ID   PRP2_BOMMO              Reviewed;         693 AA.
AC   Q27452;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   05-MAY-2009, entry version 53.
DE   RecName: Full=Phenoloxidase subunit 2;
DE            EC=1.14.18.1;
DE   AltName: Full=Tyrosinase 2;
DE   AltName: Full=PO 2;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Kinshu X Showa; TISSUE=Hemocyte;
RX   MEDLINE=95372362; PubMed=7644494; DOI=10.1073/pnas.92.17.7774;
RA   Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.;
RT   "Molecular cloning of insect pro-phenol oxidase: a copper-containing
RT   protein homologous to arthropod hemocyanin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Asano T., Ashida M.;
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   MASS SPECTROMETRY.
RC   TISSUE=Hemocyte;
RX   MEDLINE=95314310; PubMed=7793973; DOI=10.1006/abbi.1995.1337;
RA   Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.;
RT   "Reexamination of properties of phenoloxidase isolated from larval
RT   hemolymph of the silkworm Bombyx mori.";
RL   Arch. Biochem. Biophys. 320:14-23(1995).
CC   -!- FUNCTION: This is a copper-containing oxidase that functions in
CC       the formation of pigments such as melanins and other polyphenolic
CC       compounds. Catalyzes the rate-limiting conversions of tyrosine to
CC       DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to
CC       indole-5'6 quinone.
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O(2) = L-dopa +
CC       dopaquinone + H(2)O.
CC   -!- COFACTOR: Binds 2 copper ions per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized by hemocytes and released into the
CC       hemolymph plasma.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MASS SPECTROMETRY: Mass=81105; Method=MALDI; Range=52-693;
CC       Source=PubMed:7793973;
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
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DR   EMBL; D49371; BAA08369.1; -; mRNA.
DR   EMBL; AB048762; BAB41101.1; -; mRNA.
DR   RefSeq; NP_001037534.1; -.
DR   UniGene; Bmo.1389; -.
DR   HSSP; P04253; 1OXY.
DR   GeneID; 693073; -.
DR   BRENDA; 1.14.18.1; 252.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:monophenol monooxygenase activity; TAS:UniProtKB.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; TAS:UniProtKB.
DR   GO; GO:0006583; P:melanin biosynthetic process from tyrosine; TAS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR008922; Di-copper_centre.
DR   InterPro; IPR013788; Hemocyanin.
DR   InterPro; IPR005203; Hemocyanin_C.
DR   InterPro; IPR000896; Hemocyanin_Cu.
DR   InterPro; IPR005204; Hemocyanin_N.
DR   InterPro; IPR002227; Tyrosinase.
DR   Gene3D; G3DSA:1.10.1280.10; Di-copper_centre; 1.
DR   Gene3D; G3DSA:2.60.40.1520; hemocyanin_C; 1.
DR   Gene3D; G3DSA:1.20.1370.10; hemocyanin_N; 1.
DR   PANTHER; PTHR11511; Hemocyanin; 1.
DR   Pfam; PF03723; Hemocyanin_C; 1.
DR   Pfam; PF00372; Hemocyanin_M; 1.
DR   Pfam; PF03722; Hemocyanin_N; 1.
DR   PRINTS; PR00187; HAEMOCYANIN.
DR   PROSITE; PS00209; HEMOCYANIN_1; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00497; TYROSINASE_1; FALSE_NEG.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Glycoprotein; Melanin biosynthesis;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Secreted; Zymogen.
FT   PROPEP        1     51
FT                                /FTId=PRO_0000035901.
FT   CHAIN        52    693       Phenoloxidase subunit 2.
FT                                /FTId=PRO_0000035902.
FT   METAL       213    213       Copper A (By similarity).
FT   METAL       217    217       Copper A (By similarity).
FT   METAL       243    243       Copper A (By similarity).
FT   METAL       366    366       Copper B (By similarity).
FT   METAL       370    370       Copper B (By similarity).
FT   METAL       406    406       Copper B (By similarity).
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     64     64       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    462    462       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    494    494       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    680    680       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    433    433       P -> Q (in Ref. 1; AA sequence).
SQ   SEQUENCE   693 AA;  80119 MW;  013114DF4CC1A926 CRC64;
     MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI
     PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR
     VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR
     IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF
     YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD
     LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE
     LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA
     YVRPYTRSEL ENPGVQVRSV SVETPGGQPN TLNTFWMLSD VNLSRGLDFS DNGPVYARFT
     HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA
     GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG
     MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS
     LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV
//