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 18-JUL-2018, entry version 5. 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; OC Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH RP OTOL1, 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 RT aggregate 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., RA Noel B., Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., RA Louis A., Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., RA Gaspin C., Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., RA Galiana D., Bobe J., Volff J.N., Genet C., Wincker P., Jaillon O., RA Roest Crollius H., 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 RT calcium 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 CC carbonate structure of the inner ear involved in hearing and CC balance sensing (PubMed:18410381). Binds calcium (PubMed:18410381, CC PubMed:28866388). {ECO:0000269|PubMed:18410381, CC ECO:0000269|PubMed:28866388}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000269|PubMed:18410381}. Note=Accumulates in the CC ring-like structures of otoliths. {ECO:0000269|PubMed:18410381}. CC -!- TISSUE SPECIFICITY: Specifically expressed in otolith matrix- CC producing cells. {ECO:0000269|PubMed:18410381}. CC -!- DOMAIN: The Asp/Glu-rich (acidic) region mediates binding to CC calcium. {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 UniGene; Omy.4244; -. DR GeneID; 100170213; -. PE 1: Evidence at protein level; KW Extracellular matrix; Glycoprotein; Secreted; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 628 Otolith matrix protein OMM-64. FT {ECO:0000255}. FT /FTId=PRO_5001591264. FT COMPBIAS 78 608 Asp/Glu-rich (acidic). FT {ECO:0000255|PROSITE-ProRule:PRU00004}. FT CARBOHYD 318 318 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CONFLICT 44 44 G -> A (in Ref. 1; BAG14384). FT {ECO:0000305}. FT CONFLICT 166 166 E -> K (in Ref. 1; BAG14384). FT {ECO:0000305}. FT CONFLICT 369 369 K -> E (in Ref. 1; BAG14384). FT {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 //