ID OMM64_ONCMY Reviewed; 628 AA. AC A0A060XQP6; B1Q2L9; DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot. DT 03-SEP-2014, sequence version 1. DT 22-FEB-2023, entry version 15. DE RecName: Full=Otolith matrix protein OMM-64 {ECO:0000305}; DE AltName: Full=Otolith matrix macromolecule-64 {ECO:0000303|PubMed:18410381}; DE Short=OMM-64 {ECO:0000303|PubMed:18410381}; DE Flags: Precursor; GN ORFNames=GSONMT00017137001; OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH OTOL1, RP CALCIUM-BINDING, AND TISSUE SPECIFICITY. RX PubMed=18410381; DOI=10.1111/j.1742-4658.2008.06400.x; RA Tohse H., Takagi Y., Nagasawa H.; RT "Identification of a novel matrix protein contained in a protein aggregate RT associated with collagen in fish otoliths."; RL FEBS J. 275:2512-2523(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24755649; DOI=10.1038/ncomms4657; RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B., RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A., RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C., RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J., RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H., RA Guiguen Y.; RT "The rainbow trout genome provides novel insights into evolution after RT whole-genome duplication in vertebrates."; RL Nat. Commun. 5:3657-3657(2014). RN [3] RP FUNCTION. RX PubMed=28866388; DOI=10.1016/j.bbapap.2017.08.019; RA Poznar M., Holubowicz R., Wojtas M., Gapinski J., Banachowicz E., RA Patkowski A., Ozyhar A., Dobryszycki P.; RT "Structural properties of the intrinsically disordered, multiple calcium RT ion-binding otolith matrix macromolecule-64 (OMM-64)."; RL Biochim. Biophys. Acta 1865:1358-1371(2017). CC -!- FUNCTION: Calcium-binding component of otoliths, a calcium carbonate CC structure of the inner ear involved in hearing and balance sensing CC (PubMed:18410381). Binds calcium (PubMed:18410381, PubMed:28866388). CC {ECO:0000269|PubMed:18410381, ECO:0000269|PubMed:28866388}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000269|PubMed:18410381}. Note=Accumulates in the ring-like CC structures of otoliths. {ECO:0000269|PubMed:18410381}. CC -!- TISSUE SPECIFICITY: Specifically expressed in otolith matrix-producing CC cells. {ECO:0000269|PubMed:18410381}. CC -!- DOMAIN: The Asp/Glu-rich (acidic) region mediates binding to calcium. CC {ECO:0000269|PubMed:18410381}. 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; AB213022; BAG14384.1; -; mRNA. DR EMBL; FR905797; CDQ81607.1; -; Genomic_DNA. DR RefSeq; NP_001123464.1; NM_001129992.1. DR AlphaFoldDB; A0A060XQP6; -. DR GeneID; 100170213; -. DR KEGG; omy:100170213; -. DR OrthoDB; 4273706at2759; -. DR Proteomes; UP000193380; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Extracellular matrix; Glycoprotein; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..628 FT /note="Otolith matrix protein OMM-64" FT /evidence="ECO:0000255" FT /id="PRO_5001591264" FT REGION 43..628 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..111 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..176 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 177..216 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..249 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..264 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 273..366 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..451 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 460..475 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 489..518 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..534 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 554..568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CONFLICT 44 FT /note="G -> A (in Ref. 1; BAG14384)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="E -> K (in Ref. 1; BAG14384)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="K -> E (in Ref. 1; BAG14384)" FT /evidence="ECO:0000305" SQ SEQUENCE 628 AA; 66567 MW; 9487E9C6E1E5CA20 CRC64; MLSRLLIVPL IFALAGLAIS APVNDGTEAD NDERAASLLV HLKGDKDGGG LTGSPDGVSA GTTDGTDSSK ELAGGAVDSS PDTTDTPDAS SSDIFPDTNN RDTSVETTGN PDDSDAPDAA ESAGSQDTTD AADASEAVAE TVDTYDIPDT DGADDREKVS TEVSTEDLDS AGVDKSPESD STESPGSDSA ESPGSDSAES PGSDSTESPG SDSTESPRSD STDEVLTDVQ ADSADVTSDD MDEATETDKD DDKSDDKSDA DAATDKDDSD EDKDTELDGK AHAEDTQTEE AADSDSKQGA ADSDSDTDDD RPEKDVKNDS DDSKDTTEDD KPDKDDKKNR DSADNSNDDS DEMIQVPREE LEQQEINLKE GGVIGSQEET VASDMEEGSD VGDQKPGPED SIEEGSPVGR QDFKHPQDSE EEELEKEAKK EKELEEAEEE RTLKTIESDS QEDSVDESEA EPDSNSKKDI GTSDAPEPQE DDSEEDTDDS MMKEPKDSDD AESDKDDKDK NDMDKEDMDK DDMDKDDMDK DDMDKDDVDK DASDSVDDQS ESDAEPGADS HTVVDEIDGE ETMTPDSEEI MKSGEMDSVV EATEVPADIL DQPDQQDDMT QGASQAADAA ATALAAQS //