ID   CPP2_ACRMI              Reviewed;         389 AA.
AC   B8VIV4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=CUB and peptidase domain-containing protein 2 {ECO:0000303|PubMed:23765379};
DE   Flags: 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 170-183 AND 311-325, TISSUE SPECIFICITY, AND
RP   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 organic matrix of
CC       the aragonitic skeleton (at protein level).
CC       {ECO:0000269|PubMed:23765379}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; JT008002; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B8VIV4; -.
DR   SMR; B8VIV4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   SUPFAM; SSF50494; SSF50494; 2.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Repeat; Secreted.
FT   CHAIN           <1..>389
FT                   /note="CUB and peptidase domain-containing protein 2"
FT                   /id="PRO_0000429496"
FT   DOMAIN          <1..96
FT                   /note="Peptidase S1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          103..213
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   DOMAIN          228..>389
FT                   /note="Peptidase S1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        18..32
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..72
FT                   /evidence="ECO:0000255"
FT   DISULFID        157..176
FT                   /evidence="ECO:0000255"
FT   DISULFID        253..269
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         389
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  42799 MW;  28C49A9F1983DCE1 CRC64;
     QPKELMQVDL PLVSTQNCSL LYANYDPSTM ICAGTRQGGT GACNGDSGGP LVCEFKGKWY
     LEGVTSWAGV PCASPSKPTV YADVRKLKSW IAAKITGVPV LRVATNCNSV INNTLKSPGY
     PNSYPINMFC VYRVPIPCDT ELVIHFNSFH LENHVFCWYD RLRITDGSNR VIGTYCGQQT
     GRSVLVNDTV AVLTFKTDRS LNSSGFHLSF SFFRRAVCGI RPTLSGFIVG GTVAPINSWP
     WQAKLRIAGN FLCGGSLIQP EWVLTAAHCV EGESPSIIKV TLGAHYLSTA QVVGTEQYFD
     VVQIIQHENY KMPKPFSNDV ALLKLSRPAV LRNGVGLVCL SDEQFQRPFN KTTKSCWTTG
     WGTLFYRGSQ PKELMQVDLP LVSTQNCSL