ID   PA2H_XENLA              Reviewed;         127 AA.
AC   P41485;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Phospholipase A2 homolog otoconin-22;
DE            Short=Oc22;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8494877; DOI=10.1021/bi00070a007;
RA   Pote K.G., Hauer C.R. III, Michel H., Shabanowitz J., Hunt D.F.,
RA   Kretsinger R.H.;
RT   "Otoconin-22, the major protein of aragonitic frog otoconia, is a homolog
RT   of phospholipase A2.";
RL   Biochemistry 32:5017-5024(1993).
CC   -!- FUNCTION: Major protein of the aragonitic otoconia. It is unlikely that
CC       this protein has phospholipase A2 activity.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Otoconial membrane in the maculae of the saccule
CC       and utricle. Otoconia are composites of proteins and inorganic crystals
CC       formed in the peripheral portion of the vestibular system of
CC       vertebrates. The otoconial membranes contain small crystals of calcium
CC       carbonate known as otoliths (ear stones) if there is a single deposit
CC       or as otoconia (ear dust) if there are many. Each mineral polymorph of
CC       otoconia has a protein unique to that polymorph.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   PIR; A49269; A49269.
DR   AlphaFoldDB; P41485; -.
DR   SMR; P41485; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
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   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted.
FT   CHAIN           1..127
FT                   /note="Phospholipase A2 homolog otoconin-22"
FT                   /id="PRO_0000161726"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        26..120
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..90
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   127 AA;  14631 MW;  996A448766859BCE CRC64;
     TPAQFDEMIK VTTIIYGLAN FSDYGCHCGL NNQGMPVDDI DWCCHSQDCC YNKAEMSGCN
     PVTQTYRFYV EEQKKVECMK ASNRCEKMIC ECDEKAANCF RKELEDYNIY FRNFSSLGAC
     RGPRPFC