ID Q49I39_TRICA Unreviewed; 682 AA.
AC Q49I39;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Phenoloxidase subunit A3-like Protein {ECO:0000313|EMBL:EEZ99189.1};
DE SubName: Full=Pro-phenol oxidase subunit 1 {ECO:0000313|EMBL:AAX84204.1};
DE EC=1.10.3.1 {ECO:0000313|EMBL:AAX84204.1};
DE EC=1.14.18.1 {ECO:0000313|EMBL:AAX84204.1};
GN Name=AUGUSTUS-3.0.2_00325 {ECO:0000313|EMBL:EEZ99189.1};
GN ORFNames=TcasGA2_TC000325 {ECO:0000313|EMBL:EEZ99189.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:AAX84204.1};
RN [1] {ECO:0000313|EMBL:AAX84204.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16076951; DOI=10.1073/pnas.0504982102;
RA Arakane Y., Muthukrishnan S., Beeman R.W., Kanost M.R., Kramer K.J.;
RT "Laccase 2 is the phenoloxidase gene required for beetle cuticle tanning.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11337-11342(2005).
RN [2] {ECO:0000313|EMBL:EEZ99189.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ99189.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [3] {ECO:0000313|EMBL:EEZ99189.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ99189.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
RN [4] {ECO:0000313|EMBL:EEZ99189.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ99189.1};
RA Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT super scaffolding tool.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; AY884063; AAX84204.1; -; mRNA.
DR EMBL; KQ971312; EEZ99189.1; -; Genomic_DNA.
DR RefSeq; NP_001034493.1; NM_001039404.1.
DR AlphaFoldDB; Q49I39; -.
DR STRING; 7070.Q49I39; -.
DR EnsemblMetazoa; TC000325_001; TC000325_001; TC000325.
DR GeneID; 641512; -.
DR KEGG; tca:641512; -.
DR CTD; 47211; -.
DR eggNOG; ENOG502QQCG; Eukaryota.
DR HOGENOM; CLU_012213_0_1_1; -.
DR OMA; LMHRRDT; -.
DR OrthoDB; 5406463at2759; -.
DR Proteomes; UP000007266; Linkage group 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006582; P:melanin metabolic process; IEA:UniProt.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR013788; Hemocyanin/hexamerin.
DR InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR InterPro; IPR005203; Hemocyanin_C.
DR InterPro; IPR037020; Hemocyanin_C_sf.
DR InterPro; IPR005204; Hemocyanin_N.
DR InterPro; IPR036697; Hemocyanin_N_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 1.
DR PANTHER; PTHR11511:SF4; PHENOLOXIDASE 2-RELATED; 1.
DR Pfam; PF03723; Hemocyanin_C; 1.
DR Pfam; PF00372; Hemocyanin_M; 1.
DR Pfam; PF03722; Hemocyanin_N; 1.
DR PRINTS; PR00187; HAEMOCYANIN.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00209; HEMOCYANIN_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAX84204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 396..407
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 682 AA; 79101 MW; 3D066B42B6414FF5 CRC64;
MTDKSKLLLL FDRPQEPAFM PKGNKEVFDV PNNFLPERYK PIGVQIANRF GEQANEKIPL
KDITPPDLEG ILDLGRHENF SLFIPKHRKV AGKLIRIFLA AESIDDLLSN AVFCRDRVNP
YLFYYAFSVA LLHRPDTQNL DLPSFIHVFP DKYVDSQVFA RAREEAHIVP EGSRTPIEIP
QDFTASDLDE EHRVAYWRED IGLNLHHWHW HLVYPFEGAR EIVDKNRRGE IFYYMHQQII
ARFNIERLCN GLKRVVKLSN WREPLPEAYF PKLDSLVASR TWPARPVNQV PRDLNREVDQ
IRLSLDDMDR WRDRIYDAIH SGVVRGDNGQ NIPLTEFEGI DVLGNIIESS ILSPNRNYYG
DFHNMGHILI GYIHDPDHRF LEPFGVMADP AVDLRDPLFF RWHAYIDDMF QEFKATLPRY
TVAQLNYPGV TVTNIEVQAK GGKPNVLSTF WQQSDLDLSR GLDFQPRGSV FVRFTHLQNQ
DFTYKITVNN SGNNRMGTCR IFLAPQFDER GNPWLFRNQK DMFIELDRFA VSLKQGTNTI
TRHSTESSLT IPFERTFRNL DANRPTGGDA LSEFNFCGCG WPQHMLLPKG TEAGYPCHLF
VMISNYADDR VEQDTSGTCS DGDTFCGIKD KLYPDRRSMG YPFDRMPRDG VDTLQQFLTP
NMRVQEVVIQ FSNRIVKPRN RD
//
