ID MA165_PINFU Reviewed; 129 AA. AC O97048; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 25-MAY-2022, entry version 49. DE RecName: Full=N16.5 matrix protein; DE AltName: Full=N14#5; DE AltName: Full=N14#7; DE AltName: Full=Pearlin; DE Flags: Precursor; OS Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada. OX NCBI_TaxID=50426; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mantle; RX PubMed=11246407; DOI=10.1007/pl00021687; RA Miyashita T., Takagi R., Okushima M., Nakano S., Miyamoto H., Nishikawa E., RA Matsushiro A.; RT "Complementary DNA cloning and characterization of pearlin, a new class of RT matrix protein in the nacreous layer of oyster pearls."; RL Mar. Biotechnol. 2:409-418(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mantle; RA Hayashi N., Samata T.; RT "14 kD matrix protein family in nacreous layer of Japanese peal oyster, RT Pinctada fucata."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP SUBUNIT, AND FUNCTION. RX PubMed=19679771; DOI=10.1126/science.1173793; RA Suzuki M., Saruwatari K., Kogure T., Yamamoto Y., Nishimura T., Kato T., RA Nagasawa H.; RT "An acidic matrix protein, Pif, is a key macromolecule for nacre RT formation."; RL Science 325:1388-1390(2009). RN [4] RP FUNCTION. RX PubMed=19679772; DOI=10.1126/science.1177055; RA Kroger N.; RT "The molecular basis of nacre formation."; RL Science 325:1351-1352(2009). CC -!- FUNCTION: May be specifically involved in the formation of the nacreous CC layer. {ECO:0000250, ECO:0000269|PubMed:19679771, CC ECO:0000269|PubMed:19679772}. CC -!- SUBUNIT: Heterooligomer; disulfide-linked. Pif97, Pif80, N16 and other CC proteins form a complex. {ECO:0000269|PubMed:19679771}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- TISSUE SPECIFICITY: Component of conchiolin, the organic matrix of CC nacre. Specifically expressed in mantle epithelium. CC -!- SIMILARITY: Belongs to the N16 matrix protein family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=String of intrusion - Issue CC 112 of December 2009; CC URL="https://web.expasy.org/spotlight/back_issues/112"; 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; AB020779; BAA75626.1; -; mRNA. DR EMBL; AB023252; BAA83737.1; -; mRNA. DR EMBL; AB023253; BAA83738.1; -; mRNA. DR EMBL; AB023254; BAA83739.1; -; mRNA. DR AlphaFoldDB; O97048; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Disulfide bond; Extracellular matrix; Repeat; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..129 FT /note="N16.5 matrix protein" FT /id="PRO_0000379790" FT REPEAT 91..92 FT /note="1" FT REPEAT 93..94 FT /note="2" FT REPEAT 95..96 FT /note="3" FT REPEAT 97..98 FT /note="4" FT REPEAT 99..100 FT /note="5" FT REGION 91..100 FT /note="5 X 2 AA tandem repeats of N-G" SQ SEQUENCE 129 AA; 15388 MW; 6447712EA0940A9C CRC64; MTCTLRWTIT ALVLLGICHL ARPAFRTKCG RYSYCWIPYD IERDRYDNGD KKCCFCRNAW SPWQCKEDER YEWLRCGHKF YYMCCYTDDD NGNGNGNGNG FNYLKSLYGG YGNGNGEFWE EYIDERYDK //