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Protein

Phenoloxidase subunit 1

Gene
N/A
Organism
Simulium damnosum (Black fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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.Curated

Catalytic activityi

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

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Copper BBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenoloxidase subunit 1 (EC:1.14.18.1)
Alternative name(s):
PO-P1
OrganismiSimulium damnosum (Black fly)
Taxonomic identifieri37338 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraChironomoideaSimuliidaeSimulium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›195›195Phenoloxidase subunit 1PRO_0000271231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

By infection with O.dukei and O.ochengi.1 Publication

Interactioni

Subunit structurei

Heterodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP85046.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Sequence Analysis

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR005203. Hemocyanin_C.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
[Graphical view]
SUPFAMiSSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P85046-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDPFFYRWH SYIDDIFQEH KERLRPYTEA QLNFNGITVT GVQVAPERGP
60 70 80 90 100
TNTFQTSWQQ SDVDLSRGMD FVAPRGNVTA RFTHLNHTPF TYSIQVNNSS
110 120 130 140 150
GAQRMGMVRI FLAPKTDERG NEMLFRDQRL MMIEMDKFVV SMRPGQNTIR
160 170 180 190
RRSTESTVTI PFERTFRSLE ESRPDQTTDA QQQFNFCGCG WPHHM
Length:195
Mass (Da):22,867
Last modified:January 9, 2007 - v1
Checksum:i137ECB8E37454C4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 111 Publication
Non-terminal residuei195 – 19511 Publication

Cross-referencesi

3D structure databases

ProteinModelPortaliP85046.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR005203. Hemocyanin_C.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
[Graphical view]
SUPFAMiSSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Simulium damnosum s.l.: isolation and identification of prophenoloxidase following an infection with Onchocerca spp. using targeted differential display."
    Hagen H.-E., Klager S.L., McKerrow J.H., Ham P.J.
    Exp. Parasitol. 86:213-218(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.

Entry informationi

Entry nameiPRP1_SIMDA
AccessioniPrimary (citable) accession number: P85046
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: May 27, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.