OTO1A_DANRE
ID OTO1A_DANRE Reviewed; 489 AA.
AC A5PN28; Q60HI2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Otolin-1-A {ECO:0000305};
DE AltName: Full=zOtolin1 {ECO:0000303|PubMed:15905077};
DE Flags: Precursor;
GN Name=otol1a; Synonyms=otol1; ORFNames=si:dkey-119f1.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-442, AND FUNCTION.
RC STRAIN=Tuebingen; TISSUE=Inner ear;
RX PubMed=15905077; DOI=10.1016/j.mod.2005.03.002;
RA Murayama E., Herbomel P., Kawakami A., Takeda H., Nagasawa H.;
RT "Otolith matrix proteins OMP-1 and Otolin-1 are necessary for normal
RT otolith growth and their correct anchoring onto the sensory maculae.";
RL Mech. Dev. 122:791-803(2005).
RN [3]
RP FUNCTION, SUBUNIT, DOMAIN, AND CALCIUM-BINDING.
RX PubMed=29076638; DOI=10.1111/febs.14308;
RA Holubowicz R., Wojtas M., Taube M., Kozak M., Ozyhar A., Dobryszycki P.;
RT "Effect of calcium ions on structure and stability of the C1q-like domain
RT of otolin-1 from human and zebrafish.";
RL FEBS J. 284:4278-4297(2017).
CC -!- FUNCTION: Collagen-like protein, which provides an organic scaffold for
CC otoliths onto the sensory epithelium of the inner ear (PubMed:15905077,
CC PubMed:29076638). Acts as a scaffold for biomineralization by
CC sequestering calcium (PubMed:29076638). {ECO:0000269|PubMed:15905077,
CC ECO:0000269|PubMed:29076638}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked; probably forms homotrimers
CC (PubMed:29076638). Interacts with otomp (By similarity).
CC {ECO:0000250|UniProtKB:A0A060WQA3, ECO:0000269|PubMed:29076638}.
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:0000269|PubMed:29076638}.
CC -!- SIMILARITY: Belongs to the OTOL1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD61006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BX927289; CAN88052.1; -; Genomic_DNA.
DR EMBL; AB124554; BAD61006.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001093211.1; NM_001099741.1.
DR AlphaFoldDB; A5PN28; -.
DR SMR; A5PN28; -.
DR STRING; 7955.ENSDARP00000116485; -.
DR PaxDb; A5PN28; -.
DR Ensembl; ENSDART00000132859; ENSDARP00000116485; ENSDARG00000001771.
DR GeneID; 553759; -.
DR KEGG; dre:553759; -.
DR CTD; 553759; -.
DR ZFIN; ZDB-GENE-050707-1; otol1a.
DR eggNOG; ENOG502QRPC; Eukaryota.
DR GeneTree; ENSGT00940000155435; -.
DR HOGENOM; CLU_001074_0_0_1; -.
DR InParanoid; A5PN28; -.
DR OMA; YNDQGSY; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; A5PN28; -.
DR TreeFam; TF334029; -.
DR PRO; PR:A5PN28; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000001771; Expressed in ectoderm and 1 other tissue.
DR GO; GO:0005587; C:collagen type IV trimer; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0045299; P:otolith mineralization; IDA: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; 2.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..489
FT /note="Otolin-1-A"
FT /id="PRO_0000332217"
FT DOMAIN 145..204
FT /note="Collagen-like 1"
FT DOMAIN 205..255
FT /note="Collagen-like 2"
FT DOMAIN 264..323
FT /note="Collagen-like 3"
FT DOMAIN 351..488
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 27..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 10..11
FT /note="II -> ML (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> A (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> P (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> G (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..83
FT /note="GS -> DC (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> L (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="T -> P (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="I -> F (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="G -> D (in Ref. 2; BAD61006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 50792 MW; 4D41DE52604C7625 CRC64;
MPNILHPFII IMTLLVVATG NQASIDKTTQ WPRMKPTKKP PPRDEGPSKL GSISTTVSPT
AIGITEEVTD AMMDAYTITS TGSTTFSSDT YSADYHTEAM VPPGVGPGNY TLDYNECFFN
FCECCPPERG PPGPVGEKGL PGIPGGKGEM GPPGPPGQEG LTGAPGTHGV KGEKGDTGAS
GLPGIPGVTG KQGEKGESGP KGDKGDTGFP GLKGDPGERG EPGWNGTKGG MGEPGKQGLT
GPPGPDGIKG EKGDKGDCPF GEKGQKGSIG EPGPQGPKGD PGVPGTNGTD GLPGSKGPKG
DPGPLSKQGE PGPPGPQGPP GQRGMPGMKG TRGLKGARGI RGFKGFKGEP AVQKRSAFSV
GLFPSRSFPP PGLPIRFDKI IYNEEAHWDP NASKFNCTHG GVYVFSYYIT VRNRPLRAAL
VVNGIRKLRT RDSLYGQDID QASNMAVLRL SSGDQVWLET LRDWNGVYSS SEDDSTFSGF
LLYADATKD
