Reviewed, UniProtKB/Swiss-Prot O44249 (PRP1_MANSE)

Names and origin

Protein names	Recommended name:     Phenoloxidase subunit 1     EC=1.14.18.1 Alternative name(s):     proPO-P1
Organism	Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier	7130 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Sphingidae › Sphinginae › Sphingini › Manduca

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.4 Ref.1
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O. Ref.1
Cofactor	Binds 2 copper ions per subunit By similarity. UniProtKB P04253
Enzyme regulation	Activated by immulectin and lipopolysaccharide. Ref.3
Subunit structure	Heterodimer. Forms a complex with an interleukin 1-like protein as a consequence of a host defense response. Ref.1 Ref.2
Subcellular location	Secreted. Ref.1
Tissue specificity	Synthesized by oenocytoids, a type of hemocyte, and released into the hemolymph plasma. Ref.1
Post-translational modification	The N-terminus is blocked. Ref.1
Sequence similarities	Belongs to the tyrosinase family.
Mass spectrometry	Molecular mass is 78904 Da from positions 2 - 685. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	defense response Ref.1 Non-traceable author statement. Source: UniProtKB melanin biosynthetic process from tyrosine Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of melanization defense response Ref.4 Inferred from direct assay. Source: UniProtKB transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	chloride ion binding Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB monophenol monooxygenase activity Ref.1 Traceable author statement. Source: UniProtKB oxygen transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable Ref.1
	Chain	2 – 685	684	Phenoloxidase subunit 1 Ref.1		PRO_0000234110
Sites
	Metal binding	209	1	Copper A By similarity UniProtKB P04253
	Metal binding	213	1	Copper A By similarity UniProtKB P04253
	Metal binding	239	1	Copper A By similarity UniProtKB P04253
	Metal binding	366	1	Copper B By similarity UniProtKB P04253
	Metal binding	370	1	Copper B By similarity UniProtKB P04253
	Metal binding	406	1	Copper B By similarity UniProtKB P04253

Sequences

	Sequence		Length	Mass (Da)
	O44249-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BE5811D145302583	FASTA	685	78,966
	10 20 30 40 50 60 MTDAKNNLLY FFDRPNEPCF MQKGEDKVVF EIPDHYYPDK YKSLSNTLSN RFGNEATKRI 70 80 90 100 110 120 PIRNITLPNL EVPMQLPYND QFSLFVPKHR TMAAKLIDIF MGMRDVEDLQ SVCSYCQLRI 130 140 150 160 170 180 NPYMFNYCLS VAILHRPDTK GLSIPTFAET FPDKFMDSKV FLRAREVSNV VISGSRMPVN 190 200 210 220 230 240 VPINYTANTT EPEQRVAYFR EDIGINLHHW HWHLVYPFDS ADRSIVNKDR RGELFYYMHQ 250 260 270 280 290 300 QIIGRYNVER MCNGLPQVKP FSDFSAPIEE GYFPKLDSQV ASRTWPPRFA GSVFRNLDRT 310 320 330 340 350 360 VDQVKIDVRK LFTWRDQFLE AIQKMAIKMP NGRELPLDEV TGIDMLGNLM ESSIISPNRG 370 380 390 400 410 420 YYGDLHNMGH VFAAYTHDPD HRHLEQFGVM GDSATAMRDP FFYRWHRFVD DVFNIYKEKL 430 440 450 460 470 480 TPYTNERLDF PGVRVSSVGI EGARPNTLRT LWQQSTVELG RGLDFTPRGS VLARFTHLQH 490 500 510 520 530 540 DEFQYVIEVN NTTGGNLMGT VRIFMAPKVD DNGQPMSFNK QRRLMIELDK FSQALRPGTN 550 560 570 580 590 600 TIRRRSVDSS VTIPYERTFR NQSERPGDPG TAGAAEFDFC GCGWPHHMLI PKGTAQGYPV 610 620 630 640 650 660 VLFVMISNWN NDRIEQDLVG SCNDAASYCG IRDRKYPDKQ AMGYPFDRKM ANDAATLSDF 670 680 LRPNMAVRDC SIQFSDTTVE RGQQG

References

[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: 9474780] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BLOCKAGE OF N-TERMINUS, MASS SPECTROMETRY. Tissue: Hemocyte.
[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: 8626641] [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: 10436935] [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: 16291091] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF003253 mRNA. Translation: AAC05796.1.
3D structure databases
HSSP	HSSP built from PDB template 1OXY based on UniProtKB P04253.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.18.1. 15145.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR013788. Hemocyanin. IPR005203. Hemocyanin_C. IPR000896. Hemocyanin_Cu. IPR005204. Hemocyanin_N. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit. G3DSA:2.60.40.1520. hemocyanin_C. 1 hit. G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.
PANTHER	PTHR11511. Hemocyanin. 1 hit.
Pfam	PF03723. Hemocyanin_C. 1 hit. PF00372. Hemocyanin_M. 1 hit. PF03722. Hemocyanin_N. 1 hit. [Graphical view]
PRINTS	PR00187. HAEMOCYANIN.
PROSITE	PS00209. HEMOCYANIN_1. 1 hit. PS00210. HEMOCYANIN_2. 1 hit. PS00497. TYROSINASE_1. False negative. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRP1_MANSE

Accession

Primary (citable) accession number: O44249

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 51 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)