OTOAN_MOUSE
ID OTOAN_MOUSE Reviewed; 1137 AA.
AC Q8K561;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Otoancorin;
DE Flags: Precursor;
GN Name=Otoa;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Inner ear vestibule;
RX PubMed=11972037; DOI=10.1073/pnas.082515999;
RA Zwaenepoel I., Mustapha M., Leibovici M., Verpy E., Goodyear R., Liu X.Z.,
RA Nouaille S., Nance W.E., Kanaan M., Avraham K.B., Tekaia F., Loiselet J.,
RA Lathrop M., Richardson G., Petit C.;
RT "Otoancorin, an inner ear protein restricted to the interface between the
RT apical surface of sensory epithelia and their overlying acellular gels, is
RT defective in autosomal recessive deafness DFNB22.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6240-6245(2002).
CC -!- FUNCTION: May act as an adhesion molecule.
CC {ECO:0000269|PubMed:11972037}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000305|PubMed:11972037}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:11972037}; Extracellular side
CC {ECO:0000305|PubMed:11972037}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000305|PubMed:11972037}. Note=At the
CC interface between the apical surface of the epithelia and the overlying
CC acellular gel of the tectorial and otoconial membranes.
CC -!- TISSUE SPECIFICITY: Expressed in the inner ear and vestibule.
CC {ECO:0000269|PubMed:11972037}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cochlea on the upper surface of the
CC spiral limbus at 16.5 dpc onwards.
CC -!- SIMILARITY: Belongs to the stereocilin family. {ECO:0000305}.
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DR EMBL; AY055122; AAL27794.1; -; mRNA.
DR CCDS; CCDS40114.1; -.
DR RefSeq; NP_647471.1; NM_139310.1.
DR RefSeq; XP_017177756.1; XM_017322267.1.
DR AlphaFoldDB; Q8K561; -.
DR STRING; 10090.ENSMUSP00000044177; -.
DR GlyGen; Q8K561; 11 sites.
DR iPTMnet; Q8K561; -.
DR PhosphoSitePlus; Q8K561; -.
DR PaxDb; Q8K561; -.
DR PRIDE; Q8K561; -.
DR ProteomicsDB; 294350; -.
DR Antibodypedia; 50672; 83 antibodies from 19 providers.
DR DNASU; 246190; -.
DR Ensembl; ENSMUST00000047025; ENSMUSP00000044177; ENSMUSG00000034990.
DR GeneID; 246190; -.
DR KEGG; mmu:246190; -.
DR UCSC; uc009jnn.1; mouse.
DR CTD; 146183; -.
DR MGI; MGI:2149209; Otoa.
DR VEuPathDB; HostDB:ENSMUSG00000034990; -.
DR eggNOG; ENOG502QU5H; Eukaryota.
DR GeneTree; ENSGT00950000182957; -.
DR HOGENOM; CLU_291462_0_0_1; -.
DR InParanoid; Q8K561; -.
DR OMA; EQHGLPQ; -.
DR OrthoDB; 86428at2759; -.
DR PhylomeDB; Q8K561; -.
DR TreeFam; TF336607; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 246190; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Otoa; mouse.
DR PRO; PR:Q8K561; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K561; protein.
DR Bgee; ENSMUSG00000034990; Expressed in epithelium of cochlear duct and 25 other tissues.
DR ExpressionAtlas; Q8K561; baseline and differential.
DR Genevisible; Q8K561; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR InterPro; IPR026663; Otoancorin.
DR InterPro; IPR026664; Stereocilin-rel.
DR PANTHER; PTHR23412; PTHR23412; 1.
DR PANTHER; PTHR23412:SF18; PTHR23412:SF18; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Extracellular matrix; Glycoprotein; GPI-anchor; Hearing;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1113
FT /note="Otoancorin"
FT /id="PRO_0000021973"
FT PROPEP 1114..1137
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021974"
FT REGION 1095..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1113
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1137 AA; 126430 MW; 4AD20F631FE8A8A2 CRC64;
MSQGPRTCSL LLVLLLSHGG AYQREPSPRQ DLHPLLQKMA EEIIEGSYLN ALLDLTLFER
SHVWTADLSH RVLAYLNSKN VAFTIPSLQA VMEAHLEQYL YQPQKLLEDL RATDNQQFHT
AMKCLLEDKW GHLDLEDVVI NLGDIRDEAL QSPGVNRSLF LITLERCFQV LNALECVEVL
GRVLRGSSGS FLQPDITERL PQDLHEDAFK NLSAVFKDLY DQTSAHTQRA LYSWMTGILR
TPFNVTDGSV SWVSAEKLWI LGRYMVHLSF EEIMNISPIE IGLFISYDNA TKQLDMVYDI
TPELAQAFLE RIRCSSFDVR NISTIHRLGL LVCFYDGLEL LDATLAQVLL HQMLKCSRLR
GFQAGVQKLK ANLLDIATEN QTLNETLGSL SDAVVGLTSS QLESLSSDAV HSAISTLNQV
TGWGRSQIVI LSAKYLAQEK VLSFYNVCQM GVLLAGVGTQ AFYSMDHKDL WQVLRSPLSQ
DMSDLSPVQQ QGVLGKLMEA EDATSGIAEV PRALFKEVSL YDLWKESRFN ATVLKAKELR
RSQALFLYEF LGKTTERPEE LLSAGQLVKG VPCSHIDAMS DHLFLALFQY FDNNFSLLSP
DQVNCLAWKY WEVSRSSMPP FLLATLPSRF LSSIPPSRCV RFLISLGKRR LETLVLDSDK
RSVVVRKVQQ CLDGVIADEY TVDIVGHLLC HLPASFIERG ISPRAWAAAL HGLRSCTALS
SEQKAAVRVR LLEQWGPPEN WTAETTKDLA PFLAFFSGDE LHTVATKFPE ILQQTASKMV
GVLLPKEFLW AVFESVQNSS NESPSFDPTF GCHGVVTPSS DDIFKLAEAN ACWDPEVLLC
MEEDTFIRNV ELLGAVKGFS RAQLMALKEK AIQVWDLPSR WKEHHIVSLG RIALALSESE
LEQLDLSSID TVASLGQQTE WTPGQAKSIL QAFLEDSGYG IQDLKSFHLV GFGPTLCAMD
PTEIQLIKTS EFRAVVARIG TLFCSTPVLA GFKKKAEVVF GRPTEWTSSI LQELGTIAAG
ITKAELRMLN KELMTYFQPS AIRCLPGEVF KELSTEQIAS LGPQNAASVT HSQRLQLSSA
QLQSLQRALD GAKTHSWQTD PLSSSPTWPA STGSPTGEPA SQALWLGCTL LLLTAKS
