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Protein

Myocilin

Gene

Myoc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. 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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi378 – 3781CalciumBy similarity
Metal bindingi426 – 4261CalciumBy similarity
Metal bindingi427 – 4271Calcium; via carbonyl oxygenBy similarity
Metal bindingi475 – 4751Calcium; via carbonyl oxygenBy similarity
Metal bindingi476 – 4761CalciumBy 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620430. Myoc.

Subcellular locationi

  • Secreted By similarity
  • Golgi apparatus By similarity
  • 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 By similarity
  • 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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131By similarityAdd
BLAST
Chaini32 – 502471MyocilinPRO_0000020088Add
BLAST
Chaini32 – 225194Myocilin, N-terminal fragmentBy similarityPRO_0000428747Add
BLAST
Chaini226 – 502277Myocilin, C-terminal fragmentBy similarityPRO_0000428748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi243 ↔ 431PROSITE-ProRule annotationBy similarity

Post-translational modificationi

Palmitoylated.By similarity
Undergoes a calcium-dependent proteolytic cleavage at Gln-225 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
Sitei225 – 2262Cleavage; by CAPN2By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ9R1J4.
PRIDEiQ9R1J4.

PTM databases

iPTMnetiQ9R1J4.
PhosphoSiteiQ9R1J4.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle and retina. Also detected at lower levels in thyroid gland but not in other endocrine glands such as the adrenal or pituitary glands.1 Publication

Inductioni

Up-regulated by dexamethasone.1 Publication

Interactioni

Subunit structurei

Homodimer (via N-terminus). Can also form higher oligomers. 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 (By similarity). 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).By similarity

Protein-protein interaction databases

IntActiQ9R1J4. 1 interaction.
STRINGi10116.ENSRNOP00000004386.

Structurei

3D structure databases

ProteinModelPortaliQ9R1J4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini242 – 501260Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili82 – 183102Sequence 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.
InParanoidiQ9R1J4.
PhylomeDBiQ9R1J4.

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.

Q9R1J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSCAYCCSC GPKMPALQLL FLACLVWGMG ARTAQFRKAN DRSGRCQYTF
60 70 80 90 100
TVASPSESSC PREDQAMSAI QDLQRDSSIQ HADLESTKAR VRSLESLLHQ
110 120 130 140 150
MTSGGVTGTQ EVQEGLQGQL GALRRERDQL ETQTRDLEVA YNNLLRDKSA
160 170 180 190 200
LEEEKRQLEQ ENKDLARRLE GSSQEVARLR RGQCPSTHHP SQDMLPGSRE
210 220 230 240 250
VSQWNLDTLA FQELKSELTE VPASQILKNQ SGHPRSKEGD KGCGVLMWVG
260 270 280 290 300
EPVTLRTAET ITGKYGVWMR DPKPTHPYTQ ETTWRIDTVG TGIRQVFEYS
310 320 330 340 350
QISQFEQGYP SKVHVLPQAL ESTGAVVYSG SLYFQGAESR TVLRYELNTE
360 370 380 390 400
TVKAEKEIPG AGYHGQFPYA WGGYTDIDLA VDESGLWVIY STEETRGAIV
410 420 430 440 450
LSKLNPENLE LESTWETNIR KQSVANAFVI CGILYTVSSY SSVHATINFA
460 470 480 490 500
YDTNTGISKT LTIPFKNRYK YSSMVDYNPL ERKLFAWDNF NMVTYDIKLS

EM
Length:502
Mass (Da):56,442
Last modified:May 1, 2000 - v1
Checksum:i2FE8FBE53CF48BBA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Y → R in BAA34199 (PubMed:10833334).Curated
Sequence conflicti329 – 3291S → A in BAA34199 (PubMed:10833334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093567 mRNA. Translation: AAD46401.1.
AB019393 mRNA. Translation: BAA34199.1.
RefSeqiNP_110492.1. NM_030865.1.
UniGeneiRn.30051.

Genome annotation databases

GeneIDi81523.
KEGGirno:81523.
UCSCiRGD:620430. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093567 mRNA. Translation: AAD46401.1.
AB019393 mRNA. Translation: BAA34199.1.
RefSeqiNP_110492.1. NM_030865.1.
UniGeneiRn.30051.

3D structure databases

ProteinModelPortaliQ9R1J4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R1J4. 1 interaction.
STRINGi10116.ENSRNOP00000004386.

PTM databases

iPTMnetiQ9R1J4.
PhosphoSiteiQ9R1J4.

Proteomic databases

PaxDbiQ9R1J4.
PRIDEiQ9R1J4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81523.
KEGGirno:81523.
UCSCiRGD:620430. rat.

Organism-specific databases

CTDi4653.
RGDi620430. Myoc.

Phylogenomic databases

eggNOGiENOG410INPA. Eukaryota.
ENOG410YBJJ. LUCA.
HOGENOMiHOG000059654.
HOVERGENiHBG105662.
InParanoidiQ9R1J4.
PhylomeDBiQ9R1J4.

Miscellaneous databases

PROiQ9R1J4.

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...

Entry informationi

Entry nameiMYOC_RAT
AccessioniPrimary (citable) accession number: Q9R1J4
Secondary accession number(s): Q9Z2Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 97 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. 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.