PIF_PINMG
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 25-MAY-2022, entry version 30.
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 PRIDE; 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; -; 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; PF01607; CBM_14; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00494; ChtBD2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57625; SSF57625; 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
