ID   SAAR1_ACRMI             Reviewed;         386 AA.
AC   B3EWY6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Skeletal aspartic acid-rich protein 1 {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 31-48; 59-151; 167-184; 207-252; 305-332 AND 338-354,
RP   TISSUE 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; JT001945; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWY6; -.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..386
FT                   /note="Skeletal aspartic acid-rich protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429555"
FT   REGION          33..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..112
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..289
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  42838 MW;  3F3014F2C99344F4 CRC64;
     MAFVSCFHLR LLFLCLALFM AAECRPDELN KKVDSDETIS DDDVSARVQP NGGKIMIVRD
     NDYDASDDND NDNDDDDNND NDNDNDDDND VDRDNDNDDD DFDDSNDDML SFELDSIEEK
     DSDGNDVGST EGHSVESFED RPFSLSSVDR NSNALGVAAI NVNLSTKLED SNADVDIMLY
     LFREDGTISF GNETFDVQAG TVKFNIKISN WDFCDGSAQD CSEAKAGEYL DVNIKFKSKD
     TPIEVTDEER KSQNKPAVCK DKDTPDTDSD PDDSSDNAND GDDDDDDDCP HIYNMGGDSE
     MLLNRGVMNG DTYTAMPFGF PKVEIEDGEK KIKFRVPKFD DNVNIDPSVT PGRVPKNASP
     SPALCLKIHI LFIALLQAVT LFINSW