ID   SAAR2_ACRMI             Reviewed;         390 AA.
AC   B3EWY8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Skeletal aspartic acid-rich protein 2 {ECO:0000303|PubMed:23765379};
DE   Flags: Precursor; Fragment;
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 49-64; 75-88; 119-135; 146-164; 242-266 AND 309-337,
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: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}. Note=Presence in the organic matrix of the
CC       skeleton may be due to shedding of a soluble peptide. {ECO:0000255,
CC       ECO:0000303|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; JR991407; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWY8; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          <1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..390
FT                   /note="Skeletal aspartic acid-rich protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429556"
FT   TOPO_DOM        17..368
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          53..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  44149 MW;  BC2F1FA8992F7CBA CRC64;
     HCLPLESIAL FLVCLADEER KDDDNTKTIR GKNVSAKIFG RSGKIMIVRV DDDEDDTKDT
     VDRVSDKKDN VDDRRDNDDR EESIDKKDTV DKKNPIDDKD DKDDKDDVDN DNDKDDDFRD
     DDEDLLSFEL DELKEVDADG DEVDDKHSVD SFDDVEFQLS HVRTASRFKG LAVISVNLST
     HLQNNKANVG IMVYLFLEPG SVTFGNETFN VKAGTVKFNI EVNNWDFCEG SSPACSSRKE
     GKFLDLTMKI KSKDSPTEVE DDDRKKAVCN DKDDDNDDDD VDDDDDDDDD DDCPIIYSMG
     GDSEMLLNRG VMLDDDEYTA MPVGFPKLEI EDETRKFVFR IPKFSKRALV DPSVTPGERT
     PKLAISAGTW LQLNFLVTVL VQIAVMFVFH