ONCO_RAT
ID ONCO_RAT Reviewed; 109 AA.
AC P02631;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Oncomodulin;
DE Short=OM;
DE AltName: Full=Parvalbumin beta;
GN Name=Ocm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3558395; DOI=10.1016/s0021-9258(18)61189-5;
RA Gillen M.F., Banville D., Rutledge R.G., Narang S., Seligy V.L.,
RA Whitfield J.F., McManus J.P.;
RT "A complete complementary DNA for the oncodevelopmental calcium-binding
RT protein, oncomodulin.";
RL J. Biol. Chem. 262:5308-5312(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Buffalo;
RX PubMed=2474657; DOI=10.1016/0022-2836(89)90458-0;
RA Banville D., Boie Y.;
RT "Retroviral long terminal repeat is the promoter of the gene encoding the
RT tumor-associated calcium-binding protein oncomodulin in the rat.";
RL J. Mol. Biol. 207:481-490(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-109, AND ACETYLATION AT SER-2.
RX PubMed=6617664; DOI=10.1111/j.1432-1033.1983.tb07698.x;
RA McManus J.P., Watson D.C., Yaguchi M.;
RT "The complete amino acid sequence of oncomodulin -- a parvalbumin-like
RT calcium-binding protein from Morris hepatoma 5123tc.";
RL Eur. J. Biochem. 136:9-17(1983).
RN [4]
RP CALCIUM-BINDING.
RX PubMed=3571255; DOI=10.1016/s0021-9258(18)45562-7;
RA Williams T.C., Corson D.C., Sykes B.D., McManus J.P.;
RT "Oncomodulin. 1H NMR and optical stopped-flow spectroscopic studies of its
RT solution conformation and metal-binding properties.";
RL J. Biol. Chem. 262:6248-6256(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=2231727; DOI=10.1016/s0022-2836(05)80065-8;
RA Ahmed F.R., Przybylska M., Rose D.R., Birnbaum G.I., Pippy M.E.,
RA McManus J.P.;
RT "Structure of oncomodulin refined at 1.85-A resolution. An example of
RT extensive molecular aggregation via Ca2+.";
RL J. Mol. Biol. 216:127-140(1990).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02705; AAA41756.1; -; mRNA.
DR EMBL; X15836; CAA33840.1; -; Genomic_DNA.
DR EMBL; X15837; CAA33840.1; JOINED; Genomic_DNA.
DR EMBL; X15838; CAA33840.1; JOINED; Genomic_DNA.
DR PIR; S04616; PVRTO.
DR RefSeq; NP_037127.1; NM_012995.1.
DR PDB; 1OMD; X-ray; 1.85 A; A=2-109.
DR PDB; 1RRO; X-ray; 1.30 A; A=2-109.
DR PDB; 2NLN; NMR; -; A=2-109.
DR PDBsum; 1OMD; -.
DR PDBsum; 1RRO; -.
DR PDBsum; 2NLN; -.
DR AlphaFoldDB; P02631; -.
DR BMRB; P02631; -.
DR SMR; P02631; -.
DR STRING; 10116.ENSRNOP00000040755; -.
DR iPTMnet; P02631; -.
DR PaxDb; P02631; -.
DR Ensembl; ENSRNOT00000092601; ENSRNOP00000075788; ENSRNOG00000001031.
DR GeneID; 25503; -.
DR KEGG; rno:25503; -.
DR CTD; 654231; -.
DR RGD; 3222; Ocm.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000161875; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; P02631; -.
DR OMA; KKFFQVC; -.
DR OrthoDB; 1524081at2759; -.
DR PhylomeDB; P02631; -.
DR TreeFam; TF332342; -.
DR EvolutionaryTrace; P02631; -.
DR PRO; PR:P02631; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001031; Expressed in esophagus and 9 other tissues.
DR Genevisible; P02631; RN.
DR GO; GO:0032437; C:cuticular plate; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032420; C:stereocilium; IDA:RGD.
DR GO; GO:0099512; C:supramolecular fiber; IDA:CAFA.
DR GO; GO:0031982; C:vesicle; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IDA:CAFA.
DR GO; GO:1905593; P:positive regulation of optical nerve axon regeneration; IDA:CAFA.
DR GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; IDA:CAFA.
DR GO; GO:0009611; P:response to wounding; IDA:CAFA.
DR DisProt; DP00730; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6617664"
FT CHAIN 2..109
FT /note="Oncomodulin"
FT /id="PRO_0000073584"
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 BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="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:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="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: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:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="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:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6617664"
FT CONFLICT 26
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1RRO"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:1RRO"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1RRO"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:1RRO"
SQ SEQUENCE 109 AA; 12188 MW; 89A168BD30748514 CRC64;
MSITDILSAE DIAAALQECQ DPDTFEPQKF FQTSGLSKMS ASQVKDIFRF IDNDQSGYLD
GDELKYFLQK FQSDARELTE SETKSLMDAA DNDGDGKIGA DEFQEMVHS
