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Protein

Phenoloxidase subunit 2

Gene

ppo

Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed-Annotation score: 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.Curated1 Publication

Catalytic activityi

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

Cofactori

Cu2+1 PublicationNote: Binds 2 copper ions per subunit.1 Publication

Enzyme regulationi

Activated by immulectin and lipopolysaccharide.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi215Copper A1 Publication1
Metal bindingi219Copper A1 Publication1
Metal bindingi245Copper A1 Publication1
Metal bindingi368Copper B1 Publication1
Metal bindingi372Copper B1 Publication1
Metal bindingi408Copper B1 Publication1

GO - Molecular functioni

  • chloride ion binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • monophenol monooxygenase activity Source: UniProtKB

GO - Biological processi

  • defense response Source: UniProtKB
  • melanin biosynthetic process from tyrosine Source: UniProtKB
  • 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

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
ChainiPRO_00002341112 – 695Phenoloxidase subunit 2Add BLAST694

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1695
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Beta strandi19 – 21Combined sources3
Turni24 – 27Combined sources4
Beta strandi28 – 31Combined sources4
Helixi34 – 36Combined sources3
Helixi39 – 41Combined sources3
Turni42 – 44Combined sources3
Helixi45 – 53Combined sources9
Beta strandi60 – 63Combined sources4
Helixi76 – 78Combined sources3
Helixi90 – 105Combined sources16
Helixi111 – 124Combined sources14
Helixi127 – 140Combined sources14
Beta strandi141 – 143Combined sources3
Helixi152 – 155Combined sources4
Helixi157 – 159Combined sources3
Helixi165 – 175Combined sources11
Helixi198 – 202Combined sources5
Helixi203 – 206Combined sources4
Helixi209 – 221Combined sources13
Helixi229 – 232Combined sources4
Helixi237 – 257Combined sources21
Turni258 – 260Combined sources3
Turni285 – 287Combined sources3
Beta strandi303 – 305Combined sources3
Helixi306 – 308Combined sources3
Beta strandi310 – 312Combined sources3
Helixi314 – 330Combined sources17
Beta strandi331 – 334Combined sources4
Beta strandi340 – 342Combined sources3
Helixi345 – 353Combined sources9
Helixi361 – 364Combined sources4
Helixi367 – 376Combined sources10
Helixi391 – 393Combined sources3
Turni395 – 397Combined sources3
Helixi398 – 400Combined sources3
Helixi402 – 419Combined sources18
Turni422 – 424Combined sources3
Helixi430 – 433Combined sources4
Beta strandi438 – 447Combined sources10
Beta strandi454 – 465Combined sources12
Helixi467 – 469Combined sources3
Beta strandi479 – 487Combined sources9
Beta strandi490 – 498Combined sources9
Beta strandi504 – 515Combined sources12
Helixi524 – 527Combined sources4
Turni528 – 530Combined sources3
Beta strandi532 – 540Combined sources9
Beta strandi543 – 551Combined sources9
Helixi552 – 554Combined sources3
Helixi561 – 564Combined sources4
Beta strandi589 – 591Combined sources3
Helixi592 – 594Combined sources3
Beta strandi600 – 602Combined sources3
Beta strandi604 – 614Combined sources11
Helixi615 – 618Combined sources4
Helixi634 – 637Combined sources4
Turni650 – 653Combined sources4
Beta strandi654 – 656Combined sources3
Helixi664 – 667Combined sources4
Beta strandi673 – 688Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HHSX-ray1.97A2-695[»]
ProteinModelPortaliQ25519.
SMRiQ25519.
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:
EMBLi
GenBanki
DDBJi
Links Updated
L42556 mRNA. Translation: AAC37243.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42556 mRNA. Translation: AAC37243.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HHSX-ray1.97A2-695[»]
ProteinModelPortaliQ25519.
SMRiQ25519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48979N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 77 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

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 one 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.