OC90_HUMAN
ID OC90_HUMAN Reviewed; 477 AA.
AC Q02509; B4DNG8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Otoconin-90;
DE Short=Oc90;
DE AltName: Full=Phospholipase A2 homolog;
DE Flags: Precursor;
GN Name=OC90 {ECO:0000312|HGNC:HGNC:8100}; Synonyms=PLA2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8382789; DOI=10.1093/nar/21.1.135;
RA Feuchter-Murthy A.E., Freeman J.D., Mager D.L.;
RT "Splicing of a human endogenous retrovirus to a novel phospholipase A2
RT related gene.";
RL Nucleic Acids Res. 21:135-143(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
CC -!- FUNCTION: Major protein of the otoconia, a calcium carbonate structure
CC in the saccule and utricle of the ear. Together with OTOL1, acts as a
CC scaffold for otoconia biomineralization: sequesters calcium and forms
CC interconnecting fibrils between otoconia that are incorporated into the
CC calcium crystal structure. Together with OTOL1, modulates calcite
CC crystal morphology and growth kinetics. It is unlikely that this
CC protein has phospholipase A2 activity. {ECO:0000250|UniProtKB:Q9Z0L3}.
CC -!- SUBUNIT: Interacts with OTOL1. {ECO:0000250|UniProtKB:Q9Z0L3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P81869}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02509-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02509-3; Sequence=VSP_059516;
CC -!- DOMAIN: Consists of 3 PA2-type domains.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78662.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA78662.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; Z14310; CAA78662.1; ALT_SEQ; mRNA.
DR EMBL; AK297911; BAG60230.1; -; mRNA.
DR EMBL; AC092817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47919.1; -. [Q02509-1]
DR PIR; S30392; S30392.
DR RefSeq; NP_001073868.2; NM_001080399.2. [Q02509-1]
DR AlphaFoldDB; Q02509; -.
DR SMR; Q02509; -.
DR BioGRID; 609732; 35.
DR STRING; 9606.ENSP00000254627; -.
DR CarbonylDB; Q02509; -.
DR GlyGen; Q02509; 3 sites.
DR iPTMnet; Q02509; -.
DR PhosphoSitePlus; Q02509; -.
DR BioMuta; OC90; -.
DR DMDM; 215274202; -.
DR MassIVE; Q02509; -.
DR PaxDb; Q02509; -.
DR PeptideAtlas; Q02509; -.
DR PRIDE; Q02509; -.
DR ProteomicsDB; 58104; -. [Q02509-1]
DR Antibodypedia; 58400; 58 antibodies from 11 providers.
DR DNASU; 729330; -.
DR Ensembl; ENST00000254627.4; ENSP00000254627.3; ENSG00000253117.5. [Q02509-1]
DR GeneID; 729330; -.
DR KEGG; hsa:729330; -.
DR MANE-Select; ENST00000254627.4; ENSP00000254627.3; NM_001080399.3; NP_001073868.2.
DR UCSC; uc011lix.1; human. [Q02509-1]
DR CTD; 729330; -.
DR DisGeNET; 729330; -.
DR GeneCards; OC90; -.
DR HGNC; HGNC:8100; OC90.
DR HPA; ENSG00000253117; Not detected.
DR MIM; 601658; gene.
DR neXtProt; NX_Q02509; -.
DR OpenTargets; ENSG00000253117; -.
DR PharmGKB; PA31889; -.
DR VEuPathDB; HostDB:ENSG00000253117; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000159042; -.
DR HOGENOM; CLU_016613_1_0_1; -.
DR InParanoid; Q02509; -.
DR OMA; QISCENA; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q02509; -.
DR TreeFam; TF353106; -.
DR PathwayCommons; Q02509; -.
DR BioGRID-ORCS; 729330; 10 hits in 1060 CRISPR screens.
DR GenomeRNAi; 729330; -.
DR Pharos; Q02509; Tbio.
DR PRO; PR:Q02509; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q02509; protein.
DR Bgee; ENSG00000253117; Expressed in cortical plate and 12 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:UniProt.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..477
FT /note="Otoconin-90"
FT /id="PRO_0000022993"
FT REGION 76..190
FT /note="Phospholipase A2-like 1"
FT REGION 305..361
FT /note="Phospholipase A2-like 2"
FT REGION 373..425
FT /note="Phospholipase A2-like 3"
FT REGION 428..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..145
FT /evidence="ECO:0000250"
FT DISULFID 99..190
FT /evidence="ECO:0000250"
FT DISULFID 101..117
FT /evidence="ECO:0000250"
FT DISULFID 116..172
FT /evidence="ECO:0000250"
FT DISULFID 123..165
FT /evidence="ECO:0000250"
FT DISULFID 132..158
FT /evidence="ECO:0000250"
FT DISULFID 152..163
FT /evidence="ECO:0000250"
FT VAR_SEQ 227
FT /note="E -> VAAETEADRLITLSKKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8382789"
FT /id="VSP_059516"
FT CONFLICT 61
FT /note="P -> A (in Ref. 1; CAA78662)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Y -> C (in Ref. 1; CAA78662)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="N -> D (in Ref. 1; CAA78662 and 2; BAG60230)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> G (in Ref. 1; CAA78662 and 2; BAG60230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 51728 MW; 14F1A3ED1F813842 CRC64;
MIAFLLTSVL MIPHAGGHPL DTPHLPQELP PGLPNNINIT FFSGMFKNVE SVAEIFDCLG
PHFTWLQAVF TNFPVLIQFV NGMKCVAGLC PRDFEDYGCT CRFEMEGLPV DESDSCCFQH
RRCYEEAAEM DCLQDPAKLS TEVNCVSKKI ICESKDNCEH LLCTCDKAAI ECLARSSLNS
SLNLLDTSFC LAQTPETTIK EDLTTLLPRV VPVEPTDTSL TALSGEEAGH DQEGVGAARA
TSPPGSAEIV ATRVTAKIVT LVPAGIKSLG LAVSSVENDP EETTEKACDR FTFLHLGSGD
NMQVMPQLGE MLFCLTSRCP EEFESYGCYC GQEGRGEPRD DLDRCCLSHH CCLEQVRRLG
CLLERLPWSP VVCVDHTPKC GGQSLCEKLL CACDQTAAEC MTSASFNQSL KSPSRLGCPG
QPAACEDSLH PVPAAPTLGS SSEEDSEEDP PQEDLGRAKR FLRKSLGPLG IGPLHGR
