ABR1_ASPFU
ID ABR1_ASPFU Reviewed; 664 AA.
AC Q4WZB4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Multicopper oxidase abr1 {ECO:0000303|PubMed:10515939};
DE EC=1.-.-.- {ECO:0000305|PubMed:24123270};
DE AltName: Full=Conidial pigment biosynthesis oxidase abr1 {ECO:0000305};
DE Flags: Precursor;
GN Name=abr1 {ECO:0000303|PubMed:10515939}; ORFNames=AFUA_2G17540;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
RX PubMed=10515939; DOI=10.1128/jb.181.20.6469-6477.1999;
RA Tsai H.F., Wheeler M.H., Chang Y.C., Kwon-Chung K.J.;
RT "A developmentally regulated gene cluster involved in conidial pigment
RT biosynthesis in Aspergillus fumigatus.";
RL J. Bacteriol. 181:6469-6477(1999).
RN [3]
RP FUNCTION.
RX PubMed=14970241; DOI=10.1099/jmm.0.05421-0;
RA Youngchim S., Morris-Jones R., Hay R.J., Hamilton A.J.;
RT "Production of melanin by Aspergillus fumigatus.";
RL J. Med. Microbiol. 53:175-181(2004).
RN [4]
RP FUNCTION.
RX PubMed=19703288; DOI=10.1186/1471-2180-9-177;
RA Pihet M., Vandeputte P., Tronchin G., Renier G., Saulnier P.,
RA Georgeault S., Mallet R., Chabasse D., Symoens F., Bouchara J.P.;
RT "Melanin is an essential component for the integrity of the cell wall of
RT Aspergillus fumigatus conidia.";
RL BMC Microbiol. 9:177-177(2009).
RN [5]
RP FUNCTION.
RX PubMed=19156203; DOI=10.1371/journal.pone.0004224;
RA Jackson J.C., Higgins L.A., Lin X.;
RT "Conidiation color mutants of Aspergillus fumigatus are highly pathogenic
RT to the heterologous insect host Galleria mellonella.";
RL PLoS ONE 4:E4224-E4224(2009).
RN [6]
RP FUNCTION.
RX PubMed=20145078; DOI=10.1128/aac.01504-09;
RA Ben-Ami R., Lewis R.E., Leventakos K., Latge J.P., Kontoyiannis D.P.;
RT "Cutaneous model of invasive aspergillosis.";
RL Antimicrob. Agents Chemother. 54:1848-1854(2010).
RN [7]
RP FUNCTION.
RX PubMed=21747802; DOI=10.3389/fmicb.2011.00096;
RA Thywissen A., Heinekamp T., Dahse H.M., Schmaler-Ripcke J., Nietzsche S.,
RA Zipfel P.F., Brakhage A.A.;
RT "Conidial dihydroxynaphthalene melanin of the human pathogenic fungus
RT Aspergillus fumigatus interferes with the host endocytosis pathway.";
RL Front. Microbiol. 2:96-96(2011).
RN [8]
RP FUNCTION.
RX PubMed=21573171; DOI=10.1371/journal.pone.0019591;
RA Mech F., Thywissen A., Guthke R., Brakhage A.A., Figge M.T.;
RT "Automated image analysis of the host-pathogen interaction between
RT phagocytes and Aspergillus fumigatus.";
RL PLoS ONE 6:E19591-E19591(2011).
RN [9]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24123270; DOI=10.1128/ec.00217-13;
RA Upadhyay S., Torres G., Lin X.;
RT "Laccases involved in 1,8-dihydroxynaphthalene melanin biosynthesis in
RT Aspergillus fumigatus are regulated by developmental factors and copper
RT homeostasis.";
RL Eukaryot. Cell 12:1641-1652(2013).
RN [10]
RP FUNCTION.
RX PubMed=24818666; DOI=10.1128/iai.01726-14;
RA Bayry J., Beaussart A., Dufrene Y.F., Sharma M., Bansal K., Kniemeyer O.,
RA Aimanianda V., Brakhage A.A., Kaveri S.V., Kwon-Chung K.J., Latge J.P.,
RA Beauvais A.;
RT "Surface structure characterization of Aspergillus fumigatus conidia
RT mutated in the melanin synthesis pathway and their human cellular immune
RT response.";
RL Infect. Immun. 82:3141-3153(2014).
RN [11]
RP FUNCTION.
RX PubMed=25684622; DOI=10.1111/1462-2920.12808;
RA Hillmann F., Novohradska S., Mattern D.J., Forberger T., Heinekamp T.,
RA Westermann M., Winckler T., Brakhage A.A.;
RT "Virulence determinants of the human pathogenic fungus Aspergillus
RT fumigatus protect against soil amoeba predation.";
RL Environ. Microbiol. 17:2858-2869(2015).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26972005; DOI=10.1016/j.celrep.2016.02.059;
RA Upadhyay S., Xu X., Lowry D., Jackson J.C., Roberson R.W., Lin X.;
RT "Subcellular compartmentalization and trafficking of the biosynthetic
RT machinery for fungal melanin.";
RL Cell Rep. 14:2511-2518(2016).
CC -!- FUNCTION: Multicopper oxidase; part of the gene cluster that mediates
CC the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green
CC pigment and a structural component of the conidial wall
CC (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of
CC the pathway is the production of the heptaketide naphtopyrone YWA1 by
CC the polyketide synthase alb1 though condensation of acetyl-CoA with
CC malonyl-CoA (PubMed:10515939). The naphtopyrone YWA1 is then converted
CC to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the
CC heptaketide hydrolyase ayg1 though chain-length shortening
CC (PubMed:10515939,). 1,3,6,8-THN is substrate of the hydroxynaphthalene
CC reductase arp2 to yield scytalone (PubMed:10515939). The scytalone
CC dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939).
CC 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to
CC yield vermelone (PubMed:10515939). Vermelone is further converted by
CC the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939). Finally the
CC laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939). DHN-
CC melanin biosynthesis appears to be initiated in endosomes where early
CC enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading
CC to melanin deposition on the cell surface where late enzymes (abr1 and
CC abr2) localize (PubMed:26972005). DHN-melanin is an important
CC structural component of the outer cell wall and is required for the
CC presence of conidial surface hydrophobins (PubMed:19703288). DHN-
CC melanin also plays a crucial role in fungal virulence, including a
CC protective role against the host's immune defenses (PubMed:19156203,
CC PubMed:20145078, PubMed:21747802, PubMed:21573171, PubMed:24818666).
CC DHN-melanin protects also conidia against amoeba predation
CC (PubMed:25684622). {ECO:0000269|PubMed:10515939,
CC ECO:0000269|PubMed:14970241, ECO:0000269|PubMed:19156203,
CC ECO:0000269|PubMed:19703288, ECO:0000269|PubMed:20145078,
CC ECO:0000269|PubMed:21573171, ECO:0000269|PubMed:21747802,
CC ECO:0000269|PubMed:24818666, ECO:0000269|PubMed:25684622,
CC ECO:0000269|PubMed:26972005}.
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26972005}. Cell
CC surface {ECO:0000269|PubMed:24123270, ECO:0000269|PubMed:26972005}.
CC Note=Localized at the surface of stalks and conidiophores, but not in
CC young hyphae (PubMed:24123270). {ECO:0000269|PubMed:24123270}.
CC -!- INDUCTION: Expression is up-regulated upon hyphal competency and
CC drastically increased during conidiation (PubMed:24123270). Expression
CC is controlled by brlA, the master regulator of conidiophore
CC development, and is responsive to the copper level in the medium
CC (PubMed:24123270). {ECO:0000269|PubMed:24123270}.
CC -!- DISRUPTION PHENOTYPE: Changes the gray-green conidial pigment to a
CC brown color (PubMed:26972005). {ECO:0000269|PubMed:26972005}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL94051.2; -; Genomic_DNA.
DR RefSeq; XP_756089.2; XM_750996.2.
DR AlphaFoldDB; Q4WZB4; -.
DR SMR; Q4WZB4; -.
DR STRING; 746128.CADAFUBP00003257; -.
DR EnsemblFungi; EAL94051; EAL94051; AFUA_2G17540.
DR GeneID; 3512773; -.
DR KEGG; afm:AFUA_2G17540; -.
DR VEuPathDB; FungiDB:Afu2g17540; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR InParanoid; Q4WZB4; -.
DR OMA; GNLHPWH; -.
DR OrthoDB; 525810at2759; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033573; C:high-affinity iron permease complex; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:AspGD.
DR GO; GO:0046148; P:pigment biosynthetic process; IMP:AspGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
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 InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..664
FT /note="Multicopper oxidase abr1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004246518"
FT DOMAIN 19..155
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 156..339
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 340..521
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT REGION 516..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 421
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 424
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 426
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 483
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 484
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 485
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 489
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 664 AA; 73445 MW; C2E69707469C3A0A CRC64;
MFHSRALLLS WLVGFTAAKD IHLDWNITWV WAAPDGFGRP MIGINNEWPC PIVNADLGDR
LIVDVHNGLG NQSTGIHWHG FHQYMTGTMD GSNQVTQCAL PPGSSMRYEF DVNQTGTYWY
HSHEMGQYPD GLRGPFIVRD PSPPFAYDDE FTLTLTDHYH EQMSVLLQQY EADSVGAQAG
VNEPLPAAAL INEGFDTTTL RVEPNKTYLI HLVCVGNWPG HVIVFDDHEI SVVEVDGTWV
DAYPARDKKI RLATGQRMSI LLKTKDNTDR NYAIWDSMDV NMMFFYQNRA IPEGFNPNTT
AWLVYDEAKE LPPAPDVHEL DPNNDFVDDL VFVPASHEPL LEKVDRQIIF DTGVTQRDGR
SVYTINGQTY VDPEEPTLYT ALAASPENAS NASLYGQVNP FVVQYGEVVE IIINNHHGNL
HPWHMHGHQF QVLQRTIPEG GYFDGYFANI SSTPVKRDTI MVQNHGHAVL RFRANNPGVW
LIHCHIEWHV TKGLTGTLIE APAQMHKISV PLDHQRICPS YGTPPGGTPS SPPHDAPRPD
GASGSPQYPP KPWGEPDASA PEQDDSQPGG TPDSPEDFPQ PWGEPEESPQ EPPQPWSPSN
NAQPPANTYA PEYPSGYVPV APGPVIIDSE LHYGGKSSHV ECSGVNAGHT QDTTTGGDGC
ANAS
