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Protein

Phenoloxidase subunit 1

Gene
N/A
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 bindingi209Copper A1 Publication1
Metal bindingi213Copper A1 Publication1
Metal bindingi239Copper A1 Publication1
Metal bindingi366Copper B1 Publication1
Metal bindingi370Copper B1 Publication1
Metal bindingi406Copper 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 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

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
ChainiPRO_00002341102 – 685Phenoloxidase subunit 1Add BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 7Combined sources4
Helixi8 – 12Combined sources5
Turni24 – 27Combined sources4
Beta strandi28 – 30Combined sources3
Helixi34 – 36Combined sources3
Helixi39 – 44Combined sources6
Helixi45 – 53Combined sources9
Beta strandi57 – 60Combined sources4
Helixi73 – 75Combined sources3
Helixi87 – 102Combined sources16
Helixi106 – 117Combined sources12
Helixi122 – 135Combined sources14
Helixi137 – 139Combined sources3
Helixi147 – 150Combined sources4
Helixi152 – 154Combined sources3
Helixi159 – 170Combined sources12
Helixi192 – 196Combined sources5
Helixi197 – 200Combined sources4
Helixi203 – 215Combined sources13
Helixi223 – 226Combined sources4
Helixi231 – 252Combined sources22
Turni279 – 282Combined sources4
Beta strandi297 – 299Combined sources3
Helixi300 – 302Combined sources3
Beta strandi304 – 306Combined sources3
Helixi308 – 324Combined sources17
Beta strandi326 – 328Combined sources3
Beta strandi334 – 336Combined sources3
Turni339 – 341Combined sources3
Helixi342 – 351Combined sources10
Helixi359 – 362Combined sources4
Helixi365 – 374Combined sources10
Turni375 – 377Combined sources3
Helixi389 – 391Combined sources3
Turni393 – 395Combined sources3
Helixi396 – 398Combined sources3
Helixi400 – 417Combined sources18
Helixi425 – 428Combined sources4
Beta strandi433 – 440Combined sources8
Beta strandi447 – 458Combined sources12
Turni460 – 462Combined sources3
Beta strandi472 – 480Combined sources9
Beta strandi484 – 491Combined sources8
Beta strandi493 – 495Combined sources3
Beta strandi497 – 509Combined sources13
Helixi518 – 521Combined sources4
Helixi522 – 524Combined sources3
Beta strandi526 – 535Combined sources10
Beta strandi537 – 545Combined sources9
Helixi546 – 548Combined sources3
Beta strandi550 – 553Combined sources4
Helixi555 – 557Combined sources3
Beta strandi583 – 585Combined sources3
Helixi586 – 588Combined sources3
Beta strandi598 – 608Combined sources11
Helixi609 – 611Combined sources3
Helixi626 – 629Combined sources4
Turni642 – 645Combined sources4
Beta strandi646 – 648Combined sources3
Helixi657 – 660Combined sources4
Beta strandi665 – 679Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HHSX-ray1.97B2-685[»]
ProteinModelPortaliO44249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48978N.

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 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: January 20, 2016
This is version 76 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

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.