ID   CPRM_PINNO              Reviewed;          61 AA.
AC   P83631;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   10-FEB-2021, entry version 19.
DE   RecName: Full=Calprismin;
DE   Flags: Fragment;
OS   Pinna nobilis (Noble pen shell).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pinnoidea; Pinnidae; Pinna.
OX   NCBI_TaxID=111169;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, GLYCOSYLATION, AND INTERACTION WITH
RP   CALCIUM CARBONATE.
RC   TISSUE=Eggshell matrix {ECO:0000269|PubMed:15994301};
RX   PubMed=15994301; DOI=10.1074/jbc.m506526200;
RA   Marin F., Amons R., Guichard N., Stigter M., Hecker A., Luquet G.,
RA   Layrolle P., Alcaraz G., Riondet C., Westbroek P.;
RT   "Caspartin and calprismin, two proteins of the shell calcitic prisms of the
RT   Mediterranean fan mussel Pinna nobilis.";
RL   J. Biol. Chem. 280:33895-33908(2005).
CC   -!- TISSUE SPECIFICITY: Expressed by the calcifying mantle epithelium and
CC       incorporated into the shell's calcitic prismatic layer.
CC       {ECO:0000269|PubMed:15994301}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:15994301}.
CC   -!- MISCELLANEOUS: Seems to interact with calcium carbonate.
CC       {ECO:0000269|PubMed:15994301}.
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PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein.
FT   CHAIN           1..>61
FT                   /note="Calprismin"
FT                   /evidence="ECO:0000269|PubMed:15994301"
FT                   /id="PRO_0000079294"
FT   NON_TER         61
FT                   /evidence="ECO:0000303|PubMed:15994301"
SQ   SEQUENCE   61 AA;  6735 MW;  60046AD021B3BCA9 CRC64;
     ITIEQGELVL NCISDKMMCE FEAAAEMVVP SPCPSEYDTC ILETNIPPAN QXPVHXIPXM
     H