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C7G0B5 (PIF_PINFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PIF

Cleaved into the following 2 chains:

  1. Protein Pif97
  2. Protein Pif80
    Alternative name(s):
    Aragonite-binding protein
OrganismPinctada fucata (Pearl oyster)
Taxonomic identifier50426 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Protein attributes

Sequence length1007 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the organic matrix for normal growth of the nacreous layer. The complex contributes to the initiation of aragonite crystallization as well as subsequenct stacking of aragonite tablets in the nacreous layer. Ref.1 Ref.2

Pif80 binds to both aragonite and calcite crystals, with a higher specificity to aragonite crystals. Ref.1 Ref.2

Pif97 contains a chitin-binding domain that allows for attachment of the entire complex to the chitin-containing organic framework. Ref.1 Ref.2

Subunit structure

Heterooligomer; disulfide-linked. Pif97, Pif80, N16 and other proteins form a complex. Ref.1

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Component of conchiolin, the organic matrix of nacre. Expressed at extremely high levels in the dorsal region of the mantle, which region may be responsible for the nacreous layer formation, but only in trace amounts at the mantle edge, which region may be responsible for the prismatic layer formation.

Miscellaneous

Pif80 and Pif97 are rich in Asp. This amino-acid appears to be common to biomineral-forming organisms.

Sequence similarities

Contains 1 chitin-binding type-2 domain.

Contains 1 VWFA domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processchitin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitin binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 547525Protein Pif97
PRO_5000503552
Chain548 – 1007460Protein Pif80
PRO_5000503553

Regions

Domain29 – 202174VWFA
Domain255 – 372118Chitin-binding type-2
Region544 – 5474Kex2-like proteinase cleavage site
Compositional bias367 – 981615Asp-rich
Compositional bias379 – 3857Poly-Asp
Compositional bias388 – 3936Poly-Asp
Compositional bias858 – 87215Poly-Asp

Amino acid modifications

Disulfide bond296 ↔ 309 By similarity
Disulfide bond352 ↔ 364 By similarity

Sequences

Sequence LengthMass (Da)Tools
C7G0B5 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: A4C31FD25964F52B

FASTA1,007115,355
        10         20         30         40         50         60 
MQVPSIRVVF LLTAVFCVGV KSDECKTADV VVNVDASDDV SDQDFDKLKR AMLMMVRGLS 

        70         80         90        100        110        120 
IDDNQIRLGM VTYGSEVCDS IPLQGDRLDL ARTIRYMKKP TGPSKPFKGM GEARRMFSSR 

       130        140        150        160        170        180 
GRYNVPHITM NLGGDIVDTE VKDLMDETDK ARDEDIKVMA IGLGAKVDRD EIESIAYDRD 

       190        200        210        220        230        240 
QAYFMDDEDD LIRKVKEIPD YLCKIIKAKK PKVSGGKKSK PAKKVDNGPA GKSPGFDALK 

       250        260        270        280        290        300 
QSDDKSDKAK KVEVKELCDD AEWVDGVGYG SVPTRCEDFV MCQNVSGSLR KTLKSCPFGQ 

       310        320        330        340        350        360 
YWSKRQTSCV LTEDEDCSDD LCKTMLLPSR EYDVSCRAYW KCEKGKSVAR CCPSGMAYEP 

       370        380        390        400        410        420 
GKGCVLDLDC DEECPPKNDG DDDDDSSDED DDDEIEYNPN CPLRPIKGHP EKFKQHTGDD 

       430        440        450        460        470        480 
NWEDFDCAPG TLFSARDCAC SILGTAKKDD KNDDGGDAHK VCEPELYLPF CDDLHDYSGK 

       490        500        510        520        530        540 
ETHVENEGDA VIIENGKAYF NGRAGLKIPR FSGVPYGKSV FIKMKYKEDE DDDKNKNDDD 

       550        560        570        580        590        600 
KKLRMKRDER SRKDYLKAIL KRDDRKDKTD DTKGRRIIDR NDIIDDRRGR RKDDRKDGGR 

       610        620        630        640        650        660 
DDGKDGRRDD RKDNRLDDIK DKNDEPMTLI SNGECDNFEL NDCFEKPSIA ITTGKKSAGF 

       670        680        690        700        710        720 
SVTSSEKDEV DLEIDEDKKG YLWDKEDGPD RNGKDKDRNG DRSDDRRGYY WKKKDKDDNG 

       730        740        750        760        770        780 
KDKDKKGDKS DDKKGYYWKK DKDDKNGKDK DKRRDKSDDK KSLDDIVREI ERSKGNGKDD 

       790        800        810        820        830        840 
NKDDEDDDKK GWKTVSLKIS NGHIRGRRDD REDKDVLDGD LKTTFSGFQI GQGASNKNFK 

       850        860        870        880        890        900 
GYMDEVYIYF CDPGKEADYD DEDDDDDDDD SDENDKNDDK KDGKKTDDKD KKDRKDGRDD 

       910        920        930        940        950        960 
RKDGRDDRKD RRDDRKDDRK GGKDDRKDDR KGGKDDRKDG RDVRDDRDRG DKYDKKDDKD 

       970        980        990       1000 
NDRLSDKDDR KDVDDNDKDD DNEKLYKRAM KKCDYVNKNV AKWLDKR 

« Hide

References

[1]"An acidic matrix protein, Pif, is a key macromolecule for nacre formation."
Suzuki M., Saruwatari K., Kogure T., Yamamoto Y., Nishimura T., Kato T., Nagasawa H.
Science 325:1388-1390(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 548-564 AND 815-842, SUBUNIT, FUNCTION.
Tissue: Mantle.
[2]"The molecular basis of nacre formation."
Kroger N.
Science 325:1351-1352(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Web resources

Protein Spotlight

String of intrusion - Issue 112 of December 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB236929 mRNA. Translation: BAH97338.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.170.140.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR002557. Chitin-bd_dom.
IPR002035. VWF_A.
[Graphical view]
PfamPF00092. VWA. 1 hit.
[Graphical view]
SMARTSM00494. ChtBD2. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
SSF57625. SSF57625. 1 hit.
PROSITEPS50940. CHIT_BIND_II. 2 hits.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIF_PINFU
AccessionPrimary (citable) accession number: C7G0B5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: October 13, 2009
Last modified: April 16, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries