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Protein Page:
RS1 (human)

Overview
RS1 a highly conserved extracellular protein essential for proper retinal structure. Must interact with L-type voltage-gated calcium channels (L-VGCCs) correctly so that the photoreceptor cells in the eye can function properly. Genetic mutations in RS1 cause X-linked retinoschisis (XLRS) and early onset of macular degeneration. Interacts with the L-VGCCa1D subunit, regulating its activity. The expression and secretion of retinoschisin are modulated by circadian rhythms, peaking at night and diminishing during the day. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: Xp22.13
Cellular Component: extracellular space; extrinsic to plasma membrane
Molecular Function: phosphatidylinositol 3-phosphate binding; phosphatidylinositol-3,4,5-triphosphate binding; phosphatidylinositol-3,4-bisphosphate binding; phosphatidylinositol-4,5-bisphosphate binding; phosphatidylinositol-5-phosphate binding; phosphatidylserine binding
Biological Process: adaptation of rhodopsin mediated signaling; cell adhesion; multicellular organismal development; visual perception
Disease: Retinoschisis 1, X-linked, Juvenile
Reference #:  O15537 (UniProtKB)
Alt. Names/Synonyms: Retinoschisin; retinoschisin 1; retinoschisis (X-linked, juvenile) 1; RS; RS1; X-linked juvenile retinoschisis protein; XLRS1
Gene Symbols: RS1
Molecular weight: 25,592 Da
Basal Isoelectric point: 5.51  Predict pI for various phosphorylation states
Select Structure to View Below

RS1

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S105‑p ANKARLNsQGFGCAW
0 1 S114‑p GFGCAWLsKFQDsSQ
0 1 S119‑p WLsKFQDsSQWLQID
0 1 Y177‑p TGNNRVFyGNSDRtS
0 1 T183‑p FyGNSDRtSTVQNLL
  mouse

 
S105 ANKARLNSQGFGCAW
S114 GFGCAWLSKYQDSSQ
S119 WLSKYQDSSQWLQID
Y177 TGNNRVFYGNSDRSS
S183 FYGNSDRSSTVQNLL
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