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MYOC_RAT
ID   MYOC_RAT                Reviewed;         502 AA.
AC   Q9R1J4; Q9Z2Y4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Myocilin;
DE   AltName: Full=Trabecular meshwork-induced glucocorticoid response protein;
DE   Contains:
DE     RecName: Full=Myocilin, N-terminal fragment;
DE     AltName: Full=Myocilin 20 kDa N-terminal fragment;
DE   Contains:
DE     RecName: Full=Myocilin, C-terminal fragment;
DE     AltName: Full=Myocilin 35 kDa N-terminal fragment;
DE   Flags: Precursor;
GN   Name=Myoc; Synonyms=Tigr;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Eye;
RX   PubMed=10833334; DOI=10.1006/mgme.2000.2986;
RA   Taguchi M., Kanno H., Kubota R., Miwa S., Shishiba Y., Ozawa Y.;
RT   "Molecular cloning and expression profile of rat myocilin.";
RL   Mol. Genet. Metab. 70:75-80(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar Kyoto; TISSUE=Eye;
RA   Yaoeda K., Yamamoto T., Funaki H., Koyama Y., Nihei K., Tani T., Yaoita E.,
RA   Kawasaki K., Abe H., Kihara I.;
RT   "Molecular cloning of myocilin gene from rat eye.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION.
RX   PubMed=23629661; DOI=10.1074/jbc.m112.422972;
RA   Kwon H.S., Johnson T.V., Tomarev S.I.;
RT   "Myocilin stimulates osteogenic differentiation of mesenchymal stem cells
RT   through mitogen-activated protein kinase signaling.";
RL   J. Biol. Chem. 288:16882-16894(2013).
CC   -!- FUNCTION: Secreted glycoprotein regulating the activation of different
CC       signaling pathways in adjacent cells to control different processes
CC       including cell adhesion, cell-matrix adhesion, cytoskeleton
CC       organization and cell migration. Promotes substrate adhesion, spreading
CC       and formation of focal contacts. Negatively regulates cell-matrix
CC       adhesion and stress fiber assembly through Rho protein signal
CC       transduction. Modulates the organization of actin cytoskeleton by
CC       stimulating the formation of stress fibers through interactions with
CC       components of Wnt signaling pathways. Promotes cell migration through
CC       activation of PTK2 and the downstream phosphatidylinositol 3-kinase
CC       signaling. Plays a role in bone formation and promotes osteoblast
CC       differentiation in a dose-dependent manner through mitogen-activated
CC       protein kinase signaling. Mediates myelination in the peripheral
CC       nervous system through ERBB2/ERBB3 signaling. Plays a role as a
CC       regulator of muscle hypertrophy through the components of dystrophin-
CC       associated protein complex. Involved in positive regulation of
CC       mitochondrial depolarization. Plays a role in neurite outgrowth. May
CC       participate in the obstruction of fluid outflow in the trabecular
CC       meshwork. {ECO:0000250|UniProtKB:O70624, ECO:0000250|UniProtKB:Q99972}.
CC   -!- SUBUNIT: Homodimer (via N-terminus). Can also form higher oligomers.
CC       Interacts with OLFM3, FN1, NRCAM, GLDN and NFASC. Interacts (via N-
CC       terminus) with MYL2. Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and
CC       WIF1; regulates Wnt signaling (By similarity). Interacts with SNTA1;
CC       regulates muscle hypertrophy. Interacts with ERBB2 and ERBB3; activates
CC       ERBB2-ERBB3 signaling pathway. Interacts with SNCG; affects its
CC       secretion and its aggregation (By similarity).
CC       {ECO:0000250|UniProtKB:O70624, ECO:0000250|UniProtKB:Q99972}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99972}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q99972}. Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted,
CC       extracellular exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q99972}. Cell projection
CC       {ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q99972}. Note=Located preferentially in the
CC       ciliary rootlet and basal body of the connecting cilium of
CC       photoreceptor cells, and in the rough endoplasmic reticulum. It is only
CC       imported to mitochondria in the trabecular meshwork. Localizes to the
CC       Golgi apparatus in Schlemm's canal endothelial cells. Appears in the
CC       extracellular space of trabecular meshwork cells by an unconventional
CC       mechanism, likely associated with exosome-like vesicles. Localizes in
CC       trabecular meshwork extracellular matrix.
CC       {ECO:0000250|UniProtKB:Q99972}.
CC   -!- SUBCELLULAR LOCATION: [Myocilin, C-terminal fragment]: Secreted
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Myocilin, N-terminal fragment]: Endoplasmic
CC       reticulum. Note=Remains retained in the endoplasmic reticulum.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and retina.
CC       Also detected at lower levels in thyroid gland but not in other
CC       endocrine glands such as the adrenal or pituitary glands.
CC       {ECO:0000269|PubMed:10833334}.
CC   -!- INDUCTION: Up-regulated by dexamethasone.
CC       {ECO:0000269|PubMed:23629661}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.
CC   -!- PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-225 by
CC       CAPN2 in the endoplasmic reticulum. The result is the production of two
CC       fragments, one of 35 kDa containing the C-terminal olfactomedin-like
CC       domain, and another of 20 kDa containing the N-terminal leucine zipper-
CC       like domain (By similarity). {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q99972}.
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DR   EMBL; AF093567; AAD46401.1; -; mRNA.
DR   EMBL; AB019393; BAA34199.1; -; mRNA.
DR   RefSeq; NP_110492.1; NM_030865.1.
DR   AlphaFoldDB; Q9R1J4; -.
DR   SMR; Q9R1J4; -.
DR   BioGRID; 249520; 1.
DR   IntAct; Q9R1J4; 1.
DR   STRING; 10116.ENSRNOP00000004386; -.
DR   GlyGen; Q9R1J4; 1 site.
DR   iPTMnet; Q9R1J4; -.
DR   PhosphoSitePlus; Q9R1J4; -.
DR   PaxDb; Q9R1J4; -.
DR   PRIDE; Q9R1J4; -.
DR   GeneID; 81523; -.
DR   KEGG; rno:81523; -.
DR   UCSC; RGD:620430; rat.
DR   CTD; 4653; -.
DR   RGD; 620430; Myoc.
DR   eggNOG; KOG3545; Eukaryota.
DR   InParanoid; Q9R1J4; -.
DR   OrthoDB; 421994at2759; -.
DR   PhylomeDB; Q9R1J4; -.
DR   PRO; PR:Q9R1J4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0097453; C:mesaxon; IDA:RGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0035748; C:myelin sheath abaxonal region; IDA:RGD.
DR   GO; GO:0033268; C:node of Ranvier; ISS:UniProtKB.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:RGD.
DR   GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR   GO; GO:0005109; F:frizzled binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032027; F:myosin light chain binding; ISO:RGD.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR   GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:UniProtKB.
DR   GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISS:UniProtKB.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
DR   GO; GO:0021675; P:nerve development; IEP:RGD.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISS:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0014734; P:skeletal muscle hypertrophy; ISS:UniProtKB.
DR   InterPro; IPR031213; Myocilin.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR23192:SF33; PTHR23192:SF33; 1.
DR   Pfam; PF02191; OLF; 1.
DR   SMART; SM00284; OLF; 1.
DR   PROSITE; PS51132; OLF; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell projection; Cilium; Coiled coil; Cytoplasmic vesicle;
KW   Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW   Golgi apparatus; Lipoprotein; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Mitochondrion outer membrane; Palmitate;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..502
FT                   /note="Myocilin"
FT                   /id="PRO_0000020088"
FT   CHAIN           32..225
FT                   /note="Myocilin, N-terminal fragment"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000428747"
FT   CHAIN           226..502
FT                   /note="Myocilin, C-terminal fragment"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000428748"
FT   DOMAIN          242..501
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   REGION          166..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          82..183
FT                   /evidence="ECO:0000255"
FT   BINDING         378
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q99972"
FT   BINDING         426
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q99972"
FT   BINDING         427
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q99972"
FT   BINDING         475
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q99972"
FT   BINDING         476
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q99972"
FT   SITE            225..226
FT                   /note="Cleavage; by CAPN2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        243..431
FT                   /evidence="ECO:0000250|UniProtKB:Q99972,
FT                   ECO:0000255|PROSITE-ProRule:PRU00446"
FT   CONFLICT        6
FT                   /note="Y -> R (in Ref. 1; BAA34199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="S -> A (in Ref. 1; BAA34199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  56442 MW;  2FE8FBE53CF48BBA CRC64;
     MPSCAYCCSC GPKMPALQLL FLACLVWGMG ARTAQFRKAN DRSGRCQYTF TVASPSESSC
     PREDQAMSAI QDLQRDSSIQ HADLESTKAR VRSLESLLHQ MTSGGVTGTQ EVQEGLQGQL
     GALRRERDQL ETQTRDLEVA YNNLLRDKSA LEEEKRQLEQ ENKDLARRLE GSSQEVARLR
     RGQCPSTHHP SQDMLPGSRE VSQWNLDTLA FQELKSELTE VPASQILKNQ SGHPRSKEGD
     KGCGVLMWVG EPVTLRTAET ITGKYGVWMR DPKPTHPYTQ ETTWRIDTVG TGIRQVFEYS
     QISQFEQGYP SKVHVLPQAL ESTGAVVYSG SLYFQGAESR TVLRYELNTE TVKAEKEIPG
     AGYHGQFPYA WGGYTDIDLA VDESGLWVIY STEETRGAIV LSKLNPENLE LESTWETNIR
     KQSVANAFVI CGILYTVSSY SSVHATINFA YDTNTGISKT LTIPFKNRYK YSSMVDYNPL
     ERKLFAWDNF NMVTYDIKLS EM
 
 
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