ID   CPP1_ACRMI              Reviewed;         435 AA.
AC   B8V7S0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=CUB and peptidase domain-containing protein 1 {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 112-122; 158-168; 209-222 AND 335-348, 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: 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; JR970990; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B8V7S0; -.
DR   SMR; B8V7S0; -.
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:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
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   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; SSF49854; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          <1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..>435
FT                   /note="CUB and peptidase domain-containing protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429495"
FT   DOMAIN          25..261
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DOMAIN          256..378
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        116
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..218
FT                   /evidence="ECO:0000255"
FT   DISULFID        182..197
FT                   /evidence="ECO:0000255"
FT   DISULFID        208..237
FT                   /evidence="ECO:0000255"
FT   DISULFID        322..341
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         435
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   435 AA;  47906 MW;  586F5AFD73605F6A CRC64;
     SGFHLSFSFF RRAVCGIRPT LSGFIVGGTV APINSWPWQA KLRIAGNFLC GGSLIQPEWV
     LTAAHCVEGE SPSIIKVTLG AHYLSTAQVV GTEQYFDVVQ IIQHENYKMP KRFSNDVALL
     KLSRPAALRN GVGLVCLSDD QFQRPFNGTS CWTTGWGRLS WPGPVAKELM QVDLPLVSPQ
     NCLSSYPNGY DPNTMICAGR SQGGTGACRG DSGGPLVCEF KGKWYLEGVT SWGQLPCDLP
     NKPTVYADVR KLKSWITGKI SRSPALKVAT NCSSVLNNTL KSPGYPDSYP INMFCVYRVP
     IPCDTELVIH FNSFHLENHV FCWYDRLRIT DGSNRVIGTY CGQQTGRSVL VNDTVAVLTF
     KTDRSLNSSG FHLSFSFFPR GNATLLPFTT PTQTTTQRPT TTPTPGCGVV QNNTLRSPGY
     PSNYPRNTHC VYRVF