ID   USOM2_ACRMI             Reviewed;         505 AA.
AC   B7WFQ1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Uncharacterized skeletal organic matrix protein 2 {ECO:0000303|PubMed:23765379};
DE            Short=Uncharacterized SOMP-2 {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 182-196; 204-216; 411-424 AND 431-443, 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: 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; JR982706; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B7WFQ1; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..505
FT                   /note="Uncharacterized skeletal organic matrix protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429756"
FT   TOPO_DOM        20..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   505 AA;  54906 MW;  2964CC786D8E16AF CRC64;
     MILFTAIILV ASVVHVVVSS PQQCYYCVED DCETMSLWIN QTCATSQRSL GTSHCGTAAV
     RYHEGYLGGV PLETTVKGCF DCTDKSAACF ALAGLLKSSL GWVVQQCDIN CCNDTNCNTN
     VTILSQNATN VLRRDAFGTT SCYECEESDN YTCILKQQSQ TCRTSRAALG ITHCSSAKVK
     TRNVLTGTVD VSFIRGCISC EDKKSACALL AGSFKFRKHA TMLECDIECC NGSYCNDGAA
     SLSKCFHCME DDGLSCSARQ QRQICSLDPE SLGTTHCGSA VGRKRNQNGA IQNYFYRGCF
     DCSKKKEACF TLGGYWKGDV NAPGATTLLE CELQCCDPNV INGSYCNVET PILKPAAITV
     FTPTVTGPAQ CNVCLEKDET SCSENQQTQV CGIDPYSLGT THCGSAVGRY RQSNGDMVYG
     FYRGCINCAD KMAACAAVGG FRKNVQKWTQ LQCEIECCTE DNCNTHTPRL VEVEQPNSAP
     RGEIHQLFRC TFVAVFIVFA CFIVC