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O44249

- PRP1_MANSE

UniProt

O44249 - PRP1_MANSE

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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

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

Cu2+1 PublicationNote: 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
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):
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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTDAKNNLLY FFDRPNEPCF MQKGEDKVVF EIPDHYYPDK YKSLSNTLSN
60 70 80 90 100
RFGNEATKRI PIRNITLPNL EVPMQLPYND QFSLFVPKHR TMAAKLIDIF
110 120 130 140 150
MGMRDVEDLQ SVCSYCQLRI NPYMFNYCLS VAILHRPDTK GLSIPTFAET
160 170 180 190 200
FPDKFMDSKV FLRAREVSNV VISGSRMPVN VPINYTANTT EPEQRVAYFR
210 220 230 240 250
EDIGINLHHW HWHLVYPFDS ADRSIVNKDR RGELFYYMHQ QIIGRYNVER
260 270 280 290 300
MCNGLPQVKP FSDFSAPIEE GYFPKLDSQV ASRTWPPRFA GSVFRNLDRT
310 320 330 340 350
VDQVKIDVRK LFTWRDQFLE AIQKMAIKMP NGRELPLDEV TGIDMLGNLM
360 370 380 390 400
ESSIISPNRG YYGDLHNMGH VFAAYTHDPD HRHLEQFGVM GDSATAMRDP
410 420 430 440 450
FFYRWHRFVD DVFNIYKEKL TPYTNERLDF PGVRVSSVGI EGARPNTLRT
460 470 480 490 500
LWQQSTVELG RGLDFTPRGS VLARFTHLQH DEFQYVIEVN NTTGGNLMGT
510 520 530 540 550
VRIFMAPKVD DNGQPMSFNK QRRLMIELDK FSQALRPGTN TIRRRSVDSS
560 570 580 590 600
VTIPYERTFR NQSERPGDPG TAGAAEFDFC GCGWPHHMLI PKGTAQGYPV
610 620 630 640 650
VLFVMISNWN NDRIEQDLVG SCNDAASYCG IRDRKYPDKQ AMGYPFDRKM
660 670 680
ANDAATLSDF LRPNMAVRDC SIQFSDTTVE RGQQG
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF003253 mRNA. Translation: AAC05796.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003253 mRNA. Translation: AAC05796.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 75 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