ID   PRSKL_PINFU             Reviewed;         406 AA.
AC   C0J7L8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Prisilkin-39 {ECO:0000312|EMBL:ACJ06766.1};
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] {ECO:0000305, ECO:0000312|EMBL:ACJ06766.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19233851};
RX   PubMed=19233851; DOI=10.1074/jbc.m808357200;
RA   Kong Y., Jing G., Yan Z., Li C., Gong N., Zhu F., Li D., Zhang Y.,
RA   Zheng G., Wang H., Xie L., Zhang R.;
RT   "Cloning and characterization of Prisilkin-39, a novel matrix protein
RT   serving a dual role in the prismatic layer formation from the oyster
RT   Pinctada fucata.";
RL   J. Biol. Chem. 284:10841-10854(2009).
CC   -!- FUNCTION: Binds chitin and may serve as a framework constituent
CC       participating in shell formation. Inhibits aragonite precipitation and
CC       may regulate aragonite growth during shell layer formation. Does not
CC       affect calcite crystallization. {ECO:0000269|PubMed:19233851}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expression is confined to the prism and organic
CC       layers of the shell with no expression detected in the nacreous shell
CC       layer. Also expressed in the mantle edge, extrapallial fluid, hemolymph
CC       and, to a lesser extent, in the viscus (at protein level). In the
CC       mantle, localizes to inner epithelial cells of the outer fold and the
CC       outer epithelial cells of the middle fold at the bottom of the
CC       periostracal groove. {ECO:0000269|PubMed:19233851}.
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DR   EMBL; EU921665; ACJ06766.1; -; mRNA.
DR   AlphaFoldDB; C0J7L8; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Biomineralization; Chitin-binding; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..406
FT                   /note="Prisilkin-39"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000408775"
FT   TRANSMEM        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          78..197
FT                   /note="10 X 12 AA tandem repeat of G-G-Y-[SG]-G-Y-[GS]-Y-G-
FT                   Y-P-[AT]"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  41362 MW;  7CB4E9EF4D94BA5E CRC64;
     MKGFLTLLLV CAILSTGYCQ SRRRAALTGL VAGATIGALA SGGLGAGAGG FGVGGFPVGV
     GAVGIPVAVG GGIPYGYGGY SGYGYGYPAG GYGGYSYGYP TGGYGGYSYG YPTGGYGGYS
     YGYPTGGYGG YSYGYPTGGY SGYSYGYPTG GYSGYSYGYP TGGYSGYSYG YPTGGYSGYS
     YGYPTGGYSG YSYGYPTGGY SGYSYPTGGY SGYSYSSTPG YGYYGSGSGM GGMRSGYSYY
     SSPAPSYYSS GSMTPGYGYY SSGSGIGGGM GSGYSYYSSP APSYYSSSVS PGYGYYGSGS
     GMRGYGYYSS STPMYYGSRS TGYGPFSSGL GGMGSGYSYY SSSTPSYYSS GSMTPGYGYY
     GSTSYPGPGY GSYSYRTTSY QPSSYGYSSY GTTYPGHGHW HGHKDC