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H2A0N4

- PIF_PINMG

UniProt

H2A0N4 - PIF_PINMG

Protein

Protein PIF

Gene
N/A
Organism
Pinctada margaritifera (Black-lipped pearl oyster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 15 (01 Oct 2014)
      Sequence version 1 (21 Mar 2012)
      Previous versions | rss
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    Functioni

    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.By similarity
    Pif80 binds to both aragonite and calcite crystals, with a higher specificity for aragonite crystals.By similarity
    Pif97 contains a chitin-binding domain that allows for attachment of the entire complex to the chitin-containing organic framework.By similarity

    GO - Molecular functioni

    1. chitin binding Source: UniProtKB-KW

    GO - Biological processi

    1. chitin metabolic process Source: InterPro

    Keywords - Ligandi

    Chitin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein PIF
    Cleaved into the following 2 chains:
    Alternative name(s):
    Aragonite-binding proteinBy similarity
    OrganismiPinctada margaritifera (Black-lipped pearl oyster)
    Taxonomic identifieri102329 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 558536Protein Pif97PRO_0000418022Add
    BLAST
    Chaini559 – 1014456Protein Pif80PRO_0000418023Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi298 ↔ 311PROSITE-ProRule annotation
    Disulfide bondi354 ↔ 366PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    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.1 Publication

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 202174VWFAPROSITE-ProRule annotationAdd
    BLAST
    Domaini257 – 374118Chitin-binding type-2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni555 – 5584Kex2-like proteinase cleavage siteBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi369 – 990622Asp-richSequence AnalysisAdd
    BLAST
    Compositional biasi555 – 63682Arg-richSequence AnalysisAdd
    BLAST
    Compositional biasi706 – 834129Lys-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chitin-binding type-2 domain.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.170.140.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR002557. Chitin-bd_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01607. CBM_14. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    SMARTiSM00494. ChtBD2. 2 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEiPS50940. CHIT_BIND_II. 2 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    H2A0N4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVPYLQIVF LLTAVFGIGV KSDDCKTADL VVNVDGSDDV SDREFDKLKR     50
    AMLMLVRGLS IDDSQIRLGM VTYGSEIGDS IPLQGDRLDL ARTIRYMKKP 100
    GGPCKPFKGI GETRKMFSSR GRFNVPHVTL NLGGDIVDSE VRDLMDETDK 150
    ARDEDIKVMA IGLGTKVERD EIEGIAWDKE QAYFMDDADD LVRRVKEIPD 200
    YLCKIIKAKK PRKSASKKSK TKPAKKPDSD IVGKSPGFHS LQRTDDKPKM 250
    SKKVEVKELC DDAEWVEDVG YGSVPTRCED FVMCQNVSGS LRKTLKTCPY 300
    GQFWSRARTS CVLTEDEDCS DDLCKTMLLP SRDYDVSCRA YWKCENGKSV 350
    ARCCPSGMAY EPGKGCVLDS DCDEECPPKG DSDNGDDDDD DNDDDDNEYD 400
    DDDDEMEYNP NCPLRPIKGS PEKFKQHTGD DNWEEFDCAP GTLFSSRDCA 450
    CSILGRPEKD DNGKNEDDTS KVCEPELYLP FCDDLHDYSG KETHVENEGD 500
    AVIIENGKAY FNGRAGLKIP RFSGVPYGKS VFIKMKYKED EDDDKKRNDD 550
    DKKLRIKRDE RGRKGYRKGG RKDDRNGKRR DDRIGKRRDD RIFDDRKGRR 600
    TDDRKGDRRD RIDDRNGRRT DDRKDNRRDD RKDNRRDDIK DNKRDDKKDN 650
    ADEPMTLISN GECDNFELHD CFEKPSLAIT TGKKFAGFSV SSTERDEVDL 700
    EVDNDKKGYL WNKDKKDKDD KNRRDKDKNG DRTDDKKSLD DLVKEIERRK 750
    SDDKKSFDDL VKEIERRKSD DKKSFDDLVK EIERRKSDDK ISLDDLVKEI 800
    KRRKSDDKGN GRRKDDNKND EDDDKKGWKT VSLKINNGHI RGRRDDREDK 850
    DIMDGDLKTT FSGFQIGQGA SNKNFKGYMD EVYIYFCDPG KEADFDEEDD 900
    NGDDDDDDDD DDDKDNDAGD DNKDDNNNNG RKDDNNNDGR KDDNNKKDDK 950
    DRSDKNGGKD DKDKDTKDKF SDKDNGKDNE DADRDINDND KLYRRAMKKC 1000
    DFVNKNVEKW LDKR 1014
    Length:1,014
    Mass (Da):116,591
    Last modified:March 21, 2012 - v1
    Checksum:i7C4F1E7FA9555BA8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE610401 mRNA. Translation: CCE46175.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE610401 mRNA. Translation: CCE46175.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.170.140.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR002557. Chitin-bd_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01607. CBM_14. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    SMARTi SM00494. ChtBD2. 2 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    SSF57625. SSF57625. 1 hit.
    PROSITEi PS50940. CHIT_BIND_II. 2 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPIF_PINMG
    AccessioniPrimary (citable) accession number: H2A0N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 15 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3