Reviewed, UniProtKB/Swiss-Prot Q9V521 (PRPP1_DROME)

Names and origin

Protein names

Recommended name:
    Probable phenoloxidase subunit CG8193
    EC=1.14.18.1

Gene names

ORF Names:

CG8193

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	684 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.
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity. UniProtKB Q27451
Subcellular location	Secreted. Ref.4
Sequence similarities	Belongs to the tyrosinase family.
Sequence caution	The sequence BAB43866.1 differs from that shown. Reason: Miscellaneous discrepancy. Chimeric cDNA. It is a chimera between Dox-A3 and CG8193.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	melanin biosynthetic process from tyrosine Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC 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
	Propeptide	1 – 50	50	Ref.4		PRO_0000035907
	Chain	51 – 684	634	Probable phenoloxidase subunit CG8193 Ref.4		PRO_0000035908
Sites
	Metal binding	208	1	Copper A By similarity UniProtKB Q27451
	Metal binding	212	1	Copper A By similarity UniProtKB Q27451
	Metal binding	238	1	Copper A By similarity UniProtKB Q27451
	Metal binding	365	1	Copper B By similarity UniProtKB Q27451
	Metal binding	369	1	Copper B By similarity UniProtKB Q27451
	Metal binding	405	1	Copper B By similarity UniProtKB Q27451
Amino acid modifications
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
	Glycosylation	492	1	N-linked (GlcNAc...) Potential
	Glycosylation	665	1	N-linked (GlcNAc...) Potential
	Glycosylation	677	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9V521-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 16F946FFEEDB72EA	FASTA	684	79,285
	10 20 30 40 50 60 MADKKNLLLL FDHPTEPVFM DKGKRVTVFD VPDSFLTDRY RPISNEVQSR VGDKVEQRVP 70 80 90 100 110 120 VREISIPDLR IPMSLGRDEQ FSLFLPKHRR IAGRLIDIFM NMRSVDDLQS VAVYARDRVN 130 140 150 160 170 180 PVLFNYALSV ALLHRPDTQG LDLPSFSQTF PDRFIDSQVI RKMREESFVV QPGSRMPITI 190 200 210 220 230 240 PRDYTASDLD PEHRLWYFRE DLGINLHHWH WHLVYPFEAS DRSIVAKDRR GELFYYMHQQ 250 260 270 280 290 300 VIARYNAERF SNNLARVLPF NNLRDPIAEG YFPKMDSLVA SRAWPPRFES TRLSDLNRES 310 320 330 340 350 360 DQLNVEIGDL ERWRDRIYEA IHQGFVMDER GNRVPLDEAT GIDTLGNMIE SSILSPNRVL 370 380 390 400 410 420 YGDLHNNGHT FISYAHDPTS KHLESFGVMG DVSTAMRDPV FYKWHSYIDR IFQEHKSRLP 430 440 450 460 470 480 AYTENQLNYP GVSIAGIQVD TNGGRPNNLT TFWQQSDVDM SRGFDFLPRG NVFARFTHLQ 490 500 510 520 530 540 HLPFTYTISL NNDSGAQRFG YVRIFMAPKN DERGQPMLMR DQRSMMIELD KFVTSLNPGP 550 560 570 580 590 600 NTIRRRSTES SVTIPFERTF RNLDANRPAA GTPEELEFNF CGCGWPNHML VPKGLPEGLQ 610 620 630 640 650 660 CVLFIMVSNY ENDRIDQQLV GRCSDAASYC GVRDRLYPDR QSMGFPFDRL PRSGVDRLVN 670 680 FLTPNMSIVD VNIRHENRTV QRPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[4]	"Prophenol oxidase A3 in Drosophila melanogaster: activation and the PCR-based cDNA sequence." Asada N., Yokoyama G., Kawamoto N., Norioka S., Hatta T. Biochem. Genet. 41:151-163(2003) [PubMed: 12834045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-670, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION. Strain: Oregon-R. Tissue: Larva and Pupae.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF59001.1. AY060652 mRNA. Translation: AAL28200.1. AB055857 Genomic DNA. Translation: BAB43866.1. Sequence problems.
RefSeq	NP_610443.1.
UniGene	Dm.538
3D structure databases
HSSP	HSSP built from PDB template 1OXY based on UniProtKB P04253.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V521. 3 interactions.
Proteomic databases
PRIDE	Q9V521.
Genome annotation databases
Ensembl	FBgn0033367. Drosophila melanogaster. [Contig view]
GeneID	35910.
KEGG	dme:Dmel_CG8193.
NMPDR	fig|7227.3.peg.3987.
Organism-specific databases
FlyBase	FBgn0033367. CG8193.
Phylogenomic databases
HOGENOM	Q9V521.
OMA	Q9V521. RLIDIFM.
Enzyme and pathway databases
BRENDA	1.14.18.1. 48.
Gene expression databases
ArrayExpress	Q9V521.
GermOnline	CG8193. Drosophila melanogaster.
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...
Other Resources
NextBio	795776.

Entry information

Entry name

PRPP1_DROME

Accession

Primary (citable) accession number: Q9V521
Secondary accession number(s): Q9BLD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project