ID   MA161_PINFU             Reviewed;         131 AA.
AC   Q9TVT2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-OCT-2014, entry version 21.
DE   RecName: Full=N16.1 matrix protein;
DE   AltName: Full=N14#1;
DE   Flags: Precursor;
OS   Pinctada fucata (Pearl oyster).
OC   Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; Pteriomorphia;
OC   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
RT   of 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.,
RA   Kato T., 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
CC       nacreous layer. {ECO:0000269|PubMed:10580124,
CC       ECO:0000269|PubMed:19679771, ECO:0000269|PubMed:19679772}.
CC   -!- SUBUNIT: Heterooligomer; disulfide-linked. Pif97, Pif80, N16 and
CC       other 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
CC       the mantle, which region may be responsible for the nacreous layer
CC       formation, but only in trace amounts at the mantle edge, which
CC       region may be responsible for the prismatic layer formation.
CC       {ECO:0000269|PubMed:10580124}.
CC   -!- SIMILARITY: Belongs to the N16 matrix protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB023067; BAA83732.1; -; mRNA.
DR   EMBL; AB023248; BAA83733.1; -; mRNA.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    131       N16.1 matrix protein.
FT                                /FTId=PRO_0000379787.
FT   REPEAT       91     92       1.
FT   REPEAT       93     94       2.
FT   REPEAT       95     96       3.
FT   REPEAT       97     98       4.
FT   REPEAT       99    100       5.
FT   REPEAT      101    102       6.
FT   REGION       91    102       6 X 2 AA tandem repeats of N-G.
SQ   SEQUENCE   131 AA;  15504 MW;  89947FB9525616AD CRC64;
     MKCTLRWTIT ALVLLGICHL ARPAYHKKCG RYSYCWIPYD IERDRRDNGG KKYCFCRYAW
     SPWQCNEEER YEWLRCGMRF YSLCCYTDDD NGNGNGNGNG NGLNYLKSLY GGYGNGNGEF
     REEYIDERYD N
//