ID   MA163_PINFU             Reviewed;         131 AA.
AC   Q9TW98;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=N16.3 matrix protein;
DE   AltName: Full=N14#3;
DE   AltName: Full=N14#4;
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], PROTEIN SEQUENCE OF 24-57, FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Mantle, and Nacre;
RX   PubMed=10580124; DOI=10.1016/s0014-5793(99)01387-3;
RA   Samata T., Hayashi N., Kono M., Hasegawa K., Horita C., Akera S.;
RT   "A new matrix protein family related to the nacreous layer formation of
RT   Pinctada fucata.";
RL   FEBS Lett. 462:225-229(1999).
RN   [2]
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   [3]
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:0000269|PubMed:10580124, 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 {ECO:0000269|PubMed:10580124}.
CC   -!- TISSUE SPECIFICITY: Component of conchiolin, the organic matrix of
CC       nacre. Expressed at extremely high levels in the dorsal region of the
CC       mantle, which region may be responsible for the nacreous layer
CC       formation, but only in trace amounts at the mantle edge, which region
CC       may be responsible for the prismatic layer formation.
CC       {ECO:0000269|PubMed:10580124}.
CC   -!- SIMILARITY: Belongs to the N16 matrix protein family. {ECO:0000305}.
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DR   EMBL; AB023250; BAA83735.1; -; mRNA.
DR   EMBL; AB023251; BAA83736.1; -; mRNA.
DR   AlphaFoldDB; Q9TW98; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10580124"
FT   CHAIN           24..131
FT                   /note="N16.3 matrix protein"
FT                   /id="PRO_0000379789"
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   REPEAT          101..102
FT                   /note="6"
FT   REGION          91..100
FT                   /note="6 X 2 AA tandem repeats of N-G"
SQ   SEQUENCE   131 AA;  15539 MW;  035DD514A0354D75 CRC64;
     MKCTLRWTIT ALVLLGICHL ARPAYHKKCG RYSYCWIPYD IERDRYDNGD KKCCFCRYAW
     SPWQCNEEER YEWLRCGMRF YSLCCYTDDD NGNGNGNGNG NGLNYLKSLY GGYGNGNGEF
     WEEYIDERYD N