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Q27451 (PRP1_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phenoloxidase subunit 1
EC=1.14.18.1
Alternative name(s):
PO 1
Tyrosinase 1
OrganismBombyx mori (Silk moth) [Reference proteome]
Taxonomic identifier7091 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Ref.1

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit By similarity. UniProtKB P04253

Subunit structure

Heterodimer. Ref.1

Subcellular location

Secreted.

Tissue specificity

Synthesized by hemocytes and released into the hemolymph plasma. Ref.1

Post-translational modification

The N-terminus is blocked. Ref.1

Sequence similarities

Belongs to the tyrosinase family.

Mass spectrometry

Molecular mass is 78880 Da from positions 52 - 685. Determined by MALDI. Ref.2

Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentSecreted
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response

Traceable author statement Ref.1. Source: UniProtKB

melanin biosynthetic process from tyrosine

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monophenol monooxygenase activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5151 Ref.1
PRO_0000035899
Chain52 – 685634Phenoloxidase subunit 1 Ref.1
PRO_0000035900

Sites

Metal binding2091Copper A By similarity UniProtKB P04253
Metal binding2131Copper A By similarity UniProtKB P04253
Metal binding2391Copper A By similarity UniProtKB P04253
Metal binding3661Copper B By similarity UniProtKB P04253
Metal binding3701Copper B By similarity UniProtKB P04253
Metal binding4061Copper B By similarity UniProtKB P04253

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Potential
Disulfide bond581 ↔ 623 By similarity
Disulfide bond583 ↔ 630 By similarity

Experimental info

Sequence conflict1711V → A AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q27451 [UniParc].

Last modified January 1, 1999. Version 2.
Checksum: 9DE93E0760DD353C

FASTA68578,785
        10         20         30         40         50         60 
MSDAKNNLLL FFDRPSEPCF MQKGEENAVF EIPDNYYPEK YQRVSNAIGN RFGSDAGRMI 

        70         80         90        100        110        120 
PIRNIALPNL DLPMELPYNE QFSLFVPKHR KLAGRLIDIF MGMRDVEDLQ SVCSYCQLRI 

       130        140        150        160        170        180 
NPYMFNYCLS VAILHRPDTK GLSIPTFAES FPDKFMDPKV FRQAREVSSV VPSGARMPIV 

       190        200        210        220        230        240 
IPSNYTASDT EPEQRVAYFR EDIGINLHHW HWHLVYPFDA ADRAIVNKDR RGELFYYMHQ 

       250        260        270        280        290        300 
QIIARYNVER MCNNLSRVRR YNNFRAAIEE GYFPKLDSTV ASRAWPPRFA GTTIRDLDRP 

       310        320        330        340        350        360 
VDQIRSDVSE LETWRDRFLQ AIENMSVMLP NGRQLPLDEE TGIDVLGNLM ESSIISRNRP 

       370        380        390        400        410        420 
YYGDLHNMGH VFISYSHDPD HRHLEQFGVM GDSATAMRDP VFYRWHAYID DIFHLYKYKL 

       430        440        450        460        470        480 
TPYGNDRLDF PNIRVSSVSI EGGGTPNTLN TLWEQSTVDL GRGMDFTPRG SVLARFTHLQ 

       490        500        510        520        530        540 
HDEYNYVIEV NNTGGSSVMG MFRIFIAPTV DESGKPFSFD EQRKLMIELD KFSQGVKPGN 

       550        560        570        580        590        600 
NTIRRKSIDS SVTIPYERTF RNQADRPADP GTAGAAEFDF CGCGWPHHML VPKGTTQGYP 

       610        620        630        640        650        660 
MVLFVMVSNW NDDRVEQDLV GSCNDAASYC GIRDRKYPDR RAMGFPFDRP APAATTLSDF 

       670        680 
LRPNMAVRDC IVRFTDRTRQ RGQQG

« Hide

References

[1]"Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin."
Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.
Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Kinshu X Showa.
Tissue: Hemocyte.
[2]"Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori."
Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.
Arch. Biochem. Biophys. 320:14-23(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Hemocyte.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D49370 mRNA. Translation: BAA08368.1.
RefSeqNP_001037335.1. NM_001043870.1.
UniGeneBmo.344.

3D structure databases

ProteinModelPortalQ27451.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID692758.

Organism-specific databases

CTD692758.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERPTHR11511. PTHR11511. 1 hit.
PfamPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSPR00187. HAEMOCYANIN.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
SSF48050. Hemocyanin_N. 1 hit.
SSF81296. Ig_E-set. 1 hit.
PROSITEPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00497. TYROSINASE_1. False negative.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRP1_BOMMO
AccessionPrimary (citable) accession number: Q27451
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1999
Last modified: April 3, 2013
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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