ID   OTOL1_ONCMY             Reviewed;         509 AA.
AC   A0A060WQA3;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Otolin-1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Otol1; ORFNames=GSONMT00063289001 {ECO:0000312|EMBL:CDQ69321.1};
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 [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   [2]
RP   INTERACTION WITH OTOMP.
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: Collagen-like protein, which provides an organic scaffold for
CC       otoliths onto the sensory epithelium of the inner ear. Acts as a
CC       scaffold for biomineralization by sequestering calcium.
CC       {ECO:0000250|UniProtKB:A5PN28}.
CC   -!- SUBUNIT: Homooligomer; disulfide-linked; probably forms homotrimers (By
CC       similarity). Interacts with otomp (PubMed:14689310).
CC       {ECO:0000250|UniProtKB:A5PN28, ECO:0000269|PubMed:14689310}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the
CC       surrounding otoconial matrix and otoconia.
CC       {ECO:0000250|UniProtKB:Q4ZJM7}.
CC   -!- DOMAIN: The C1q domain mediates calcium-binding.
CC       {ECO:0000250|UniProtKB:A5PN28}.
CC   -!- SIMILARITY: Belongs to the OTOL1 family. {ECO:0000305}.
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DR   EMBL; FR904664; CDQ69321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060WQA3; -.
DR   SMR; A0A060WQA3; -.
DR   STRING; 8022.A0A060WQA3; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0045299; P:otolith mineralization; ISS:UniProtKB.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..509
FT                   /note="Otolin-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5001590201"
FT   DOMAIN          193..244
FT                   /note="Collagen-like 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          285..329
FT                   /note="Collagen-like 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          372..509
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          23..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   509 AA;  52759 MW;  2CA5CBB359783E5B CRC64;
     MPSLRLLAIL TTLLAVVLMA TQSSATRTTR RPKPQNTKKP PRGGGTGGGG GGGDQPARLG
     FRQTTTTMSP SSSLGTDETT EDTMTDAYSL SPTDSTTYAG DAYPTEFHTD SMALPGAGMG
     NYTLDYSHCY LNVCECCPPE KGPVGPPGER GPPGPGAERA PAVPSETLAL MLGTDIYTHT
     FKIPILLSFY LIGDKGDQGD TGMPGAPGIL GKEGQKGDLG PKGEKGETGL PGLKGDLGER
     GKPGWNGTQG EKGDLGKIGP AGPSGLTGPM GQNGQKGEMG ECPTGEKGEK GEAGLPGPPG
     PRGSVGPPGV NGSNGLPGPV GLRGQLGSPG GKGEAGGRGP PGLRGMPGPK GEKGPKGPRG
     VRGPKGPQGE TAEQIRSAFS VGLFPSKSFP PPGLPVKFDK VLYNEEEHWD PMLSKFNCTH
     PGVYVFSYHI TVRNRPLRAA LVINGVKKLR TRDSLYGQDI DQASNLALLR LASGDQVWLE
     TLRDWNGVYS SSEDDSTFTG FLLYADPKA