DQRP_ACRMI
ID DQRP_ACRMI Reviewed; 522 AA.
AC B7W112;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Aspartic and glutamic acid-rich 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 287-305 AND 397-426, 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-soluble organic matrix of the
CC aragonitic skeleton (at protein level). {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; JR983175; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B7W112; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..522
FT /note="Aspartic and glutamic acid-rich protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429554"
FT REGION 72..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 319..465
FT /evidence="ECO:0000255"
FT COMPBIAS 72..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..380
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 60167 MW; 1B1C0247FD444231 CRC64;
MKVFVYLLVT FSLTNASPLR NRFNEDHDEF SKDDMARESF DTEEMYNAFL NRRDSSESQL
EDHLLSHAKP LYDDFFPKDT SPDDDEDSYW LESRNDDGYD LAKRKRGYDD EEAYDDFDEV
DDRADDEGAR DVDESDFEED DKLPAEEESK NDMDEETFED EPEEDKEEAR EEFAEDERAD
EREDDDADFD FNDEEDEDEV DNKAESDIFT PEDFAGVSDE AMDNFRDDNE EEYADESDDE
AEEDSEETAD DFEDDPEDES DETFRDEVED ESEENYQDDT EEGSEIKQND ETEEQPEKKF
DADKEHEDAP EPLKEKLSDE SKARAEDESD KSEDAAKEIK EPEDAVEDFE DGAKVSEDEA
ELLDDEAELS DDEAELSKDE AEQSSDEAEK SEDKAEKSED EAELSEDEAK QSEDEAEKAE
DAAGKESNDE GKKREDEAVK SKGIARDESE FAKAKKSNLA LKRDENRPLA KGLRESAAHL
RDFPSEKKSK DAAQGNIENE LDYFKRNAFA DSKDAEPYEF DK