ID   NRP_PINMG               Reviewed;         686 AA.
AC   H2A0M0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Asparagine-rich protein;
DE   AltName: Full=Prism uncharacterized shell protein 1;
DE            Short=PUSP1;
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 260-277; 595-616 AND 641-663, SUBCELLULAR LOCATION, AND
RP   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; HE610387; CCE46161.1; -; mRNA.
DR   AlphaFoldDB; H2A0M0; -.
DR   SMR; H2A0M0; -.
DR   PRIDE; H2A0M0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..686
FT                   /note="Asparagine-rich protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417943"
FT   REGION          34..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   686 AA;  74849 MW;  685D68B9B33E90B0 CRC64;
     MKGTSALLLI GFFHATISQD PGGTVVIGSL SGRKRGNLNT GGQITSNSAI LGDVNAGSKL
     SEPPKRRNTD KTARMLENNP RIGGSLIPPP GVIMEPNPYD INPPYFVSNK NSQSTNSATN
     TMLQSLTSDT KTTTRTSQTS STRASSSITQ GINTMNRNSM RFNQVDRNKI SGFVNSGGQI
     QTNPLNTNSQ SSPILAAQRQ ITRQKSENTQ GNSIVRNGGT NSLNIPSSTR RSQPPNMAVQ
     IGQNTATFNM GTDGKVLHKF LPTNLFENIN SVSKEPRNTA SVPGIGGMRN PGPSISIRNI
     FGTNNIEGSS VQLTGSSGVF VSDPGPKGNP TDVPQFVPSG ISPTVRDPNA LDPFKSIRNQ
     IVPDIKRNEV NRGNSMISAP VIDNPTNSNS MVELNSILQN VQNGFLSEAL GNSNNQNNRV
     TNIVNQINSA DPQPVRRCQF LPYRDLRTNK IDRRYFRQLV NGKWLNLKCA DGAGFNETTC
     LCSIHLTGDA QCSPEVRLNF NDGTIQNLTP INVHIDAEGV DASKGWAHFN GSTQMKFEYF
     NAYDVQRDFL IKLRFKADSY IPNQSHPIVT NCVAGQENTD PSIGVFLTGN YPHKIVFILQ
     TDKSKLLQHL IFDVPRDGWH DITYKYDGST LTGILDGKEK SLPTEGRIEN RQAVLVFGGC
     GNRIFRGNID DIQIYTCIPP SHRNKG