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O44249

- PRP1_MANSE

UniProt

O44249 - PRP1_MANSE

Protein

Phenoloxidase subunit 1

Gene
N/A
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 bindingi209 – 2091Copper A
    Metal bindingi213 – 2131Copper A
    Metal bindingi239 – 2391Copper A
    Metal bindingi366 – 3661Copper B
    Metal bindingi370 – 3701Copper B
    Metal bindingi406 – 4061Copper 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 1 (EC:1.14.18.1)
    Alternative name(s):
    proPO-P1
    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 – 685684Phenoloxidase subunit 1PRO_0000234110Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi580 ↔ 6221 Publication
    Disulfide bondi582 ↔ 6291 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-48978N.

    Structurei

    Secondary structure

    1
    685
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Helixi8 – 125
    Turni24 – 274
    Beta strandi28 – 303
    Helixi34 – 363
    Helixi39 – 446
    Helixi45 – 539
    Beta strandi57 – 604
    Helixi73 – 753
    Helixi87 – 10216
    Helixi106 – 11712
    Helixi122 – 13514
    Helixi137 – 1393
    Helixi147 – 1504
    Helixi152 – 1543
    Helixi159 – 17012
    Helixi192 – 1965
    Helixi197 – 2004
    Helixi203 – 21513
    Helixi223 – 2264
    Helixi231 – 25222
    Turni279 – 2824
    Beta strandi297 – 2993
    Helixi300 – 3023
    Beta strandi304 – 3063
    Helixi308 – 32417
    Beta strandi326 – 3283
    Beta strandi334 – 3363
    Turni339 – 3413
    Helixi342 – 35110
    Helixi359 – 3624
    Helixi365 – 37410
    Turni375 – 3773
    Helixi389 – 3913
    Turni393 – 3953
    Helixi396 – 3983
    Helixi400 – 41718
    Helixi425 – 4284
    Beta strandi433 – 4408
    Beta strandi447 – 45812
    Turni460 – 4623
    Beta strandi472 – 4809
    Beta strandi484 – 4918
    Beta strandi493 – 4953
    Beta strandi497 – 50913
    Helixi518 – 5214
    Helixi522 – 5243
    Beta strandi526 – 53510
    Beta strandi537 – 5459
    Helixi546 – 5483
    Beta strandi550 – 5534
    Helixi555 – 5573
    Beta strandi583 – 5853
    Helixi586 – 5883
    Beta strandi598 – 60811
    Helixi609 – 6113
    Helixi626 – 6294
    Turni642 – 6454
    Beta strandi646 – 6483
    Helixi657 – 6604
    Beta strandi665 – 67915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HHSX-ray1.97B2-685[»]
    ProteinModelPortaliO44249.
    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.

    O44249-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDAKNNLLY FFDRPNEPCF MQKGEDKVVF EIPDHYYPDK YKSLSNTLSN    50
    RFGNEATKRI PIRNITLPNL EVPMQLPYND QFSLFVPKHR TMAAKLIDIF 100
    MGMRDVEDLQ SVCSYCQLRI NPYMFNYCLS VAILHRPDTK GLSIPTFAET 150
    FPDKFMDSKV FLRAREVSNV VISGSRMPVN VPINYTANTT EPEQRVAYFR 200
    EDIGINLHHW HWHLVYPFDS ADRSIVNKDR RGELFYYMHQ QIIGRYNVER 250
    MCNGLPQVKP FSDFSAPIEE GYFPKLDSQV ASRTWPPRFA GSVFRNLDRT 300
    VDQVKIDVRK LFTWRDQFLE AIQKMAIKMP NGRELPLDEV TGIDMLGNLM 350
    ESSIISPNRG YYGDLHNMGH VFAAYTHDPD HRHLEQFGVM GDSATAMRDP 400
    FFYRWHRFVD DVFNIYKEKL TPYTNERLDF PGVRVSSVGI EGARPNTLRT 450
    LWQQSTVELG RGLDFTPRGS VLARFTHLQH DEFQYVIEVN NTTGGNLMGT 500
    VRIFMAPKVD DNGQPMSFNK QRRLMIELDK FSQALRPGTN TIRRRSVDSS 550
    VTIPYERTFR NQSERPGDPG TAGAAEFDFC GCGWPHHMLI PKGTAQGYPV 600
    VLFVMISNWN NDRIEQDLVG SCNDAASYCG IRDRKYPDKQ AMGYPFDRKM 650
    ANDAATLSDF LRPNMAVRDC SIQFSDTTVE RGQQG 685
    Length:685
    Mass (Da):78,966
    Last modified:January 23, 2007 - v3
    Checksum:iBE5811D145302583
    GO

    Mass spectrometryi

    Molecular mass is 78904 Da from positions 2 - 685. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003253 mRNA. Translation: AAC05796.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003253 mRNA. Translation: AAC05796.1 .

    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 B 2-685 [» ]
    ProteinModelPortali O44249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48978N.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BLOCKAGE OF N-TERMINUS, MASS SPECTROMETRY.
      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. "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.
    4. "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.
    5. "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 nameiPRP1_MANSE
    AccessioniPrimary (citable) accession number: O44249
    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

    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