ONCO_CAVPO
ID ONCO_CAVPO Reviewed; 109 AA.
AC O35508;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Oncomodulin;
DE Short=OM;
DE AltName: Full=CBP-15;
DE AltName: Full=Parvalbumin beta;
GN Name=OCM;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Organ of Corti;
RX PubMed=9112110; DOI=10.1016/s0378-5955(97)00005-1;
RA Henzl M.T., Shibasaki O., Comegys T.H., Thalmann I., Thalmann R.;
RT "Oncomodulin is abundant in the organ of Corti.";
RL Hear. Res. 106:105-111(1997).
CC -!- FUNCTION: Has some calmodulin-like activity with respect to enzyme
CC activation and growth regulation. Binds two calcium ions (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in the organ of Corti.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR EMBL; U77842; AAB61901.1; -; mRNA.
DR RefSeq; NP_001166459.1; NM_001172988.2.
DR AlphaFoldDB; O35508; -.
DR BMRB; O35508; -.
DR SMR; O35508; -.
DR STRING; 10141.ENSCPOP00000010715; -.
DR Ensembl; ENSCPOT00000012026; ENSCPOP00000010715; ENSCPOG00000011911.
DR GeneID; 100135585; -.
DR KEGG; cpoc:100135585; -.
DR CTD; 654231; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000161875; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; O35508; -.
DR OMA; KKFFQVC; -.
DR OrthoDB; 1524081at2759; -.
DR TreeFam; TF332342; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000011911; Expressed in testis and 1 other tissue.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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_0000073581"
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: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; 12115 MW; 5D3F0D3D25634A72 CRC64;
MSITDVLSAD DIAAALQECQ DPDTFEPQKF FQTSGLSKMS ASQVKDVFRF IDNDQSGYLD
EEELKFFLQK FESGARELTE SETKSLMAAA DNDGDGKIGA DEFQEMVHS
