ID   NCP_PINMG               Reviewed;         148 AA.
AC   H2A0N2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=NTR domain-containing protein;
DE   AltName: Full=Prism tissue inhibitor metalloproteinase protein 2;
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 106-114, SUBCELLULAR LOCATION, 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; HE610399; CCE46173.1; -; mRNA.
DR   AlphaFoldDB; H2A0N2; -.
DR   SMR; H2A0N2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.40.50.120; -; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   Pfam; PF00965; TIMP; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..148
FT                   /note="NTR domain-containing protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417978"
FT   DOMAIN          27..146
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        27..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        29..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   DISULFID        40..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ   SEQUENCE   148 AA;  17178 MW;  EBD2972B3BFC6EC9 CRC64;
     MVCRFSYVQV VLILVVLSVI ISWANACSCF PPDETRQQKC RRADFVFLGR GYVTGIQQIG
     SFFYLRYCFL IDRVFKDRAS SLNIPCALTN VESSYCGVRF ERGRRYIVSG YLTRSGNQIG
     ACEWNERWSN VPFLTRLQLF NDPQWCLP