OC90_MOUSE
ID OC90_MOUSE Reviewed; 485 AA.
AC Q9Z0L3; Q9CZ60; Q9Z225;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Otoconin-90;
DE Short=Oc90;
DE AltName: Full=Otoconin-95 {ECO:0000303|PubMed:9892667};
DE Short=Oc95 {ECO:0000303|PubMed:9892667};
DE Flags: Precursor;
GN Name=Oc90 {ECO:0000312|MGI:MGI:1313269};
GN Synonyms=Onc-95 {ECO:0000303|PubMed:9892667}, Pla2ll;
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] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RX PubMed=9892667; DOI=10.1073/pnas.96.2.529;
RA Verpy E., Leibovici M., Petit C.;
RT "Characterization of otoconin-95, the major protein of murine otoconia,
RT provides insights into the formation of these inner ear biominerals.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:529-534(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [GENOMIC DNA / MRNA] OF 18-485 (ISOFORM 5), AND PROTEIN
RP SEQUENCE OF 18-63.
RC STRAIN=C57BL/6J, and Swiss Webster;
RX PubMed=9860971; DOI=10.1073/pnas.95.26.15345;
RA Wang Y., Kowalski P.E., Thalmann I., Ornitz D.M., Mager D.L., Thalmann R.;
RT "Otoconin-90, the mammalian otoconial matrix protein, contains two domains
RT of homology to secretory phospholipase A2.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15345-15350(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH OTOL1.
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 INTERACTION WITH OTOL1.
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, DISRUPTION PHENOTYPE, CALCIUM-BINDING, AND INTERACTION WITH
RP OTOL1.
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 FUNCTION, 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).
CC -!- FUNCTION: Major protein of the otoconia, a calcium carbonate structure
CC in the saccule and utricle of the ear (PubMed:17300776). Together with
CC OTOL1, acts as a scaffold for otoconia biomineralization: sequesters
CC calcium and forms interconnecting fibrils between otoconia that are
CC incorporated into the calcium crystal structure (PubMed:21655225,
CC PubMed:24748133). Together with OTOL1, modulates calcite crystal
CC morphology and growth kinetics (PubMed:24748133). It is unlikely that
CC this protein has phospholipase A2 activity (PubMed:17300776).
CC {ECO:0000269|PubMed:17300776, ECO:0000269|PubMed:21655225,
CC ECO:0000269|PubMed:24748133}.
CC -!- SUBUNIT: Interacts with OTOL1. {ECO:0000269|PubMed:17300776,
CC ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21655225}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81869}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Z0L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0L3-2; Sequence=VSP_004510;
CC Name=3;
CC IsoId=Q9Z0L3-3; Sequence=VSP_004511, VSP_004513;
CC Name=4;
CC IsoId=Q9Z0L3-4; Sequence=VSP_004515;
CC Name=5;
CC IsoId=Q9Z0L3-5; Sequence=VSP_004512, VSP_004514;
CC -!- TISSUE SPECIFICITY: In the embryo, highly expressed in the developing
CC otocyst with weak expression in the brain. Also expressed in nonsensory
CC epithelia of both the vestibular and cochlear portions of the
CC developing inner ear. Not expressed in adult or embryonic macular
CC sensory epithelia. {ECO:0000269|PubMed:9892667}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 9.5.
CC {ECO:0000269|PubMed:9892667}.
CC -!- DOMAIN: Consists of 3 PA2-type domains.
CC -!- DISRUPTION PHENOTYPE: Otoconia show a strongly reduced matrix-calcium.
CC {ECO:0000269|PubMed:21655225}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF093591; AAD08924.1; -; mRNA.
DR EMBL; AF091846; AAC99455.1; -; mRNA.
DR EMBL; AF091847; AAC99456.1; -; Genomic_DNA.
DR EMBL; AK012981; BAB28578.1; -; mRNA.
DR CCDS; CCDS27508.1; -. [Q9Z0L3-1]
DR RefSeq; NP_035083.1; NM_010953.2. [Q9Z0L3-1]
DR RefSeq; XP_011243792.1; XM_011245490.1. [Q9Z0L3-5]
DR AlphaFoldDB; Q9Z0L3; -.
DR SMR; Q9Z0L3; -.
DR BioGRID; 201892; 1.
DR IntAct; Q9Z0L3; 1.
DR STRING; 10090.ENSMUSP00000062865; -.
DR GlyGen; Q9Z0L3; 4 sites.
DR iPTMnet; Q9Z0L3; -.
DR PhosphoSitePlus; Q9Z0L3; -.
DR PaxDb; Q9Z0L3; -.
DR PRIDE; Q9Z0L3; -.
DR DNASU; 18256; -.
DR Ensembl; ENSMUST00000060522; ENSMUSP00000062865; ENSMUSG00000015001. [Q9Z0L3-1]
DR GeneID; 18256; -.
DR KEGG; mmu:18256; -.
DR UCSC; uc007vzx.2; mouse. [Q9Z0L3-1]
DR CTD; 729330; -.
DR MGI; MGI:1313269; Oc90.
DR VEuPathDB; HostDB:ENSMUSG00000015001; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000159042; -.
DR InParanoid; Q9Z0L3; -.
DR OMA; HCEHLLC; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9Z0L3; -.
DR TreeFam; TF353106; -.
DR BioGRID-ORCS; 18256; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Oc90; mouse.
DR PRO; PR:Q9Z0L3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9Z0L3; protein.
DR Bgee; ENSMUSG00000015001; Expressed in vestibular epithelium and 24 other tissues.
DR ExpressionAtlas; Q9Z0L3; baseline and differential.
DR Genevisible; Q9Z0L3; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0045299; P:otolith mineralization; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd04707; otoconin_90; 2.
DR Gene3D; 1.20.90.10; -; 2.
DR InterPro; IPR041798; Otoconin-90.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 2.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 2.
DR SUPFAM; SSF48619; SSF48619; 2.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:9860971"
FT CHAIN 18..485
FT /note="Otoconin-90"
FT /id="PRO_0000022994"
FT REGION 75..189
FT /note="Phospholipase A2-like 1"
FT REGION 315..371
FT /note="Phospholipase A2-like 2"
FT REGION 383..435
FT /note="Phospholipase A2-like 3"
FT REGION 444..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..144
FT /evidence="ECO:0000250"
FT DISULFID 98..189
FT /evidence="ECO:0000250"
FT DISULFID 100..116
FT /evidence="ECO:0000250"
FT DISULFID 115..171
FT /evidence="ECO:0000250"
FT DISULFID 122..164
FT /evidence="ECO:0000250"
FT DISULFID 131..157
FT /evidence="ECO:0000250"
FT DISULFID 151..162
FT /evidence="ECO:0000250"
FT VAR_SEQ 208..240
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9892667"
FT /id="VSP_004511"
FT VAR_SEQ 208..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9892667"
FT /id="VSP_004510"
FT VAR_SEQ 225..240
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9860971"
FT /id="VSP_004512"
FT VAR_SEQ 241
FT /note="K -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9892667"
FT /id="VSP_004513"
FT VAR_SEQ 241
FT /note="K -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9860971"
FT /id="VSP_004514"
FT VAR_SEQ 297..330
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9892667"
FT /id="VSP_004515"
FT CONFLICT 114
FT /note="I -> S (in Ref. 1; AAD08924)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> AA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="Q -> R (in Ref. 1; AAD08924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52445 MW; 07C21BE695CFE0E8 CRC64;
MIMLLMVGML MAPCVGAHAL DTPNPQELPP GLSKNINITF FNGVFKNVES VAEIFDCLGS
HFTWLQAVFT NFPLLLQFVN SMRCVTGLCP RDFEDYGCAC RFEMEGMPVD ESDICCFQHR
RCYEEAVEMD CLQDPAKLSA DVDCTNKQIT CESEDPCERL LCTCDKAAVE CLAQSGINSS
LNFLDASFCL PQTPETTSGK AATLLPRGIP EKPTDTSQIA LSGEVAGEVR ADTLTTLSRT
KSVQDLQDTQ ASRTTSSPGS AEIIALAKGT THSAGIKPLR LGVSSVDNGS QEAAGKACDR
LAFVHLGDGD SMTAMLQLGE MLFCLTSHCP EEFETYGCYC GREGRGEPRD TLDRCCLSHH
CCLEQMRQVG CLHGRRSQSS VVCEDHMAKC VGQSLCEKLL CACDQMAAEC MASAFFNQSL
KSPDGAECQG EPVSCEDGML QGTLASSVDS SSEENSEEAP PQMERLRRFL EKPPGPLGAR
PLGGK
