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Q27451

- PRP1_BOMMO

UniProt

Q27451 - PRP1_BOMMO

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Protein

Phenoloxidase subunit 1

Gene
N/A
Organism
Bombyx mori (Silk moth)
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.

Catalytic activityi

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

Cofactori

Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Copper ABy similarity
Metal bindingi213 – 2131Copper ABy similarity
Metal bindingi239 – 2391Copper ABy similarity
Metal bindingi366 – 3661Copper BBy similarity
Metal bindingi370 – 3701Copper BBy similarity
Metal bindingi406 – 4061Copper BBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB

GO - Biological processi

  1. defense response Source: UniProtKB
  2. melanin biosynthetic process from tyrosine 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):
PO 1
Tyrosinase 1
OrganismiBombyx mori (Silk moth)Imported
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
ProteomesiUP000005204: Unplaced

Subcellular locationi

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
Propeptidei1 – 51511 PublicationPRO_0000035899Add
BLAST
Chaini52 – 685634Phenoloxidase subunit 1PRO_0000035900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi581 ↔ 623By similarity
Disulfide bondi583 ↔ 630By similarity

Post-translational modificationi

The N-terminus is blocked.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Synthesized by hemocytes and released into the hemolymph plasma.1 Publication

Interactioni

Subunit structurei

Heterodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ27451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

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.

Q27451-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDAKNNLLL FFDRPSEPCF MQKGEENAVF EIPDNYYPEK YQRVSNAIGN
60 70 80 90 100
RFGSDAGRMI PIRNIALPNL DLPMELPYNE QFSLFVPKHR KLAGRLIDIF
110 120 130 140 150
MGMRDVEDLQ SVCSYCQLRI NPYMFNYCLS VAILHRPDTK GLSIPTFAES
160 170 180 190 200
FPDKFMDPKV FRQAREVSSV VPSGARMPIV IPSNYTASDT EPEQRVAYFR
210 220 230 240 250
EDIGINLHHW HWHLVYPFDA ADRAIVNKDR RGELFYYMHQ QIIARYNVER
260 270 280 290 300
MCNNLSRVRR YNNFRAAIEE GYFPKLDSTV ASRAWPPRFA GTTIRDLDRP
310 320 330 340 350
VDQIRSDVSE LETWRDRFLQ AIENMSVMLP NGRQLPLDEE TGIDVLGNLM
360 370 380 390 400
ESSIISRNRP YYGDLHNMGH VFISYSHDPD HRHLEQFGVM GDSATAMRDP
410 420 430 440 450
VFYRWHAYID DIFHLYKYKL TPYGNDRLDF PNIRVSSVSI EGGGTPNTLN
460 470 480 490 500
TLWEQSTVDL GRGMDFTPRG SVLARFTHLQ HDEYNYVIEV NNTGGSSVMG
510 520 530 540 550
MFRIFIAPTV DESGKPFSFD EQRKLMIELD KFSQGVKPGN NTIRRKSIDS
560 570 580 590 600
SVTIPYERTF RNQADRPADP GTAGAAEFDF CGCGWPHHML VPKGTTQGYP
610 620 630 640 650
MVLFVMVSNW NDDRVEQDLV GSCNDAASYC GIRDRKYPDR RAMGFPFDRP
660 670 680
APAATTLSDF LRPNMAVRDC IVRFTDRTRQ RGQQG
Length:685
Mass (Da):78,785
Last modified:January 1, 1999 - v2
Checksum:i9DE93E0760DD353C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711V → A AA sequence (PubMed:7644494)Curated

Mass spectrometryi

Molecular mass is 78880 Da from positions 52 - 685. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49370 mRNA. Translation: BAA08368.1.
RefSeqiNP_001037335.1. NM_001043870.1.
UniGeneiBmo.344.

Genome annotation databases

GeneIDi692758.
KEGGibmor:692758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49370 mRNA. Translation: BAA08368.1 .
RefSeqi NP_001037335.1. NM_001043870.1.
UniGenei Bmo.344.

3D structure databases

ProteinModelPortali Q27451.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 692758.
KEGGi bmor:692758.

Organism-specific databases

CTDi 37044.

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. "Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin."
    Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.
    Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Kinshu X Showa1 Publication.
    Tissue: Hemocyte1 Publication.
  2. "Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori."
    Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.
    Arch. Biochem. Biophys. 320:14-23(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Hemocyte1 Publication.

Entry informationi

Entry nameiPRP1_BOMMO
AccessioniPrimary (citable) accession number: Q27451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1999
Last modified: October 29, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3