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 26-JUN-2013, entry version 7. DE RecName: Full=NTR domain-containing protein; DE AltName: Full=Prism tissue inhibitor metalloproteinase protein 2; DE Flags: Precursor; OS Pinctada margaritifera (Black-lipped pearl oyster). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia; OC Pterioida; Pterioidea; Pteriidae; Pinctada. OX NCBI_TaxID=102329; RN [1] 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 RT calcifying 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 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., RA Montagnani C.; RT "Different secretory repertoires control the biomineralization RT processes of 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. CC -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level). CC Expressed primarily in the mantle with highest level in the mantle CC edge and lower level in the mantle pallium. CC -!- SIMILARITY: Contains 1 NTR domain. 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; HE610399; CCE46173.1; -; mRNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:InterPro. DR InterPro; IPR001134; Netrin_domain. DR InterPro; IPR001820; Prot_inh_TIMP. DR InterPro; IPR008993; TIMP-like_OB-fold. DR Pfam; PF00965; TIMP; 1. DR SUPFAM; SSF50242; TIMP_like; 1. DR PROSITE; PS50189; NTR; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Secreted; Signal. FT SIGNAL 1 26 Potential. FT CHAIN 27 148 NTR domain-containing protein. FT /FTId=PRO_0000417978. FT DOMAIN 27 146 NTR. FT DISULFID 27 96 By similarity. FT DISULFID 29 122 By similarity. FT DISULFID 40 146 By similarity. SQ SEQUENCE 148 AA; 17178 MW; EBD2972B3BFC6EC9 CRC64; MVCRFSYVQV VLILVVLSVI ISWANACSCF PPDETRQQKC RRADFVFLGR GYVTGIQQIG SFFYLRYCFL IDRVFKDRAS SLNIPCALTN VESSYCGVRF ERGRRYIVSG YLTRSGNQIG ACEWNERWSN VPFLTRLQLF NDPQWCLP //