ID GIP1_GIBZE Reviewed; 677 AA. AC I1RF62; A0A098D823; DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2012, sequence version 1. DT 14-DEC-2022, entry version 61. DE RecName: Full=Multicopper oxidase GIP1 {ECO:0000303|PubMed:15811992}; DE EC=1.-.-.- {ECO:0000305}; DE AltName: Full=Aurofusarin biosynthesis cluster protein GIP1 {ECO:0000303|PubMed:16461721}; DE AltName: Full=Gibberella pigment protein 1 {ECO:0000303|PubMed:15811992}; DE AltName: Full=Laccase-1 {ECO:0000303|PubMed:15809006}; DE Flags: Precursor; GN Name=GIP1 {ECO:0000303|PubMed:15811992}; GN Synonyms=lac1 {ECO:0000303|PubMed:15809006}; GN ORFNames=FG02328, FGRAMPH1_01T05601; OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium. OX NCBI_TaxID=229533; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=17823352; DOI=10.1126/science.1143708; RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T., RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S., RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S., RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R., RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M., RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.; RT "The Fusarium graminearum genome reveals a link between localized RT polymorphism and pathogen specialization."; RL Science 317:1400-1402(2007). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J., RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B., RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R., RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W., RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J., RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E., RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M., RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D., RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A., RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C., RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.; RT "Comparative genomics reveals mobile pathogenicity chromosomes in RT Fusarium."; RL Nature 464:367-373(2010). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1; RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1; RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K., RA Hammond-Kosack K.E.; RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium RT graminearum."; RL BMC Genomics 16:544-544(2015). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005; RA Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.; RT "Putative polyketide synthase and laccase genes for biosynthesis of RT aurofusarin in Gibberella zeae."; RL Appl. Environ. Microbiol. 71:1701-1708(2005). RN [5] RP FUNCTION, AND PATHWAY. RX PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010; RA Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A., RA Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.; RT "Identification of a gene cluster responsible for the biosynthesis of RT aurofusarin in the Fusarium graminearum species complex."; RL Fungal Genet. Biol. 42:420-433(2005). RN [6] RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY. RX PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x; RA Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S., RA Nielsen J., Giese H.; RT "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a RT close link between the naphthoquinones and naphthopyrones."; RL Mol. Microbiol. 61:1069-1080(2006). RN [7] RP INDUCTION. RX PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006; RA Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.; RT "GIP2, a putative transcription factor that regulates the aurofusarin RT biosynthetic gene cluster in Gibberella zeae."; RL Appl. Environ. Microbiol. 72:1645-1652(2006). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND PATHWAY. RX PubMed=21296881; DOI=10.1074/jbc.m110.179853; RA Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S., RA Giese H.; RT "Two novel classes of enzymes are required for the biosynthesis of RT aurofusarin in Fusarium graminearum."; RL J. Biol. Chem. 286:10419-10428(2011). RN [9] RP FUNCTION. RX PubMed=23557488; DOI=10.1186/1475-2859-12-31; RA Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.; RT "Reconstruction of the biosynthetic pathway for the core fungal polyketide RT scaffold rubrofusarin in Saccharomyces cerevisiae."; RL Microb. Cell Fact. 12:31-31(2013). CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that mediates CC the biosynthesis of aurofusarin, a red mycelium pigment which is acting CC as a mycotoxin (PubMed:15811992, PubMed:15809006, PubMed:16879655). The CC first step is performed by the polyketide synthase which condenses one CC acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the CC cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, CC PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is CC probably formed during ring closure by an aldol-type cyclization CC reaction (PubMed:21296881). The dehydratase aurZ then acts as the first CC tailoring enzyme in the aurofusarin biosynthetic pathway by converting CC YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor- CC rubrofusarin is then methylated to rubrofusarin by the O- CC methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin CC is then transported across the plasma membrane by the rubrofusarin- CC specific pump aurT for further enzymatic processing by the CC extracellular complex composed of GIP1, aurF, aurO and aurS to yield CC aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006, CC ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655, CC ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}. CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006, CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}. CC -!- SUBUNIT: Might be part of an extracellular enzyme complex composed of CC GIP1, aurF, aurO and aurS (PubMed:21296881). CC {ECO:0000305|PubMed:21296881}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21296881}. Secreted, CC extracellular space {ECO:0000305|PubMed:21296881}. CC -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis CC cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655, CC PubMed:16461721). {ECO:0000269|PubMed:16461721, CC ECO:0000269|PubMed:16879655}. CC -!- DISRUPTION PHENOTYPE: Impairs autofusarin biosynthesis and leads to a CC yellow pigmentation via accumulation of the intermediate rubrofusarin CC (PubMed:15811992, PubMed:16879655). {ECO:0000269|PubMed:15811992, CC ECO:0000269|PubMed:16879655}. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HG970332; CEF74605.1; -; Genomic_DNA. DR RefSeq; XP_011318237.1; XM_011319935.1. DR AlphaFoldDB; I1RF62; -. DR SMR; I1RF62; -. DR STRING; 5518.FGSG_02328P0; -. DR GeneID; 23549710; -. DR KEGG; fgr:FGSG_02328; -. DR VEuPathDB; FungiDB:FGRAMPH1_01G05601; -. DR eggNOG; KOG1263; Eukaryota. DR HOGENOM; CLU_006504_5_0_1; -. DR InParanoid; I1RF62; -. DR BioCyc; MetaCyc:MON-19450; -. DR PHI-base; PHI:3991; -. DR PHI-base; PHI:712; -. DR Proteomes; UP000070720; Chromosome 1. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.420; -; 3. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011706; Cu-oxidase_C. DR InterPro; IPR045087; Cu-oxidase_fam. DR InterPro; IPR011707; Cu-oxidase_N. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR SUPFAM; SSF49503; Cupredoxins; 3. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 1: Evidence at protein level; KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..677 FT /note="Multicopper oxidase GIP1" FT /id="PRO_5010124150" FT DOMAIN 31..150 FT /note="Plastocyanin-like 1" FT /evidence="ECO:0000255" FT DOMAIN 179..379 FT /note="Plastocyanin-like 2" FT /evidence="ECO:0000255" FT DOMAIN 469..588 FT /note="Plastocyanin-like 3" FT /evidence="ECO:0000255" FT REGION 629..651 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 80 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q70KY3" FT BINDING 82 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q70KY3" FT BINDING 130 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q70KY3" FT BINDING 132 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q70KY3" FT BINDING 503 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q70KY3" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 283 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 396 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 478 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 520 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" SQ SEQUENCE 677 AA; 75310 MW; 6DC1B77634B307F2 CRC64; MLTSPRLILL LLAWVFSALV ASALVKKDWT ITWEPGAPNG QERNMIKINN QFPGPTILCD EDDDIEVTVH NKMPFNTTVH WHGLERVNCV RMMGTPWSDG TPGMSQKPIE MGQSFIYRFK ASPAGTHWYH SHSRATVLDG LYGPIFIRRK PDAPAPWHLI SKEQADIDAM SRAVIDPKLV MVSDWTRFMS WEYMAAEESS GMAIFCSDSI LVNGKGSLYC PDVDVLINHT STYMKYGLYP RQVNDKGCFP FMRSTQGPYL TTGKPETIPL HLQHGCTPAE GTNETIEVDP ADQWASLNFI GGATFKTIVF SVDEHDMWVY EVDGHYIVPQ RVNTVHMYAG ERYAVMIKLD KTPKDYTIRV ADSGLTQVIS AFATLRYKGG IQGSDSVGVI DYGGQNSTKD GSVITLDREH LPPYPPNPPA RKADAMHVLS THRWKSAWQY TMSGHGMYEE DRSAYGPLLY DPHSADAMDE GLVIRTKNGS WVDLVLQVGS LPGQPQEFPH MMHKHTGKTW QIGSGMGIWN YSSVEEAIAA EPHNFDLDTP KWRDTFVTSF DGSAWIVLRY QVTNPGPWLF HCHIETHLAG GMAIAILDGI DVWPQIPAEY GPDQRGFMPG TLPELESGGK QGTVDKQCPL LAVSPSGGPK KDSGETSASD SRWETLIRGL IQVLQGWLSD EASSRSS //