ID   SAP1A_ACRMI             Reviewed;         168 AA.
AC   B3EWZ0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Secreted acidic protein 1A {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 26-53, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   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; JT018094; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWZ0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..168
FT                   /note="Secreted acidic protein 1A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429557"
FT   REGION          49..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..168
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  18111 MW;  658AFD59F327FA17 CRC64;
     MARDLLLVVF FACLLQSFWG LPLPLKNENA IVDGDGTSVV TTKEDASTIF ERDPNPANQV
     SAMVTGVILD ENGDPGESDE SVENVDNDGE GGDKDDDKNG EDNDLDNKEH EEEKGDDDRG
     DDEEEDDAEG DNDSNDNEGD DDDDDDSGDD DDVDESGADE DDDDDSGD