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P31227 (SMOD_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-modulin
Alternative name(s):
Sensitivity-modulating protein
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent regulator of light sensitivity of cGMP phosphodiesterase in rod outer segments. Control rhodopsin phosphorylation in a Ca2+-dependent manner.

Subcellular location

Note: The binding target of the Ca2+/S-modulin complex is possibly ROS membrane lipid(s).

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the recoverin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMLipoprotein
Myristate
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processresponse to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 202201S-modulin
PRO_0000073799

Regions

Domain25 – 6036EF-hand 1
Domain61 – 9636EF-hand 2
Domain97 – 13236EF-hand 3
Domain147 – 18236EF-hand 4
Calcium binding74 – 85121 Potential
Calcium binding110 – 121122 Potential

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity

Experimental info

Sequence conflict911M → H in BAA19728. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31227 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 5FFE379649904A2B

FASTA20223,527
        10         20         30         40         50         60 
MGNTKSGALS KEILEELQLN TKFTQEELCT WYQSFLKECP SGRISKKQFE SIYSKFFPDA 

        70         80         90        100        110        120 
DPKAYAQHVF RSFDANNDGT LDFKEYMIAL MMTSSGKANQ KLEWAFCLYD VDGNGTINKK 

       130        140        150        160        170        180 
EVLEIITAIF KMINAEDQKH LPEDENTPEK RTNKIWVYFG KKDDDKLTEG EFIQGIVKNK 

       190        200 
EILRLIQYEP QKVKDKLKEK KH 

« Hide

References

[1]"Recoverin has S-modulin activity in frog rods."
Kawamura S., Hisatomi O., Kayada S., Tokunaga F., Kuo C.-H.
J. Biol. Chem. 268:14579-14582(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Purification and characterization of S-modulin, a calcium-dependent regulator on cGMP phosphodiesterase in frog rod photoreceptors."
Kawamura S., Takamatsu K., Kitamura K.
Biochem. Biophys. Res. Commun. 186:411-417(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-28; 47-55; 63-97; 131-150; 154-162; 167-177 AND 180-192.
Tissue: Retina.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83641 mRNA. Translation: BAA19728.1.
PIRJC1107.
T10531.

3D structure databases

ProteinModelPortalP31227.
SMRP31227. Positions 2-191.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG108179.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin_like.
[Graphical view]
PfamPF13202. EF-hand_5. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
PRINTSPR00450. RECOVERIN.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSMOD_LITCT
AccessionPrimary (citable) accession number: P31227
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 78 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families