OMM64_ONCMY
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 25-MAY-2022, entry version 14.
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}.
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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; 1073664at2759; -.
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
