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Myocilin [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)]

 MYOC_CANLF              Reviewed;         483 AA.
Q2PT31; Q3Y9M0;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
28-MAR-2018, entry version 81.
RecName: Full=Myocilin;
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;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, AND
PALMITOYLATION.
STRAIN=Beagle; TISSUE=Trabecular meshwork;
PubMed=17149370;
Ricard C.S., Mukherjee A., Silver F.-L., Wagenknecht P.L.;
"Canine myocilin is associated with lipid modified by palmitic acid.";
Mol. Vis. 12:1427-1436(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle; TISSUE=Trabecular meshwork;
PubMed=17973835; DOI=10.1111/j.1463-5224.2007.00530.x;
Kato K., Sasaki N., Matsunaga S., Nishimura R., Ogawa H.;
"Cloning of canine myocilin cDNA and molecular analysis of the
myocilin gene in Shiba Inu dogs.";
Vet. Ophthalmol. 10:53-62(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:0000250|UniProtKB:Q99972}.
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:O70624,
ECO:0000250|UniProtKB:Q99972}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99972}.
Golgi apparatus {ECO:0000250|UniProtKB:Q99972}. Cytoplasmic
vesicle {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular
space {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular
space, extracellular matrix {ECO:0000250|UniProtKB:Q99972}.
Secreted, exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum
{ECO:0000250|UniProtKB:Q99972}. Cell projection
{ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q99972}. 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. {ECO:0000250|UniProtKB:Q99972}.
-!- SUBCELLULAR LOCATION: Myocilin, C-terminal fragment: Secreted
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Myocilin, N-terminal fragment: Endoplasmic
reticulum. Note=Remains retained in the endoplasmic reticulum.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in optic nerve head, ciliary body
and retina. {ECO:0000269|PubMed:17149370}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:17149370}.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:17149370}.
-!- PTM: Undergoes a calcium-dependent proteolytic cleavage at Arg-205
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). {ECO:0000250}.
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EMBL; DQ149972; AAZ78213.1; -; mRNA.
EMBL; DQ303878; ABC17625.2; -; mRNA.
RefSeq; NP_001041495.2; NM_001048030.3.
UniGene; Cfa.13102; -.
SMR; Q2PT31; -.
STRING; 9615.ENSCAFP00000021988; -.
PaxDb; Q2PT31; -.
PRIDE; Q2PT31; -.
Ensembl; ENSCAFT00000023685; ENSCAFP00000021988; ENSCAFG00000014924.
GeneID; 490344; -.
KEGG; cfa:490344; -.
CTD; 4653; -.
VGNC; VGNC:43576; MYOC.
eggNOG; ENOG410INPA; Eukaryota.
eggNOG; ENOG410YBJJ; LUCA.
GeneTree; ENSGT00760000119005; -.
HOGENOM; HOG000059654; -.
HOVERGEN; HBG105662; -.
InParanoid; Q2PT31; -.
OMA; RYKYSSM; -.
OrthoDB; EOG091G05HN; -.
TreeFam; TF315964; -.
Proteomes; UP000002254; Chromosome 7.
Bgee; ENSCAFG00000014924; -.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; ISS: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; IEA:Ensembl.
GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032027; F:myosin light chain binding; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; ISS: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;
Calcium; Cell projection; Cilium; Coiled coil; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum;
Extracellular matrix; Glycoprotein; Golgi apparatus; Lipoprotein;
Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Palmitate; Reference proteome; Secreted;
Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 483 Myocilin.
/FTId=PRO_0000232718.
CHAIN 19 205 Myocilin, N-terminal fragment.
{ECO:0000250}.
/FTId=PRO_0000428737.
CHAIN 206 483 Myocilin, C-terminal fragment.
{ECO:0000250}.
/FTId=PRO_0000428738.
DOMAIN 223 482 Olfactomedin-like. {ECO:0000255|PROSITE-
ProRule:PRU00446}.
COILED 51 162 {ECO:0000255}.
MOTIF 481 483 Microbody targeting signal.
{ECO:0000255}.
METAL 359 359 Calcium. {ECO:0000250|UniProtKB:Q99972}.
METAL 407 407 Calcium. {ECO:0000250|UniProtKB:Q99972}.
METAL 408 408 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q99972}.
METAL 456 456 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q99972}.
METAL 457 457 Calcium. {ECO:0000250|UniProtKB:Q99972}.
SITE 205 206 Cleavage; by CAPN2. {ECO:0000250}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 224 412 {ECO:0000250|UniProtKB:Q99972,
ECO:0000255|PROSITE-ProRule:PRU00446}.
SEQUENCE 483 AA; 54262 MW; DB8BA5467D4C6E6A CRC64;
MPTAQLLLLA CLLWGLEART AQLRKANDRS GRCQYIFSVA SPNESSCPEQ GQAMSAIQDL
QRDLESTKAR LSSLEGLLHQ LTLGQAAGPS ESQEGLHREL GTLRKEREQL ETQARELEVA
YSNLLRDKSA LEEEKRRLGE ENEDLAQRLE HSSQEVARLR RGQCPQAHSS SQDVPAGSRE
VSKWNVETVN FQELKSELTE VPASRILKES PSGHPRNEEG DSGCGELVWV GEPLTLRTAE
TITGKYGVWM RDPKPTYPHT RETTWRIDTV GTDIRQVFEY ELASQFLQGY PSKVHVLPRP
LESTGAVVYR GSLYFQGAGS GTVVRYELTA ETVKAEREIP GAGYHGQFPY SWGGYTDIDL
AVDETGLWVI YSTQEAKGAI VLSKLNPETL ELEQTWETNI RKQSVANAFV ICGHLYTISS
YSSPDATVNF AYDTGTGRSR VLSIPFKNRY KYSSMIDYNP LEKKLFAWDN FNMVTYDIRL
SKM


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