CDP_ACRMI
ID CDP_ACRMI Reviewed; 409 AA.
AC B3EX01;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=CUB domain-containing protein {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 106-121; 239-257 AND 272-293, 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 and acid-soluble
CC organic matrix of the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JR989025; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3EX01; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR SMART; SM00042; CUB; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS01180; CUB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..409
FT /note="CUB domain-containing protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429493"
FT DOMAIN 232..338
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 154..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 232..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 409 AA; 44777 MW; 22160E981B7C4A55 CRC64;
MFLFSLTVLS ALVLITESIP SVATDFPFFE ITKKFDDIET YNNDYGILKF QEQEPMENLT
CASCEAPSER ECTLNQTAVV CDQDPNIACL TFEAFNNFTM TTTFRRGCFL SGILCENACR
SFNASQDGNL TSCVQDCCNS SLCNAGSLPT EVTTEASTTA QETTATSTTT KQSTGASTTA
EPSTTAAPST TTKQTTVAST TATTTKPTTA PQTRATTLPT TAPTTAPAPI ACGGVLRGRG
TFTSPGFPGN YPNNVRCEWR VFLPRRQAIV FRIVSLDLAD PGDSLEFFDS GRVIRTFRGL
SRRKRSPSHR QTTNEKVLGE GEDGYYDDQE YVDYYYYDGR RKREPYFYQR RKKRRQQDRI
VIQGRNQVAG AIFQSDAAGN AAGFSTQFVQ GAADSESEAS ASSESSDED