ONCO_MOUSE
ID ONCO_MOUSE Reviewed; 109 AA.
AC P51879; Q62004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Oncomodulin;
DE Short=OM;
DE AltName: Full=Parvalbumin beta;
GN Name=Ocm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1468649; DOI=10.1007/bf00133713;
RA Banville D., Rotaru M., Boie Y.;
RT "The intracisternal A particle derived solo LTR promoter of the rat
RT oncomodulin gene is not present in the mouse gene.";
RL Genetica 86:85-97(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=8597631; DOI=10.1007/bf00539001;
RA Staubli F., Klein A., Rentsch J., Hameister H., Berchtold M.W.;
RT "Structure and chromosomal localization of the mouse oncomodulin gene.";
RL Mamm. Genome 6:769-777(1995).
CC -!- FUNCTION: Has some calmodulin-like activity with respect to enzyme
CC activation and growth regulation. Binds two calcium ions.
CC -!- TISSUE SPECIFICITY: Found in tumor tissues and not detected in normal
CC tissues.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; S51661; AAB24617.1; -; Genomic_DNA.
DR EMBL; S51656; AAB24617.1; JOINED; Genomic_DNA.
DR EMBL; S51658; AAB24617.1; JOINED; Genomic_DNA.
DR EMBL; S51659; AAB24617.1; JOINED; Genomic_DNA.
DR EMBL; Z48237; CAA88274.1; -; Genomic_DNA.
DR EMBL; Z48238; CAA88275.1; -; Genomic_DNA.
DR CCDS; CCDS51693.1; -.
DR RefSeq; NP_149028.2; NM_033039.3.
DR AlphaFoldDB; P51879; -.
DR SMR; P51879; -.
DR STRING; 10090.ENSMUSP00000031622; -.
DR PhosphoSitePlus; P51879; -.
DR MaxQB; P51879; -.
DR PaxDb; P51879; -.
DR PeptideAtlas; P51879; -.
DR PRIDE; P51879; -.
DR ProteomicsDB; 294073; -.
DR DNASU; 18261; -.
DR Ensembl; ENSMUST00000031622; ENSMUSP00000031622; ENSMUSG00000029618.
DR Ensembl; ENSMUST00000085704; ENSMUSP00000082848; ENSMUSG00000029618.
DR GeneID; 18261; -.
DR KEGG; mmu:18261; -.
DR UCSC; uc029vqf.1; mouse.
DR CTD; 654231; -.
DR MGI; MGI:97401; Ocm.
DR VEuPathDB; HostDB:ENSMUSG00000029618; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000161875; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; P51879; -.
DR OMA; KKFFQVC; -.
DR OrthoDB; 1524081at2759; -.
DR PhylomeDB; P51879; -.
DR TreeFam; TF332342; -.
DR BioGRID-ORCS; 18261; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ocm; mouse.
DR PRO; PR:P51879; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P51879; protein.
DR Bgee; ENSMUSG00000029618; Expressed in ileum and 34 other tissues.
DR ExpressionAtlas; P51879; baseline and differential.
DR GO; GO:0032437; C:cuticular plate; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; ISO:MGI.
DR GO; GO:0099512; C:supramolecular fiber; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; ISO:MGI.
DR GO; GO:1905593; P:positive regulation of optical nerve axon regeneration; ISO:MGI.
DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; ISO:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008080; Parvalbumin.
DR PANTHER; PTHR11653; PTHR11653; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02631"
FT CHAIN 2..109
FT /note="Oncomodulin"
FT /id="PRO_0000073583"
FT DOMAIN 39..74
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..109
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 82..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0CE72,
FT ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02631"
SQ SEQUENCE 109 AA; 12260 MW; 1385D3846C33CE1B CRC64;
MSITDILSAD DIAAALQECQ DPDTFEPQKF FQTSGLSKMS ASQLKDIFQF IDNDQSGYLD
EDELKYFLQR FQSDARELTE SETKSLMDAA DNDGDGKIGA DEFQEMVHS
