ID   ASOMP_ACRMI             Reviewed;         359 AA.
AC   B3EWY7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Acidic skeletal organic matrix protein {ECO:0000303|PubMed:23765379};
DE            Short=Acidic SOMP {ECO:0000303|PubMed:23765379};
DE   Flags: Precursor;
OS   Acropora millepora (Staghorn coral) (Heteropora millepora).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Acroporidae; Acropora.
OX   NCBI_TaxID=45264;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA   Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA   Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT   "Whole transcriptome analysis of the coral Acropora millepora reveals
RT   complex responses to CO(2)-driven acidification during the initiation of
RT   calcification.";
RL   Mol. Ecol. 21:2440-2454(2012).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 40-55; 142-171; 223-297 AND 303-329, TISSUE
RP   SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23765379; DOI=10.1093/molbev/mst109;
RA   Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA   Guichard N., Miller D.J., Marin F.;
RT   "The skeletal proteome of the coral Acropora millepora: the evolution of
RT   calcification by co-option and domain shuffling.";
RL   Mol. Biol. Evol. 30:2099-2112(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23765379}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC       organic matrix of the aragonitic skeleton (at protein level).
CC       {ECO:0000269|PubMed:23765379}.
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DR   EMBL; JR972076; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWY7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..359
FT                   /note="Acidic skeletal organic matrix protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429490"
FT   REGION          60..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..89
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        224..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   359 AA;  38915 MW;  D9C882ED5A8C29D0 CRC64;
     MLAPRLAFVL LLSSYFGSIL ITSVESSDEV DMEKKTVKMR GSNTSVLVEG DGGKISTLYF
     EEDDDDDDDE DNEESENEVE DFDDENALSF QVESLQEVDE SGKPVKASKS SEIQHSVSSV
     GSLAFTVSAL QNSTTYQNLS AKTVTLQAQL PNMATLELMV VLFLEDGTIK FGNETFKVLS
     GTMKFNINVT GWQYCDGATV SCLSDSNQPA AVGDNLDLAL TVKSEAEDPE EVDDAKRAET
     GKDPICVDPD DPNEEDDDCP VVYDMGGNSE MVLNKGVLVN NMDYVAMPQG FPNLEKTGMM
     QKKLTFRLPK TPGSVIIDPS VNIGVPPKKQ SGNSGTSIKA SSLCFFTLTL LLSVLIAHF