ID   OTOMP_ONCMY             Reviewed;         367 AA.
AC   Q9IBF7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Otolith matrix protein 1;
DE            Short=OMP-1;
DE   Flags: Precursor;
GN   Name=otomp; Synonyms=omp1;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Otolith;
RX   PubMed=11026663; DOI=10.1016/s0305-0491(00)00223-6;
RA   Murayama E., Okuno A., Ohira T., Takagi Y., Nagasawa H.;
RT   "Molecular cloning and expression of an otolith matrix protein cDNA from
RT   the rainbow trout, Oncorhynchus mykiss.";
RL   Comp. Biochem. Physiol. 126B:511-520(2000).
RN   [2]
RP   INTERACTION WITH OTOL1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14689310; DOI=10.1007/s00418-003-0605-5;
RA   Murayama E., Takagi Y., Nagasawa H.;
RT   "Immunohistochemical localization of two otolith matrix proteins in the
RT   otolith and inner ear of the rainbow trout, Oncorhynchus mykiss:
RT   comparative aspects between the adult inner ear and embryonic otocysts.";
RL   Histochem. Cell Biol. 121:155-166(2004).
CC   -!- FUNCTION: Required for normal otolith growth and deposition of otolin-1
CC       in the otolith. {ECO:0000250|UniProtKB:Q0VIL3}.
CC   -!- SUBUNIT: Interacts with OTOL1. {ECO:0000269|PubMed:14689310}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14689310}.
CC   -!- TISSUE SPECIFICITY: Expressed in the sacculus during the day.
CC       {ECO:0000269|PubMed:11026663, ECO:0000269|PubMed:14689310}.
CC   -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00741}.
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DR   EMBL; AB030389; BAA90399.1; -; mRNA.
DR   RefSeq; NP_001117664.1; NM_001124192.1.
DR   AlphaFoldDB; Q9IBF7; -.
DR   SMR; Q9IBF7; -.
DR   MEROPS; S60.976; -.
DR   GeneID; 100135796; -.
DR   KEGG; omy:100135796; -.
DR   CTD; 565818; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001156; Transferrin-like_dom.
DR   Pfam; PF00405; Transferrin; 1.
DR   PRINTS; PR00422; TRANSFERRIN.
DR   SMART; SM00094; TR_FER; 1.
DR   PROSITE; PS51408; TRANSFERRIN_LIKE_4; 1.
PE   1: Evidence at protein level;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..367
FT                   /note="Otolith matrix protein 1"
FT                   /id="PRO_0000332931"
FT   DOMAIN          27..363
FT                   /note="Transferrin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ   SEQUENCE   367 AA;  40629 MW;  956F2069EC983711 CRC64;
     MDRLDRRLAA TLLLFSFISF STQKTSISWC VVSEAEEQKC LDLAGSATAR NIRGTLLCVR
     GQSPTDCMEK IKNGTADAAA MFADDIYTAG WCFGLELAAG ESYNGVDGIS YYVVALARRS
     SSDLSLLEMH ERSSCHPRIR TTVGWTVPIG FLVNTSQISV DEQCNFPKAV GDFFGYSCVP
     GVKDREHDPR GSNPKYLCEA CIGDDNERHI CVNNHRERHY GEAGALRCVA ENLGDVAFVK
     HTTIFDNMDG NNMESWAMDL ELEDLKLLCP DGSEAGPFDH ETCHLAVVPA NAVVVRPEDK
     CRVWKYLERL QNAFGNTTMF SSVGYTQSDL LFSDSTHHLL RVVGSYTSWL GPSYTTVLQA
     FECESLC