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 27-MAR-2024, entry version 25. 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}. 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 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 PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1. DR PANTHER; PTHR11844:SF33; TISSUE INHIBITOR OF METALLOPROTEINASE; 1. 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 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 //