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Q25519

- PRP2_MANSE

UniProt

Q25519 - PRP2_MANSE

Protein

Phenoloxidase subunit 2

Gene

ppo

Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. Binds to the surface of hemocytes and is involved in hemocyte melanization.1 PublicationCurated

    Catalytic activityi

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

    Cofactori

    Binds 2 copper ions per subunit.1 Publication

    Enzyme regulationi

    Activated by immulectin and lipopolysaccharide.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi215 – 2151Copper A
    Metal bindingi219 – 2191Copper A
    Metal bindingi245 – 2451Copper A
    Metal bindingi368 – 3681Copper B
    Metal bindingi372 – 3721Copper B
    Metal bindingi408 – 4081Copper B

    GO - Molecular functioni

    1. chloride ion binding Source: UniProtKB
    2. copper ion binding Source: UniProtKB
    3. monophenol monooxygenase activity Source: UniProtKB

    GO - Biological processi

    1. defense response Source: UniProtKB
    2. melanin biosynthetic process from tyrosine Source: UniProtKB
    3. positive regulation of melanization defense response Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenoloxidase subunit 2 (EC:1.14.18.1)
    Alternative name(s):
    proPO-p2
    Gene namesi
    Name:ppoImported
    OrganismiManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
    Taxonomic identifieri7130 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 695694Phenoloxidase subunit 2PRO_0000234111Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi586 ↔ 6301 Publication
    Disulfide bondi588 ↔ 6371 Publication

    Post-translational modificationi

    The N-terminus is blocked.1 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Synthesized by oenocytoids, a type of hemocyte, and released into the hemolymph plasma.1 Publication

    Interactioni

    Subunit structurei

    Heterodimer. Forms a complex with an interleukin 1-like protein as a consequence of a host defense response.3 Publications

    Protein-protein interaction databases

    DIPiDIP-48979N.

    Structurei

    Secondary structure

    1
    695
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Beta strandi19 – 213
    Turni24 – 274
    Beta strandi28 – 314
    Helixi34 – 363
    Helixi39 – 413
    Turni42 – 443
    Helixi45 – 539
    Beta strandi60 – 634
    Helixi76 – 783
    Helixi90 – 10516
    Helixi111 – 12414
    Helixi127 – 14014
    Beta strandi141 – 1433
    Helixi152 – 1554
    Helixi157 – 1593
    Helixi165 – 17511
    Helixi198 – 2025
    Helixi203 – 2064
    Helixi209 – 22113
    Helixi229 – 2324
    Helixi237 – 25721
    Turni258 – 2603
    Turni285 – 2873
    Beta strandi303 – 3053
    Helixi306 – 3083
    Beta strandi310 – 3123
    Helixi314 – 33017
    Beta strandi331 – 3344
    Beta strandi340 – 3423
    Helixi345 – 3539
    Helixi361 – 3644
    Helixi367 – 37610
    Helixi391 – 3933
    Turni395 – 3973
    Helixi398 – 4003
    Helixi402 – 41918
    Turni422 – 4243
    Helixi430 – 4334
    Beta strandi438 – 44710
    Beta strandi454 – 46512
    Helixi467 – 4693
    Beta strandi479 – 4879
    Beta strandi490 – 4989
    Beta strandi504 – 51512
    Helixi524 – 5274
    Turni528 – 5303
    Beta strandi532 – 5409
    Beta strandi543 – 5519
    Helixi552 – 5543
    Helixi561 – 5644
    Beta strandi589 – 5913
    Helixi592 – 5943
    Beta strandi600 – 6023
    Beta strandi604 – 61411
    Helixi615 – 6184
    Helixi634 – 6374
    Turni650 – 6534
    Beta strandi654 – 6563
    Helixi664 – 6674
    Beta strandi673 – 68816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HHSX-ray1.97A2-695[»]
    ProteinModelPortaliQ25519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Sequence Analysis

    Family and domain databases

    Gene3Di1.10.1280.10. 1 hit.
    1.20.1370.10. 1 hit.
    2.60.40.1520. 1 hit.
    InterProiIPR013788. Hemocyanin/hexamerin.
    IPR000896. Hemocyanin/hexamerin_mid_dom.
    IPR005203. Hemocyanin_C.
    IPR005204. Hemocyanin_N.
    IPR014756. Ig_E-set.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PANTHERiPTHR11511. PTHR11511. 1 hit.
    PfamiPF03723. Hemocyanin_C. 1 hit.
    PF00372. Hemocyanin_M. 1 hit.
    PF03722. Hemocyanin_N. 1 hit.
    [Graphical view]
    PRINTSiPR00187. HAEMOCYANIN.
    SUPFAMiSSF48050. SSF48050. 1 hit.
    SSF48056. SSF48056. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
    PS00210. HEMOCYANIN_2. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q25519-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADIFDSFEL LYDRPGEPMI NTKGEDKVLF ELTEQFLTPE YANNGLELNN    50
    RFGDEEEVSR KIILKNLDKI PEFPKAKQLP NDADFSLFLP SHQEMANEVI 100
    DVLMSVTENQ LQELLSTCVY ARINLNPQLF NYCYTVAIMH RRDTGKVRVQ 150
    NYAEIFPAKF LDSQVFTQAR EAAAVIPKTI PRTPIIIPRD YTATDLEEEH 200
    RLAYWREDLG INLHHWHWHL VYPFSASDEK IVAKDRRGEL FFYMHQQIIA 250
    RYNCERLCNS LKRVKKFSDW REPIPEAYYP KLDSLTSARG WPPRQAGMRW 300
    QDLKRPVDGL NVTIDDMERY RRNIEEAIAT GNVILPDKST KKLDIDMLGN 350
    MMEASVLSPN RDLYGSIHNN MHSFSAYMHD PEHRYLESFG VIADEATTMR 400
    DPFFYRVHAW VDDIFQSFKE APHNVRPYSR SQLENPGVQV TSVAVESAGG 450
    QQNVLNTFWM QSDVNLSKGL DFSDRGPVYA RFTHLNHRPF RYVIKANNTA 500
    SARRTTVRIF IAPKTDERNL PWALSDQRKM FIEMDRFVVP LSAGENTITR 550
    QSTESSLTIP FEQTFRDLSI QGSDPRRSEL AAFNYCGCGW PQHMLVPKGT 600
    VGGVAYQLFV MLSNYELDKI EQPDGRELSC VEASMFCGLK DKKYPDARPM 650
    GYPFDRPSNS ATNIEDFSAM SNMGLQDIVI KLSDVTEPNP RNPPA 695
    Length:695
    Mass (Da):80,061
    Last modified:January 23, 2007 - v3
    Checksum:i93DB6D7F2490A386
    GO

    Mass spectrometryi

    Molecular mass is 79791 Da from positions 2 - 695. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42556 mRNA. Translation: AAC37243.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42556 mRNA. Translation: AAC37243.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HHS X-ray 1.97 A 2-695 [» ]
    ProteinModelPortali Q25519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48979N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1280.10. 1 hit.
    1.20.1370.10. 1 hit.
    2.60.40.1520. 1 hit.
    InterProi IPR013788. Hemocyanin/hexamerin.
    IPR000896. Hemocyanin/hexamerin_mid_dom.
    IPR005203. Hemocyanin_C.
    IPR005204. Hemocyanin_N.
    IPR014756. Ig_E-set.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    PANTHERi PTHR11511. PTHR11511. 1 hit.
    Pfami PF03723. Hemocyanin_C. 1 hit.
    PF00372. Hemocyanin_M. 1 hit.
    PF03722. Hemocyanin_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00187. HAEMOCYANIN.
    SUPFAMi SSF48050. SSF48050. 1 hit.
    SSF48056. SSF48056. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00209. HEMOCYANIN_1. 1 hit.
    PS00210. HEMOCYANIN_2. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme, and molecular cloning."
      Hall M., Scott T., Sugumaran M., Soderhall K., Law J.H.
      Proc. Natl. Acad. Sci. U.S.A. 92:7764-7768(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-51 AND 401-406.
      Tissue: Hemocyte1 Publication.
    2. "Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco hornworm, Manduca sexta."
      Beck G., Cardinale S., Wang L., Reiner M., Sugumaran M.
      J. Biol. Chem. 271:11035-11038(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    3. "Subunit composition of pro-phenol oxidase from Manduca sexta: molecular cloning of subunit ProPO-P1."
      Jiang H., Wang Y., Ma C., Kanost M.R.
      Insect Biochem. Mol. Biol. 27:835-850(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: BLOCKAGE OF N-TERMINUS, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
    4. "Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase."
      Yu X.-Q., Gan H., Kanost M.R.
      Insect Biochem. Mol. Biol. 29:585-597(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    5. "Prophenoloxidase binds to the surface of hemocytes and is involved in hemocyte melanization in Manduca sexta."
      Ling E., Yu X.-Q.
      Insect Biochem. Mol. Biol. 35:1356-1366(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes."
      Li Y., Wang Y., Jiang H., Deng J.
      Proc. Natl. Acad. Sci. U.S.A. 106:17002-17006(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH COPPER IONS, COFACTOR, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiPRP2_MANSE
    AccessioniPrimary (citable) accession number: Q25519
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 74 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3