ID   NRP_PINMA               Reviewed;         265 AA.
AC   P86967;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Asparagine-rich protein;
DE   AltName: Full=Nacre uncharacterized shell protein 5;
DE            Short=NUSP5;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 208-219 AND 225-232, SUBCELLULAR LOCATION, AND TISSUE
RP   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: Nacreous layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle
CC       pallium and lower level in the mantle edge.
CC       {ECO:0000269|PubMed:23213212}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GT280013; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=GT281828; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; GT277780; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT277989; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT279760; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT280013; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281522; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281589; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT281828; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283071; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283312; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT283632; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420175; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86967; -.
DR   PRIDE; P86967; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..265
FT                   /note="Asparagine-rich protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000412720"
FT   REGION          20..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..171
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        65
FT                   /note="D -> G (in Ref. 1; GT281522/GT279760)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="A -> T (in Ref. 1; GT281522/GT279760/GT283071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="N -> H (in Ref. 1; GT280013)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="Q -> P (in Ref. 1; GT277780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="Q -> L (in Ref. 1; GT277780)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  32108 MW;  8DA601E11A9E2534 CRC64;
     MSRLTLLVLL VIAAVIQKVH GQGRENEKKN EHEPGNQDGG NQNEKTERNL REPNRQTRRF
     NTRNDNRNRN IMQKRAMLLW QRRMNQRSNQ NNFGNNRSIP PTNTFNRNRS RTKSNKSEVE
     KENGSNKASK GKMQSGDGGG NGSEKEGPER RKVQHRIAKR FQKRHPSNSP KPKPARKTTN
     QQYRRHFMNN YNNKYWNWRR NMLNRRRTSP QHYQNQQARW RYYRYGPYTW YRYKNKWRLV
     RYNNMYRRNI KTNQSKKSNQ NNQGD