Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q25519

- PRP2_MANSE

UniProt

Q25519 - PRP2_MANSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
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 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
Complete GO annotation...

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

        10         20         30         40         50
MADIFDSFEL LYDRPGEPMI NTKGEDKVLF ELTEQFLTPE YANNGLELNN
60 70 80 90 100
RFGDEEEVSR KIILKNLDKI PEFPKAKQLP NDADFSLFLP SHQEMANEVI
110 120 130 140 150
DVLMSVTENQ LQELLSTCVY ARINLNPQLF NYCYTVAIMH RRDTGKVRVQ
160 170 180 190 200
NYAEIFPAKF LDSQVFTQAR EAAAVIPKTI PRTPIIIPRD YTATDLEEEH
210 220 230 240 250
RLAYWREDLG INLHHWHWHL VYPFSASDEK IVAKDRRGEL FFYMHQQIIA
260 270 280 290 300
RYNCERLCNS LKRVKKFSDW REPIPEAYYP KLDSLTSARG WPPRQAGMRW
310 320 330 340 350
QDLKRPVDGL NVTIDDMERY RRNIEEAIAT GNVILPDKST KKLDIDMLGN
360 370 380 390 400
MMEASVLSPN RDLYGSIHNN MHSFSAYMHD PEHRYLESFG VIADEATTMR
410 420 430 440 450
DPFFYRVHAW VDDIFQSFKE APHNVRPYSR SQLENPGVQV TSVAVESAGG
460 470 480 490 500
QQNVLNTFWM QSDVNLSKGL DFSDRGPVYA RFTHLNHRPF RYVIKANNTA
510 520 530 540 550
SARRTTVRIF IAPKTDERNL PWALSDQRKM FIEMDRFVVP LSAGENTITR
560 570 580 590 600
QSTESSLTIP FEQTFRDLSI QGSDPRRSEL AAFNYCGCGW PQHMLVPKGT
610 620 630 640 650
VGGVAYQLFV MLSNYELDKI EQPDGRELSC VEASMFCGLK DKKYPDARPM
660 670 680 690
GYPFDRPSNS ATNIEDFSAM SNMGLQDIVI KLSDVTEPNP RNPPA
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