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H2A0M7 (PLSP_PINMG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 11. 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:
Peroxidase-like protein
OrganismPinctada margaritifera (Black-lipped pearl oyster)
Taxonomic identifier102329 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted Ref.2.

Tissue specificity

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

Sequence similarities

Belongs to the peroxidase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processresponse to oxidative stress

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 793773Peroxidase-like protein
PRO_0000418021

Sequences

Sequence LengthMass (Da)Tools
H2A0M7 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: DD91EEE3CD70A1E4

FASTA79388,310
        10         20         30         40         50         60 
MNLFICHVFL LLLHGYLIIC QDIPPDTIIS AVNTAQQEVT QREASSFSQQ QARASVAAFA 

        70         80         90        100        110        120 
GAPQPAAVLA ASRPARTGLD RFNRRNDPQR NTELSIGGQV TQRATLALRS SDPASAAAPA 

       130        140        150        160        170        180 
ARTLTPLDAR APAAGFSASS TMTFRNAAAQ SCTDSRPVTV CDPQQRYRET DGQCNNLVFP 

       190        200        210        220        230        240 
SFPSGAFKLG AAFTAQGRFL FPAYDDGVSS PRIRSVIPGF LLPNARLVSR NVHSGTAFDS 

       250        260        270        280        290        300 
DRHTPFLTHF GQFIDHDIVS TPETEPKFTM PNSHCCLEPN LEECFNINFE PDPLLQGSCI 

       310        320        330        340        350        360 
RFNRADTAPS YFCNPGPRLQ QNQRSSFVDG TMVYGWDVEQ ENRLREPGTG RLISEGDDQL 

       370        380        390        400        410        420 
KLEPVADPLN PPCFPVDNRC FEAGDHRSLE TVPLTVMHIM FLRRHNLIVQ ELQNLPLPWT 

       430        440        450        460        470        480 
PELLFQEAKR IVVAELQHIT YNEFLPRVLG PQFMTIFRLW PAPLFSDTYS PLVDPRTTSG 

       490        500        510        520        530        540 
FSVAAYRFGH SLVRNVHDQI GPGGLPVNNL LLQDHFDRLQ THLNVFPGGN TEGFARWMKL 

       550        560        570        580        590        600 
SQKSRADRTL VDGLQNNLFP CEDPDCPMGG GVTKSFDLAA LNIQRGRDHG LPPYTAWRYW 

       610        620        630        640        650        660 
CTGRRAFVFT PNAVGLSDHS PFEANILSNT YRHVDDIDLF TGGMTEMRRP GALLGPTLSC 

       670        680        690        700        710        720 
IIGLQFSNYK RGDRFFYERP DPVMAFTPGQ LQAIKETSLA KILCSTMRSF SNVQIBAMDR 

       730        740        750        760        770        780 
VSPSNPIVNC DELRSQDIIA KIPFLWNQLP NRAIQSAAAR ASNISGRTGL RVSTRFEDPA 

       790 
MLRLIGRRRL YKH 

« 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 431-447 AND 633-648, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Shell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE610394 mRNA. Translation: CCE46168.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.640.10. 2 hits.
InterProIPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLSP_PINMG
AccessionPrimary (citable) accession number: H2A0M7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: March 21, 2012
Last modified: February 19, 2014
This is version 11 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