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Database: UniProt/TrEMBL
Entry: H2N4Q4_PONAB
LinkDB: H2N4Q4_PONAB
Original site: H2N4Q4_PONAB 
ID   H2N4Q4_PONAB            Unreviewed;       504 AA.
AC   H2N4Q4; A0A2J8UBR4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Myocilin {ECO:0000256|ARBA:ARBA00017216};
DE   AltName: Full=Trabecular meshwork-induced glucocorticoid response protein {ECO:0000256|ARBA:ARBA00033004};
GN   Name=MYOC {ECO:0000313|Ensembl:ENSPPYP00000000593.3};
GN   ORFNames=CR201_G0028905 {ECO:0000313|EMBL:PNJ42716.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000000593.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000000593.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ42716.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ42716.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000000593.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004294}. Rough endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004427}. Secreted, extracellular exosome
CC       {ECO:0000256|ARBA:ARBA00004550}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000256|ARBA:ARBA00004498}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00446}.
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DR   EMBL; NDHI03003464; PNJ42716.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000000593; -.
DR   Ensembl; ENSPPYT00000000618.3; ENSPPYP00000000593.3; ENSPPYG00000000512.3.
DR   eggNOG; KOG3545; Eukaryota.
DR   GeneTree; ENSGT00940000158561; -.
DR   HOGENOM; CLU_035236_4_0_1; -.
DR   OMA; REVSKWN; -.
DR   OrthoDB; 2876896at2759; -.
DR   TreeFam; TF315964; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR   GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032027; F:myosin light chain binding; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   GO; GO:0045162; P:clustering of voltage-gated sodium channels; IEA:Ensembl.
DR   GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IEA:Ensembl.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0035567; P:non-canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0014734; P:skeletal muscle hypertrophy; IEA:Ensembl.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR23192:SF33; MYOCILIN; 1.
DR   PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1.
DR   Pfam; PF02191; OLF; 1.
DR   SMART; SM00284; OLF; 1.
DR   PROSITE; PS51132; OLF; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..504
FT                   /note="Myocilin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041198908"
FT   DOMAIN          244..503
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   REGION          106..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  57077 MW;  1FA04BC5552CF397 CRC64;
     PRFFCARCCS FGPEMPAVQL LLLACLVWDV GARTAQLRKA NDQSGRCQYT FSVVSPNESS
     CPEQSQAMSV IRNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QDTQEGLQRE
     LGTLRRERDQ LETQTRELET AYNNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL
     RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSKLT EVPASRILKE SPSGYLRSRE
     GDNGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE
     YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI
     PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPDN LELEQTWETN
     IRKQSVANAF IICGTLYTVS SYSSADATIN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN
     PLEKKLFAWD NLNMVTYDIK LSKI
//
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