OTOL1_MOUSE
ID OTOL1_MOUSE Reviewed; 482 AA.
AC Q4ZJM7; B9EKG7; Q3TYP6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Otolin-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=Otol1 {ECO:0000312|MGI:MGI:2685260};
GN Synonyms=Gm414 {ECO:0000312|MGI:MGI:2685260};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Wong G.W., Lodish H.F.;
RT "Genomic analysis of all C1q domain containing genes.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH OC90, AND TISSUE SPECIFICITY.
RX PubMed=17300776; DOI=10.1016/j.ydbio.2007.01.013;
RA Zhao X., Yang H., Yamoah E.N., Lundberg Y.W.;
RT "Gene targeting reveals the role of Oc90 as the essential organizer of the
RT otoconial organic matrix.";
RL Dev. Biol. 304:508-524(2007).
RN [5]
RP SUBCELLULAR LOCATION, SUBUNIT, HYDROXYLATION AT PRO-141; PRO-144; PRO-174;
RP PRO-177; LYS-189; PRO-180; PRO-222; PRO-234; PRO-288; PRO-306 AND LYS-315,
RP GLYCOSYLATION AT LYS-189 AND LYS-315, AND INTERACTION WITH OC90 AND CBLN1.
RX PubMed=20856818; DOI=10.1371/journal.pone.0012765;
RA Deans M.R., Peterson J.M., Wong G.W.;
RT "Mammalian Otolin: a multimeric glycoprotein specific to the inner ear that
RT interacts with otoconial matrix protein Otoconin-90 and Cerebellin-1.";
RL PLoS ONE 5:E12765-E12765(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, CALCIUM-BINDING, AND INTERACTION WITH OC90.
RX PubMed=21655225; DOI=10.1371/journal.pone.0020498;
RA Yang H., Zhao X., Xu Y., Wang L., He Q., Lundberg Y.W.;
RT "Matrix recruitment and calcium sequestration for spatial specific otoconia
RT development.";
RL PLoS ONE 6:E20498-E20498(2011).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22841569; DOI=10.1016/j.heares.2012.07.003;
RA Andrade L.R., Lins U., Farina M., Kachar B., Thalmann R.;
RT "Immunogold TEM of otoconin 90 and otolin - relevance to mineralization of
RT otoconia, and pathogenesis of benign positional vertigo.";
RL Hear. Res. 292:14-25(2012).
RN [8]
RP FUNCTION, SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=24748133; DOI=10.1371/journal.pone.0095333;
RA Moreland K.T., Hong M., Lu W., Rowley C.W., Ornitz D.M., De Yoreo J.J.,
RA Thalmann R.;
RT "In vitro calcite crystal morphology is modulated by otoconial proteins
RT otolin-1 and otoconin-90.";
RL PLoS ONE 9:E95333-E95333(2014).
RN [9]
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 specifically expressed in the inner
CC ear, which provides an organic scaffold for otoconia, a calcium
CC carbonate structure in the saccule and utricle of the ear
CC (PubMed:21655225, PubMed:24748133, PubMed:29076638). Acts as a scaffold
CC for biomineralization: sequesters calcium and forms interconnecting
CC fibrils between otoconia that are incorporated into the calcium crystal
CC structure (PubMed:21655225, PubMed:24748133, PubMed:29076638). Together
CC with OC90, modulates calcite crystal morphology and growth kinetics
CC (PubMed:24748133). {ECO:0000269|PubMed:21655225,
CC ECO:0000269|PubMed:24748133, ECO:0000269|PubMed:29076638}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked; probably forms homotrimers
CC (PubMed:20856818, PubMed:24748133, PubMed:29076638). Interacts with
CC OC90 (PubMed:17300776, PubMed:20856818, PubMed:21655225). Interacts
CC with CBLN1 (PubMed:20856818). {ECO:0000269|PubMed:17300776,
CC ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21655225,
CC ECO:0000269|PubMed:24748133, ECO:0000269|PubMed:29076638}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:20856818}. Note=Localized in both the
CC surrounding otoconial matrix and otoconia.
CC {ECO:0000269|PubMed:20856818}.
CC -!- TISSUE SPECIFICITY: Expressed in the organic matrix of otoconia (at
CC protein level) (PubMed:17300776, PubMed:22841569). Expressed in
CC neonatal sensory epithelium of vestibular utricle and saccule and also
CC in otoconia (PubMed:21655225). {ECO:0000269|PubMed:17300776,
CC ECO:0000269|PubMed:21655225, ECO:0000269|PubMed:22841569}.
CC -!- DOMAIN: The C1q domain mediates calcium-binding.
CC {ECO:0000269|PubMed:29076638}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:20856818}.
CC -!- SIMILARITY: Belongs to the OTOL1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ002405; AAY21937.2; -; mRNA.
DR EMBL; AK158454; BAE34516.1; -; mRNA.
DR EMBL; BC150904; AAI50905.1; -; mRNA.
DR CCDS; CCDS17409.1; -.
DR RefSeq; NP_001018041.2; NM_001018031.2.
DR AlphaFoldDB; Q4ZJM7; -.
DR SMR; Q4ZJM7; -.
DR STRING; 10090.ENSMUSP00000057607; -.
DR GlyGen; Q4ZJM7; 2 sites.
DR iPTMnet; Q4ZJM7; -.
DR PhosphoSitePlus; Q4ZJM7; -.
DR MaxQB; Q4ZJM7; -.
DR PaxDb; Q4ZJM7; -.
DR PRIDE; Q4ZJM7; -.
DR ProteomicsDB; 294130; -.
DR Antibodypedia; 50531; 67 antibodies from 15 providers.
DR DNASU; 229389; -.
DR Ensembl; ENSMUST00000053013; ENSMUSP00000057607; ENSMUSG00000027788.
DR GeneID; 229389; -.
DR KEGG; mmu:229389; -.
DR UCSC; uc008pmo.2; mouse.
DR CTD; 131149; -.
DR MGI; MGI:2685260; Otol1.
DR VEuPathDB; HostDB:ENSMUSG00000027788; -.
DR eggNOG; ENOG502QRPC; Eukaryota.
DR GeneTree; ENSGT00940000155435; -.
DR HOGENOM; CLU_001074_0_0_1; -.
DR InParanoid; Q4ZJM7; -.
DR OMA; YNDQGSY; -.
DR OrthoDB; 1258047at2759; -.
DR PhylomeDB; Q4ZJM7; -.
DR TreeFam; TF334029; -.
DR BioGRID-ORCS; 229389; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q4ZJM7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q4ZJM7; protein.
DR Bgee; ENSMUSG00000027788; Expressed in placenta 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:0005576; C:extracellular region; IDA:UniProtKB.
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:0045299; P:otolith mineralization; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; 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; 3.
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 Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..482
FT /note="Otolin-1"
FT /id="PRO_0000332216"
FT DOMAIN 130..189
FT /note="Collagen-like 1"
FT DOMAIN 217..276
FT /note="Collagen-like 2"
FT DOMAIN 283..342
FT /note="Collagen-like 3"
FT DOMAIN 343..478
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 120..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 144
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 174
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 177
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 180
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 189
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 222
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 234
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 288
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 306
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20856818"
FT MOD_RES 315
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:20856818"
FT CARBOHYD 189
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:20856818"
FT CARBOHYD 315
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:20856818"
FT CONFLICT 162
FT /note="K -> R (in Ref. 2; BAE34516)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="P -> S (in Ref. 1; AAY21937)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="G -> E (in Ref. 2; BAE34516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 49601 MW; D6236B23CB7919C3 CRC64;
MWIFSSLCAV LTILAMDDVA TEAKTTPYTK FTKKSEGKEM LKGLKPSSGF FLDGEETVHT
ETAAMAEPTT GSPALAMAES TAGPSASATT RLLPFESFSL DTTGFVLNCC HCCSFVTGQK
GEPGKMGKQG PKGETGDTGS PGHPGTTGPQ GPKGQKGEKG LKGDRGDQGA GGIPGYPGKP
GEQGALGPKG DKGTIGPAGT KGQKGSKGEL CGNGTKGEKG DPGASGAHGF IGEPGAKGEK
GGVGEKGYRG DLGERGEKGQ KGEKGMEGEK GSRGDVGSEG KRGSDGLPGL RGDSGPKGEK
GEIGSPGFTG PAGPKGELGS KGVRGPTGKK GSRGVKGSKG EATQVPQSAF SALLSKPFPP
PNVPIKFDKI LSNDQGDYSP VTGKFNCSVP GTYIFSYHVT VRGRPARISL VARNRKQFKS
RETLYGQQVD QASLLLILKL SAGDQVWLEV SKDWNGLYVG PEDDSIFSGF LLYPEETFSK
SP
