ID   PIF_PINMG               Reviewed;        1014 AA.
AC   H2A0N4;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Protein PIF;
DE   Contains:
DE     RecName: Full=Protein Pif97;
DE   Contains:
DE     RecName: Full=Protein Pif80;
DE     AltName: Full=Aragonite-binding protein {ECO:0000250|UniProtKB:C7G0B5};
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-87; 99-108; 123-152; 158-166; 170-193; 226-243;
RP   297-306; 309-339; 353-364; 426-459; 472-491; 522-529; 791-798; 848-873 AND
RP   989-995, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- FUNCTION: Essential component of the organic matrix for normal growth
CC       of the nacreous layer. The complex contributes to the initiation of
CC       aragonite crystallization as well as subsequenct stacking of aragonite
CC       tablets in the nacreous layer (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Pif80 binds to both aragonite and calcite crystals, with a
CC       higher specificity for aragonite crystals. {ECO:0000250}.
CC   -!- FUNCTION: Pif97 contains a chitin-binding domain that allows for
CC       attachment of the entire complex to the chitin-containing organic
CC       framework. {ECO:0000250|UniProtKB:C7G0B5}.
CC   -!- SUBUNIT: Heterooligomer; disulfide-linked. Pif97, Pif80, N16 and other
CC       proteins form a complex (By similarity).
CC       {ECO:0000250|UniProtKB:C7G0B5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Nacreous layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle
CC       pallium and lower level in the mantle edge.
CC       {ECO:0000269|PubMed:23213212}.
CC   -!- MISCELLANEOUS: Pif80 and Pif97 are rich in Asp. This amino-acid appears
CC       to be common to biomineral-forming organisms (By similarity).
CC       {ECO:0000250|UniProtKB:C7G0B5}.
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DR   EMBL; HE610401; CCE46175.1; -; mRNA.
DR   AlphaFoldDB; H2A0N4; -.
DR   SMR; H2A0N4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00494; ChtBD2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Chitin-binding; Direct protein sequencing; Disulfide bond; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..558
FT                   /note="Protein Pif97"
FT                   /id="PRO_0000418022"
FT   CHAIN           559..1014
FT                   /note="Protein Pif80"
FT                   /id="PRO_0000418023"
FT   DOMAIN          29..202
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   DOMAIN          257..374
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          212..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..558
FT                   /note="Kex2-like proteinase cleavage site"
FT                   /evidence="ECO:0000250|UniProtKB:C7G0B5"
FT   REGION          710..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..407
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..558
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..919
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..995
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        298..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        354..366
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   1014 AA;  116591 MW;  7C4F1E7FA9555BA8 CRC64;
     MQVPYLQIVF LLTAVFGIGV KSDDCKTADL VVNVDGSDDV SDREFDKLKR AMLMLVRGLS
     IDDSQIRLGM VTYGSEIGDS IPLQGDRLDL ARTIRYMKKP GGPCKPFKGI GETRKMFSSR
     GRFNVPHVTL NLGGDIVDSE VRDLMDETDK ARDEDIKVMA IGLGTKVERD EIEGIAWDKE
     QAYFMDDADD LVRRVKEIPD YLCKIIKAKK PRKSASKKSK TKPAKKPDSD IVGKSPGFHS
     LQRTDDKPKM SKKVEVKELC DDAEWVEDVG YGSVPTRCED FVMCQNVSGS LRKTLKTCPY
     GQFWSRARTS CVLTEDEDCS DDLCKTMLLP SRDYDVSCRA YWKCENGKSV ARCCPSGMAY
     EPGKGCVLDS DCDEECPPKG DSDNGDDDDD DNDDDDNEYD DDDDEMEYNP NCPLRPIKGS
     PEKFKQHTGD DNWEEFDCAP GTLFSSRDCA CSILGRPEKD DNGKNEDDTS KVCEPELYLP
     FCDDLHDYSG KETHVENEGD AVIIENGKAY FNGRAGLKIP RFSGVPYGKS VFIKMKYKED
     EDDDKKRNDD DKKLRIKRDE RGRKGYRKGG RKDDRNGKRR DDRIGKRRDD RIFDDRKGRR
     TDDRKGDRRD RIDDRNGRRT DDRKDNRRDD RKDNRRDDIK DNKRDDKKDN ADEPMTLISN
     GECDNFELHD CFEKPSLAIT TGKKFAGFSV SSTERDEVDL EVDNDKKGYL WNKDKKDKDD
     KNRRDKDKNG DRTDDKKSLD DLVKEIERRK SDDKKSFDDL VKEIERRKSD DKKSFDDLVK
     EIERRKSDDK ISLDDLVKEI KRRKSDDKGN GRRKDDNKND EDDDKKGWKT VSLKINNGHI
     RGRRDDREDK DIMDGDLKTT FSGFQIGQGA SNKNFKGYMD EVYIYFCDPG KEADFDEEDD
     NGDDDDDDDD DDDKDNDAGD DNKDDNNNNG RKDDNNNDGR KDDNNKKDDK DRSDKNGGKD
     DKDKDTKDKF SDKDNGKDNE DADRDINDND KLYRRAMKKC DFVNKNVEKW LDKR
//