ID   OTOL1_ONCKE             Reviewed;         508 AA.
AC   P83371;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Otolin-1 {ECO:0000303|PubMed:11856329};
DE   Flags: Precursor;
GN   Name=otol1; Synonyms=oto1;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-40 AND 452-482,
RP   FUNCTION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=11856329; DOI=10.1046/j.0014-2956.2001.02701.x;
RA   Murayama E., Takagi Y., Ohira T., Davis J.G., Greene M.I., Nagasawa H.;
RT   "Fish otolith contains a unique structural protein, otolin-1.";
RL   Eur. J. Biochem. 269:688-696(2002).
CC   -!- FUNCTION: Collagen-like protein, which provides an organic scaffold for
CC       otoliths onto the sensory epithelium of the inner ear
CC       (PubMed:11856329). Acts as a scaffold for biomineralization by
CC       sequestering calcium (By similarity). {ECO:0000250|UniProtKB:A5PN28,
CC       ECO:0000269|PubMed:11856329}.
CC   -!- SUBUNIT: Homooligomer; disulfide-linked; probably forms homotrimers (By
CC       similarity). Interacts with otomp (By similarity).
CC       {ECO:0000250|UniProtKB:A0A060WQA3, ECO:0000250|UniProtKB:A5PN28}.
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   -!- TISSUE SPECIFICITY: Selectively expressed in the sacculus where it is
CC       localized to the otolith, the gelatinous layer of the otolithic
CC       membrane, and part of the transitional epithelium.
CC       {ECO:0000269|PubMed:11856329}.
CC   -!- DOMAIN: The C1q domain mediates calcium-binding.
CC       {ECO:0000250|UniProtKB:A5PN28}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11856329}.
CC   -!- SIMILARITY: Belongs to the OTOL1 family. {ECO:0000305}.
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DR   EMBL; AB067770; BAB84561.1; -; mRNA.
DR   AlphaFoldDB; P83371; -.
DR   SMR; P83371; -.
DR   PRIDE; P83371; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; 5.
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; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:11856329"
FT   CHAIN           26..508
FT                   /note="Otolin-1"
FT                   /id="PRO_0000003561"
FT   DOMAIN          144..367
FT                   /note="Collagen-like"
FT   DOMAIN          371..508
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          24..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   508 AA;  52138 MW;  90438799ACE3E9BE CRC64;
     MPSLRLLAIL TTLLAVVLIA TQSSATRTTR RPKPQNTKKP PRGGGTGGGG GGGDQPARLG
     FRQTTTTMAP SSSLGTDETT EDTMTDAYSL SPTDSTTYAG DAYPTEFHTD SMALPGAGMG
     NYTLDYSHCY LNVCECCPPE KGRGPPGERG PPGPGAERGL PGVPGEKGDV GLMGPPGLDG
     MPGATGLEGD KGDKGDQGDT GMPGAPGILG KEGPKGDLGP KGEKGETGLP GLKGDLGERG
     KPGWNGTQGE KGDLGKIGPA GPSGLTGPMG QNGQKGEMGE CPTGEKGEKG EAGLPGPPGP
     RGLVGTPGVN GTNGLPGPVG LRGQLGSPGG KGEAGGRGPP GLRGMPGPKG EKGPKGPRGV
     RGPKGPQGET AEQIRSAFSV GLFPSKSFPP PGLPVKFDKI LYNEEEHWDP MLSKFNCTHP
     GVYVFSYHIT VRNRPLRAAL VINGVKKLRT RDSLYGQDID QASNLALLRL ASGDQVWLET
     LRDWNGVYSS SEDDSTFTGF LLYADPKA