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Reviewed, UniProtKB/Swiss-Prot P02631 (ONCO_RAT)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Oncomodulin
      Short name=OM
Alternative name(s):
    Parvalbumin beta
Gene names
Name: Ocm
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.

Tissue specificity

Found in tumor tissues and not detected in normal tissues.

Sequence similarities

Belongs to the parvalbumin family.

Contains 2 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 109108Oncomodulin
PRO_0000073584

Regions

Domain39 – 7436EF-hand 1
Domain78 – 10932EF-hand 2
Calcium binding52 – 63121 Ref.4
Calcium binding91 – 102122 Ref.4

Amino acid modifications

Modified residue21N-acetylserine Ref.3

Experimental info

Sequence conflict261E → Q AA sequence Ref.3

Secondary structure

...................... 109
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02631-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 89A168BD30748514

FASTA10912,188
        10         20         30         40         50         60 
MSITDILSAE DIAAALQECQ DPDTFEPQKF FQTSGLSKMS ASQVKDIFRF IDNDQSGYLD 

        70         80         90        100 
GDELKYFLQK FQSDARELTE SETKSLMDAA DNDGDGKIGA DEFQEMVHS 

« Hide

References

[1]"A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin."
Gillen M.F., Banville D., Rutledge R.G., Narang S., Seligy V.L., Whitfield J.F., McManus J.P.
J. Biol. Chem. 262:5308-5312(1987) [PubMed: 3558395] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Retroviral long terminal repeat is the promoter of the gene encoding the tumor-associated calcium-binding protein oncomodulin in the rat."
Banville D., Boie Y.
J. Mol. Biol. 207:481-490(1989) [PubMed: 2474657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Buffalo.
[3]"The complete amino acid sequence of oncomodulin -- a parvalbumin-like calcium-binding protein from Morris hepatoma 5123tc."
McManus J.P., Watson D.C., Yaguchi M.
Eur. J. Biochem. 136:9-17(1983) [PubMed: 6617664] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-109, ACETYLATION AT SER-2.
[4]"Oncomodulin. 1H NMR and optical stopped-flow spectroscopic studies of its solution conformation and metal-binding properties."
Williams T.C., Corson D.C., Sykes B.D., McManus J.P.
J. Biol. Chem. 262:6248-6256(1987) [PubMed: 3571255] [Abstract]
Cited for: CALCIUM-BINDING DATA.
[5]"Structure of oncomodulin refined at 1.85-A resolution. An example of extensive molecular aggregation via Ca2+."
Ahmed F.R., Przybylska M., Rose D.R., Birnbaum G.I., Pippy M.E., McManus J.P.
J. Mol. Biol. 216:127-140(1990) [PubMed: 2231727] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

J02705 mRNA. Translation: AAA41756.1.
X15836, X15837, X15838 Genomic DNA. Translation: CAA33840.1.
IPIIPI00363600.
PIRPVRTO. S04616.
RefSeqNP_037127.1.
UniGeneRn.9719

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OMDX-ray1.85A2-109[»]
1RROX-ray1.30A2-108[»]
2NLNNMR-A2-108[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000001031. Rattus norvegicus. [Contig view]
GeneID25503.
KEGGrno:25503.

Organism-specific databases

RGD3222. Ocm.

Phylogenomic databases

HOVERGENP02631.
OMAP02631. KDIFRFI.

Gene expression databases

ArrayExpressP02631.
GermOnlineENSRNOG00000001031. Rattus norvegicus.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR008080. Parvalbumin.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF00036. efhand. 2 hits.
[Graphical view]
PRINTSPR01697. PARVALBUMIN.
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio606913.

Entry information

Entry nameONCO_RAT
AccessionPrimary (citable) accession number: P02631
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents