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H2A0N4 (PIF_PINMG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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 margaritifera (Black-lipped pearl oyster)
Taxonomic identifier102329 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Protein attributes

Sequence length1014 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 By similarity. UniProtKB C7G0B5

Pif80 binds to both aragonite and calcite crystals, with a higher specificity for aragonite crystals By similarity. UniProtKB C7G0B5

Pif97 contains a chitin-binding domain that allows for attachment of the entire complex to the chitin-containing organic framework By similarity. UniProtKB C7G0B5

Subunit structure

Heterooligomer; disulfide-linked. Pif97, Pif80, N16 and other proteins form a complex By similarity. UniProtKB C7G0B5

Subcellular location

Secreted Ref.2.

Tissue specificity

Nacreous layer of shell (at protein level). Expressed primarily in the mantle with highest level in the mantle pallium and lower level in the mantle edge. Ref.2

Miscellaneous

Pif80 and Pif97 are rich in Asp. This amino-acid appears to be common to biomineral-forming organisms By similarity. UniProtKB C7G0B5

Sequence similarities

Contains 1 chitin-binding type-2 domain.

Contains 1 VWFA domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandChitin-binding
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processchitin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 558536Protein Pif97
PRO_0000418022
Chain559 – 1014456Protein Pif80
PRO_0000418023

Regions

Domain29 – 202174VWFA
Domain257 – 374118Chitin-binding type-2 UniProtKB C7G0B5
Region555 – 5584Kex2-like proteinase cleavage site By similarity UniProtKB C7G0B5
Compositional bias369 – 990622Asp-rich
Compositional bias555 – 63682Arg-rich
Compositional bias706 – 834129Lys-rich

Amino acid modifications

Disulfide bond298 ↔ 311 By similarity
Disulfide bond354 ↔ 366 By similarity

Sequences

Sequence LengthMass (Da)Tools
H2A0N4 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 7C4F1E7FA9555BA8

FASTA1,014116,591
        10         20         30         40         50         60 
MQVPYLQIVF LLTAVFGIGV KSDDCKTADL VVNVDGSDDV SDREFDKLKR AMLMLVRGLS 

        70         80         90        100        110        120 
IDDSQIRLGM VTYGSEIGDS IPLQGDRLDL ARTIRYMKKP GGPCKPFKGI GETRKMFSSR 

       130        140        150        160        170        180 
GRFNVPHVTL NLGGDIVDSE VRDLMDETDK ARDEDIKVMA IGLGTKVERD EIEGIAWDKE 

       190        200        210        220        230        240 
QAYFMDDADD LVRRVKEIPD YLCKIIKAKK PRKSASKKSK TKPAKKPDSD IVGKSPGFHS 

       250        260        270        280        290        300 
LQRTDDKPKM SKKVEVKELC DDAEWVEDVG YGSVPTRCED FVMCQNVSGS LRKTLKTCPY 

       310        320        330        340        350        360 
GQFWSRARTS CVLTEDEDCS DDLCKTMLLP SRDYDVSCRA YWKCENGKSV ARCCPSGMAY 

       370        380        390        400        410        420 
EPGKGCVLDS DCDEECPPKG DSDNGDDDDD DNDDDDNEYD DDDDEMEYNP NCPLRPIKGS 

       430        440        450        460        470        480 
PEKFKQHTGD DNWEEFDCAP GTLFSSRDCA CSILGRPEKD DNGKNEDDTS KVCEPELYLP 

       490        500        510        520        530        540 
FCDDLHDYSG KETHVENEGD AVIIENGKAY FNGRAGLKIP RFSGVPYGKS VFIKMKYKED 

       550        560        570        580        590        600 
EDDDKKRNDD DKKLRIKRDE RGRKGYRKGG RKDDRNGKRR DDRIGKRRDD RIFDDRKGRR 

       610        620        630        640        650        660 
TDDRKGDRRD RIDDRNGRRT DDRKDNRRDD RKDNRRDDIK DNKRDDKKDN ADEPMTLISN 

       670        680        690        700        710        720 
GECDNFELHD CFEKPSLAIT TGKKFAGFSV SSTERDEVDL EVDNDKKGYL WNKDKKDKDD 

       730        740        750        760        770        780 
KNRRDKDKNG DRTDDKKSLD DLVKEIERRK SDDKKSFDDL VKEIERRKSD DKKSFDDLVK 

       790        800        810        820        830        840 
EIERRKSDDK ISLDDLVKEI KRRKSDDKGN GRRKDDNKND EDDDKKGWKT VSLKINNGHI 

       850        860        870        880        890        900 
RGRRDDREDK DIMDGDLKTT FSGFQIGQGA SNKNFKGYMD EVYIYFCDPG KEADFDEEDD 

       910        920        930        940        950        960 
NGDDDDDDDD DDDKDNDAGD DNKDDNNNNG RKDDNNNDGR KDDNNKKDDK DRSDKNGGKD 

       970        980        990       1000       1010 
DKDKDTKDKF SDKDNGKDNE DADRDINDND KLYRRAMKKC DFVNKNVEKW LDKR 

« Hide

References

[1]"Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization."
Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F., Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.
BMC Genomics 11:613-613(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION.
Tissue: Mantle.
[2]"Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell."
Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C., Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.
Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-87; 99-108; 123-152; 158-166; 170-193; 226-243; 297-306; 309-339; 353-364; 426-459; 472-491; 522-529; 791-798; 848-873 AND 989-995, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Shell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE610401 mRNA. Translation: CCE46175.1.

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]
PfamPF01607. CBM_14. 1 hit.
PF00092. 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_PINMG
AccessionPrimary (citable) accession number: H2A0N4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 14 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