DRP_PINMG
ID DRP_PINMG Reviewed; 152 AA.
AC H2A0M1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Aspartate-rich protein;
DE AltName: Full=Prism uncharacterized shell protein 2;
DE Short=PUSP2;
DE Flags: Precursor;
OS Margaritifera margaritifera (Freshwater pearl mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=102329;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC TISSUE=Mantle;
RX PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT mantle and shell: focus on biomineralization.";
RL BMC Genomics 11:613-613(2010).
RN [2]
RP PROTEIN SEQUENCE OF 36-50; 57-68; 86-100 AND 112-131, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Shell;
RX PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT "Different secretory repertoires control the biomineralization processes of
RT prism and nacre deposition of the pearl oyster shell.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC Expressed primarily in the mantle with highest level in the mantle edge
CC and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
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DR EMBL; HE610388; CCE46162.1; -; mRNA.
DR AlphaFoldDB; H2A0M1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..152
FT /note="Aspartate-rich protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417942"
FT REGION 82..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 16954 MW; C7427C7C8CBEC87F CRC64;
MQKLLLAVLF FSLLAVATAR PKYHKQGRRK GDACRLNCIF DNVVCEIPCK LLFRSRSKYI
DCVLPCRRDR VDCYIHCNHF DATPKTEAEP GSLDKGEGTK GEKGKEGKKE KGEYAIGNAE
SGNGSSGGSN KTHDDDDDDR DDVHENDDEN ED