleanExiMM_MYOC.
ExpressionAtlasiO70624. baseline and differential.
GenevisibleiO70624. MM.

Family and domain databases

InterProiIPR031213. Myocilin.
IPR003112. Olfac-like_dom.
[Graphical view]
PANTHERiPTHR23192:SF33. PTHR23192:SF33. 1 hit.
PfamiPF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ALA-164.
    Strain: BALB/cJ, C3H/HeJ and C57BL/6J.
    Tissue: Brain and Muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ALA-164.
    Strain: BALB/cJ.
    Tissue: Skeletal muscle.
  3. "Characterization and comparison of the human and mouse GLC1A glaucoma genes."
    Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C., Alward W.L.M., Sheffield V.C., Stone E.M.
    Genome Res. 8:377-384(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/Sv.
  5. "Optimedin: a novel olfactomedin-related protein that interacts with myocilin."
    Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.
    Hum. Mol. Genet. 11:1291-1301(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OLFM3.
  6. "Interaction of myocilin with gamma-synuclein affects its secretion and aggregation."
    Surgucheva I., Park B.C., Yue B.Y., Tomarev S., Surguchov A.
    Cell. Mol. Neurobiol. 25:1009-1033(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNCG, SUBCELLULAR LOCATION.
  7. Cited for: INTERACTION WITH FRZB AND SFRP1.
  8. "Myocilin interacts with syntrophins and is member of dystrophin-associated protein complex."
    Joe M.K., Kee C., Tomarev S.I.
    J. Biol. Chem. 287:13216-13227(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MUSCLE HYPERTROPHY, INTERACTION WITH SNTA1.
  9. "Myocilin stimulates osteogenic differentiation of mesenchymal stem cells through mitogen-activated protein kinase signaling."
    Kwon H.S., Johnson T.V., Tomarev S.I.
    J. Biol. Chem. 288:16882-16894(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BONE FORMATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  10. "Myocilin mediates myelination in the peripheral nervous system through ErbB2/3 signaling."
    Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C., Tomarev S.I.
    J. Biol. Chem. 288:26357-26371(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MYELINATION, INTERACTION WITH NFASC; GLDN; NRCAM; ERBB2 AND ERBB3, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMYOC_MOUSE
AccessioniPrimary (citable) accession number: O70624
Secondary accession number(s): O70289
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.