Home Page for Recoverin

Recoverin

Primary information about recoverin:
Basic chemical and physical information	Basic biological information	Basic genomic information	Metal ion binding constants	Interspecies sequence alignment	Information on function
Summary of structural studies	Information on the conformational change	List of available structures	Information about mutations	References about recoverin	Other web resources about recoverin

Basic Information

Basic Chemical and Physical Information:
Additional names and abbreviations:	recoverin: S-modulin (the frog homolog); p26
Isoforms:	No information about isoforms is stored in the database
Yeast Protein Database Entries:	No links to the YPD are stored in the database

Number of amino acids:	199 (Homo sapiens) - 201 (Bos taurus, Mus musculus, Rana catesbeiana) View a list of all sources stored in the database
Molecular weight:	22.999 kD (Homo sapiens) - 23.396 kD (Rana catesbeiana) View a list of all sources stored in the database
pI:	calculated pI (Bos taurus) = 5.2 (InfoCard)
Number of functional calcium binding sites:	not yet available in the data library
Macroscopic calcium binding constants:	not yet available in the data library
Other metal binding constants:	not yet available in the data library
Protein stability:	not yet available in the data library
Post-translational modifications:	Bos taurus: myristoylation on N-terminus ( effect: is required for cooperativity in calcium binding) (InfoCard)

Basic Biological Information:
Source organisms:	Bos taurus, Homo sapiens, Mus musculus, Rana catesbeiana View an annotated list of all sources stored in the database
Tissues:	not yet available in the data library
Subcellular localization:	not yet available in the data library
Regulation:	not yet available in the data library

Genomic Information:
GenBank entries:	not yet available in the data library
Gene length:	not yet available in the data library
Gene structure:	not yet available in the data library
Promoter:	not yet available in the data library
Gene copies:	not yet available in the data library
Alleles:	no alleles are currently stored in the data library
Chromosomal localization:	not yet available in the data library

Interspecies Sequence Alignment



                                     |helixI-|--loop1----|helixII|
                                     En**nn**nX*Y*ZG#Ix**zn**nn*n

BOVINE  :  GNSKSGALSKEILEELQLNTKFTEEELSSWYQSFLKECPSGRITRQEFQTIYSKFFPEA
MOUSE   :  GNSKSGALSKEILEELQLNTKFTEEELSAWYQSFLKECPSGRITRQEFESIYSKFFPDS
HUMAN   :  GNSKSGALSKEILEELQLNTKFSEEELCSWYQSFLKDCPTGRITQQQFQSIYAKFFPDT
RANCA   :  GNTKSGALSKEILEELQLNTKFTQEELCTWYQSFLKECPSGRISKKQFESIYSKFFPDA

             |helixIII|--loop2----|helixIV|       |-helixV-|--loop3----|
              En**nn**nX*Y*ZG#Ix**zn**nn*n         En**nn**nX*Y*ZG#Ix**z

BOVINE  :  DPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTSAGKTNQKLEWAFSLYDVDGNGTISKNE
MOUSE   :  DPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTTAGKPTQKLEWAFSLYDVDGNGTISKNE
HUMAN   :  DPKAYAQHVFRSFDSNLDGTLDFKEYVIALHMTTAGKTNQKLEWAFSLYDVDGNGTISKNE
RANCA   :  DPKAYAQHVFRSFDANNDGTLDFKEYMIALMMTSSGKANQKLEWAFCLYDVDGNGTINKKE

           helixVI|                  |-helixVII|--loop4----|helixVIII|
           n**nn*n                    En**nn**nX*Y*ZG#Ix**zn**nn*n

BOVINE  :  VLEIVTAIFKMISPEDTKHLPEDENTPEKRAEKIWGFFGKKDDDKLTEKEFIEGTLANK
MOUSE   :  VLEIVMAIFKMIKPEDVKLLPDDENTPEKRAEKIWAFFGKKEDDKLTEEEFIEGTLANK
HUMAN   :  VLEIVMAIFKMITPEDVKLLPDDENTPEKRAEKIWKYFGKNDDDKLTEKEFIEGTLANK
RANCA   :  VLEIITAIFKMINAEDQKHLPEDENTPEKRTNKIWVYFGKKDDDKLTEGEFIQGIVKNK

BOVINE  :  EILRLIQFEPQKVKEKLKEKKL
MOUSE   :  EILRLIQFEPQKVKERIKEKKQ
HUMAN   :  EILRLIQFEPQKVKEKMKNA--
RANCA   :  EILRLIQYEPQKVKDKLKEKKH

the RANCA form of recoverin is usually called S-modulin

Sequence alignment of the entire neuronal calcium sensors subfamily

Functional Information:

General information:

no general functional information is currently stored in the database

Biological roles:

photoresponse in eye: calcium-loaded recoverin seems to prolong this process by inhibiting phosphorylation of rhodopsin by rhodopsin kinase
biochemical evidence in Bos taurus: Inhibition of rhodopsin phosphorylation by calcium-loaded recoverin is seen both cell homogenates and reconstituted systems (InfoCard)
biochemical evidence in Xenopus laevis: Inhibition of rhodopsin phosphorylation by calcium-loaded recoverin is seen both cell homogenates and reconstituted systems (InfoCard)

Disease states:

not yet available in the data library

Target molecules:

rhodopsin kinase
biochemical evidence for interaction in Bos taurus: Recoverin binds to rhodopsin kinase in a calcium-dependent manner (InfoCard)
effect of interaction in Bos taurus: Recoverin binding inhibits the activity of rhodopsin kinase in a calcium-dependent manner (InfoCard)

Structural Information:

Calcium-coordination:
not yet available in the data library

Nature of the conformational changes:
Conformational change between apo and two calcium ions bound states:	Calcium-binding leads to the exposure of the covalently attached myristoyl group to solvent. This is accomplished by rotation of a "hinge" at Gly42, which moves helix I of the first EF_hand, pulling the N-terminal helix away from the rest of the protein, and exposing the myristoyl group. (InfoCard)

Secondary structure: (as reported in the PDB file and its accompanying reference)
not yet available in the data library

Additional structural information:
View a table of interhelical angles from various structures View a table of hydrogen bonds observed in various structures

Available structures: (follow the links from the PDB code to the retrieve the PDB files)
Apo Structures:	1IKU: Bos taurus, full length protein, NMR solution structure, 24 models, 14.34 restraints per residue (InfoCard)
Calcium Loaded Structures:	1JSA: Bos taurus, full length protein, pH 7 NMR solution structure, 24 models, 12.9 restraints per residue 2 Ca ions bound (InfoCard)
Partially Saturated Structures:	1REC: Bos taurus, full length protein, Crystal structure, 1.9 angstrom resolution, R-value = 19.1 1 Ca ion bound (InfoCard)

Information about mutants:

no mutants are currently stored in the database