P-POD: Princeton Protein Orthology Database: GO3/Jaccard404

This family has 49 members: 39 Arabidopsis thaliana, 1 Caenorhabditis elegans, 5 Drosophila melanogaster, 3 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/Jaccard404
49 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_182180.1 · TAIR:locus:2039944 (LAC6 · F13A10.10 · AT2G46570)laccase 6⌘
A. thalianaNCBI:NP_177743.1 · TAIR:locus:2199798
A. thalianaNCBI:NP_195555.2 · TAIR:locus:2121823 (F22I13.190 · AT4G38420 · sks9 · F22I13_190)SKU5 Similar 9⌘
A. thalianaNCBI:NP_194254.2 · TAIR:locus:2122689 (F24A6.80 · SKS1 · F24A6_80 · AT4G25240)SKU5 SIMILAR 1⌘
A. thalianaNCBI:NP_195725.1 · TAIR:locus:2150049 (LAC9 · F7J8_30 · AT5G01050 · F7J8.30)⌘
A. thalianaNCBI:NP_197609.1 · TAIR:locus:2178973
A. thalianaNCBI:NP_173603.1 · TAIR:locus:2036911
A. thalianaNCBI:NP_680176.2 · TAIR:locus:505006625 (AT5G21105)⌘
A. thalianaNCBI:NP_180477.1 · TAIR:locus:2066117 (T9I4_21 · AT2G29130 · T9I4.21 · LAC2)laccase 2⌘
A. thalianaNCBI:NP_564479.1 · TAIR:locus:2033513 (AT1G41830 · SKS6 · F5A13_5 · F5A13.5)SKU5-SIMILAR 6 · SKU5 SIMILAR 6⌘
A. thalianaNCBI:NP_195946.2 · TAIR:locus:2143563 (F15A17_290 · AT5G03260 · LAC11 · F15A17.290)laccase 11⌘
A. thalianaNCBI:NP_196158.1 · TAIR:locus:2153469 (K18I23_20 · K18I23.20 · LAC12 · AT5G05390)laccase 12⌘
A. thalianaNCBI:NP_195724.1 · TAIR:locus:2150039 (LAC8 · F7J8_20 · F7J8.20 · AT5G01040)laccase 8⌘
A. thalianaNCBI:NP_569041.1 · TAIR:locus:2174954
A. thalianaNCBI:NP_187533.1 · TAIR:locus:2083604 (F3L24.9 · AT3G09220 · LAC7)laccase 7⌘
A. thalianaNCBI:NP_181568.1 · TAIR:locus:2063109 (T3G21.14 · T3G21_14 · AT2G40370 · LAC5)laccase 5⌘
A. thalianaNCBI:NP_565881.1 · TAIR:locus:2042842 (AT2G38080 · F16M14.1 · F16M14_1 · IRX12 · LAC4)IRREGULAR XYLEM 12 · LACCASE 4⌘
A. thalianaNCBI:NP_195433.1 · TAIR:locus:2115154 (sks15 · AP22_55 · AP22.55 · AT4G37160)SKU5 Similar 15⌘
A. thalianaNCBI:NP_196498.1 · TAIR:locus:2184802 (LAC14 · T5E8.160 · AT5G09360 · T5E8_160)laccase 14⌘
A. thalianaNCBI:NP_196330.3 · TAIR:locus:2182895 (T28J14.70 · LAC13 · T28J14_70 · AT5G07130)laccase 13⌘
A. thalianaNCBI:NP_193932.1 · TAIR:locus:2120648
A. thalianaNCBI:NP_199656.1 · TAIR:locus:2166086 (sks3 · MJE7.8 · AT5G48450 · MJE7_8)SKU5 Similar 3⌘
A. thalianaNCBI:NP_195693.1 · TAIR:locus:2135242
A. thalianaNCBI:NP_200810.1 · TAIR:locus:2168128 (MMN10_20 · MMN10.20 · AT5G60020 · LAC17)laccase 17⌘
A. thalianaNCBI:NP_177707.1 · TAIR:locus:2005594 (F10A5.2 · sks18 · AT1G75790 · F10A5_2)SKU5 Similar 18⌘
A. thalianaNCBI:NP_192979.1 · TAIR:locus:2135535 (T1P17.10 · T1P17_10 · AT4G12420 · SKU5)⌘
A. thalianaNCBI:NP_565554.1 · TAIR:locus:2046763 (AT2G23630 · F26B6.30 · sks16)SKU5 Similar 16⌘
A. thalianaNCBI:NP_175953.1 · TAIR:locus:2193894
A. thalianaNCBI:NP_564697.1 · TAIR:locus:2193899
A. thalianaNCBI:NP_199621.2 · TAIR:locus:2162677 (TT10 · LAC15 · MDN11_18 · AT5G48100 · MDN11.18)TRANSPARENT TESTA 10 · LACCASE-LIKE 15⌘
A. thalianaTAIR:locus:2092865 · NCBI:NP_187948.1
A. thalianaNCBI:NP_194538.1 · TAIR:locus:2132927
A. thalianaNCBI:NP_200699.1 · TAIR:locus:2154518 (K19M22.11 · AT5G58910 · K19M22_11 · LAC16)laccase 16⌘
A. thalianaNCBI:NP_199961.1 · TAIR:locus:2153107 (K17N15_3 · SKS2 · AT5G51480 · K17N15.3)SKU5 SIMILAR 2⌘
A. thalianaNCBI:NP_187947.1 · TAIR:locus:2092845
A. thalianaNCBI:NP_173604.1 · TAIR:locus:2201133
A. thalianaNCBI:NP_173252.2 · TAIR:locus:2194110 (T10F20.14 · AT1G18140 · LAC1)Laccase 1⌘
A. thalianaNCBI:NP_195739.2 · TAIR:locus:2150139 (F7J8_170 · LAC10 · F7J8.170 · AT5G01190)laccase 10⌘
A. thalianaNCBI:NP_180580.1 · TAIR:locus:2060879 (LAC3 · T9D9.2 · AT2G30210)laccase 3⌘
C. elegansWB:WBGene00009008 (F21D5.3) · UniProtKB:Q19687⌘
D. melanogasterFB:FBgn0050437 · UniProtKB:A1Z6F4
D. melanogasterFB:FBgn0052838 · UniProtKB:A1Z6F7
D. melanogasterFB:FBgn0032116 (laccase-like · CG3759) · UniProtKB:Q8SYT6⌘
D. melanogasterFB:FBgn0039387 (CG5959) · UniProtKB:Q9VBK7⌘
D. melanogasterFB:FBgn0052557 (CG7871 · CG32557) · UniProtKB:Q9VX11⌘
S. cerevisiaeUniProtKB:P38993 · SGD:S000004662 (YMR058W · FET3)Ferro-O2-oxidoreductase required for high-affinity iron uptake and involved in mediating resistance to copper ion toxicity, belongs to class of integral membrane multicopper oxidases⌘
S. cerevisiaeUniProtKB:P43561 · SGD:S000001853 (YFL041W · FET5)Multicopper oxidase, integral membrane protein with similarity to Fet3p⌘
S. cerevisiaeUniProtKB:Q04399 · SGD:S000002914 (YDR506C)Possible membrane-localized protein⌘
S. pombeUniProtKB:Q09920 · GeneDB_Spombe:SPAC1F7.08 (SPAC1F7.08 · fio1)iron transport multicopper oxidase Fio1⌘
ProteinPublicationCurator Notes
UniProtKB:P38993 · SGD:S000004662PMID:8643627 Eide D, et al. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5624-8.The A. thaliana protein AT4G19690.1 was expressed in S. cerevisiae, but complementation was not directly tested. IRT1 was cloned by transforming an Arabidopsis library into fet3 fet4 yeast, but IRT1 is more closely related to yeast ZRT1 and ZRT2 and shows no similarity to FET3 or FET4.
UniProtKB:P38993 · SGD:S000004662PMID:15147898 Southron JL, et al. Complementation of Saccharomyces cerevisiae ccc2 mutant by a putative P1B-ATPase from Brassica napus supports a copper-transporting function. FEBS Lett. 2004 May 21;566(1-3):218-22.The B. napus protein BnRAN1 does not complement a homologous mutation in S. cerevisiae. BnRAN1 complements yeast ccc2 but does not suppress fet3.
UniProtKB:P38993 · SGD:S000004662PMID:14739215 Harris ZL, et al. A fungal multicopper oxidase restores iron homeostasis in aceruloplasminemia. Blood. 2004 Jun 15;103(12):4672-3.The S. cerevisiae protein FET3 complements a homologous mutation in M. musculus. Injection of Fet3p into mice restores iron homeostasis to ceruloplasmin-deficient mice.
UniProtKB:P38993 · SGD:S000004662PMID:17655522 Park YS, et al. Physical and functional interaction of FgFtr1-FgFet1 and FgFtr2-FgFet2 is required for iron uptake in Fusarium graminearum. Biochem J. 2007 Nov 15;408(1):97-104.The F. graminearum protein FgFet1 complements a homologous mutation in S. cerevisiae. The combined expression of F. graminearum Ftr1 and Fet1 complements a yeast ftr1 fet3 double mutant, but Ftr2 and Fet1 do not.
UniProtKB:P38993 · SGD:S000004662PMID:16750173 Park YS, et al. Cellular iron utilization is regulated by putative siderophore transporter FgSit1 not by free iron transporter in Fusarium graminearum. Biochem Biophys Res Commun. 2006 Jul 14;345(4):1634-42.The F. graminearum protein FgSit1 was expressed in S. cerevisiae, but complementation was not directly tested. F. graminearum Sit1 functions as a siderophore-iron transporter in yeast and complements an arn1 arn2 arn3 arn4 quadruple mutant; this experiment was performed in an fet3 background to prevent the uptake of free iron, which would interfere with the analysis.
UniProtKB:P38993 · SGD:S000004662PMID:17000865 Huynh C, et al. A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes. J Exp Med. 2006 Oct 2;203(10):2363-75.The L. amazonensis protein LIT1 complements a homologous mutation in S. cerevisiae. LIT1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:16412081 Ishimaru Y, et al. Rice plants take up iron as an Fe3+-phytosiderophore and as Fe2+. Plant J. 2006 Feb;45(3):335-46.The O. sativa protein OsIRT1 complements a homologous mutation in S. cerevisiae. Rice IRT1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:12921533 Li L, et al. Functional studies of hephaestin in yeast: evidence for multicopper oxidase activity in the endocytic pathway. Biochem J. 2003 Nov 1;375(Pt 3):793-8.The M. musculus protein Q9Z0Z4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38993 · SGD:S000004662PMID:14648120 Cohen CK, et al. Kinetic properties of a micronutrient transporter from Pisum sativum indicate a primary function in Fe uptake from the soil. Planta. 2004 Mar;218(5):784-92.The P. sativum protein RIT1 complements a homologous mutation in S. cerevisiae. Pea RIT1 complements an fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:16267047 Smyth DJ, et al. Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes. J Biol Chem. 2006 Jan 27;281(4):2242-8.The S. mansoni protein SmDMT1A complements a homologous mutation in S. cerevisiae. SmDMT1A complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:12888492 Pelletier B, et al. Fep1 represses expression of the fission yeast Schizosaccharomyces pombe siderophore-iron transport system. Nucleic Acids Res. 2003 Aug 1;31(15):4332-44.The S. pombe protein str1+ does not complement a homologous mutation in S. cerevisiae. Expression of str1+ in an fet3 arn1-4 background restored ferrichrome-dependent iron uptake.
UniProtKB:P38993 · SGD:S000004662PMID:10769179 Curie C, et al. Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem J. 2000 May 1;347 Pt 3:749-55.The A. thaliana protein AT1G47240.1 does not complement a homologous mutation in S. cerevisiae. A. thaliana NRAMP2 does not complement a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:10769179 Curie C, et al. Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem J. 2000 May 1;347 Pt 3:749-55.The A. thaliana protein AT1G80830.1 complements a homologous mutation in S. cerevisiae. A. thaliana NRAMP1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:12887581 Kaiser BN, et al. The soybean NRAMP homologue, GmDMT1, is a symbiotic divalent metal transporter capable of ferrous iron transport. Plant J. 2003 Aug;35(3):295-304.The A. thaliana proteins AT4G19690.1 and AT4G19690.2 complement a homologous mutation in S. cerevisiae. A. thaliana IRT1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:10769179 Curie C, et al. Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem J. 2000 May 1;347 Pt 3:749-55.The A. thaliana proteins AT4G19690.1 and AT4G19690.2 complement a homologous mutation in S. cerevisiae. A. thaliana IRT1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:11035780 Rogers EE, et al. Altered selectivity in an Arabidopsis metal transporter. Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12356-60.The A. thaliana proteins AT4G19690.1 and AT4G19690.2 complement a homologous mutation in S. cerevisiae. A. thaliana IRT1 complements a yeast fet3 fet4 double mutant; IRT1 is also shown to transport zinc, manganese, and cadmium.
UniProtKB:P38993 · SGD:S000004662PMID:8995275 Askwith C, et al. An oxidase-permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae. J Biol Chem. 1997 Jan 3;272(1):401-5.The S. pombe protein fio1+ complements a homologous mutation in S. cerevisiae. S. pombe fio1+ complements an S. cerevisiae fet3 mutant, but only in conjunction with the FTR1 homolog fip1+; in this experiment, FTR1 was not mutated.
UniProtKB:P38993 · SGD:S000004662PMID:12887581 Kaiser BN, et al. The soybean NRAMP homologue, GmDMT1, is a symbiotic divalent metal transporter capable of ferrous iron transport. Plant J. 2003 Aug;35(3):295-304.The G. max protein GmDmt1;1 complements a homologous mutation in S. cerevisiae. Soybean GmDmt1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:10769179 Curie C, et al. Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem J. 2000 May 1;347 Pt 3:749-55.The O. sativa protein OsNramp1 complements a homologous mutation in S. cerevisiae. Rice NRAMP1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:10769179 Curie C, et al. Involvement of NRAMP1 from Arabidopsis thaliana in iron transport. Biochem J. 2000 May 1;347 Pt 3:749-55.The O. sativa protein OsNramp2 does not complement a homologous mutation in S. cerevisiae. Rice NRAMP2 does not complement a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:16267047 Smyth DJ, et al. Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes. J Biol Chem. 2006 Jan 27;281(4):2242-8.The A. thaliana proteins AT4G19690.1 and AT4G19690.2 complement a homologous mutation in S. cerevisiae. A. thaliana IRT1 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:17655522 Park YS, et al. Physical and functional interaction of FgFtr1-FgFet1 and FgFtr2-FgFet2 is required for iron uptake in Fusarium graminearum. Biochem J. 2007 Nov 15;408(1):97-104.The F. graminearum protein FgFet2 does not complement a homologous mutation in S. cerevisiae. Expression of F. graminearum Fet2 in conjunction with either Ftr1 or Ftr2 does not complement a yeast ftr1 fet3 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:16412081 Ishimaru Y, et al. Rice plants take up iron as an Fe3+-phytosiderophore and as Fe2+. Plant J. 2006 Feb;45(3):335-46.The O. sativa protein OsIRT2 complements a homologous mutation in S. cerevisiae. Rice IRT2 complements a yeast fet3 fet4 double mutant.
UniProtKB:P38993 · SGD:S000004662PMID:16267047 Smyth DJ, et al. Two isoforms of a divalent metal transporter (DMT1) in Schistosoma mansoni suggest a surface-associated pathway for iron absorption in schistosomes. J Biol Chem. 2006 Jan 27;281(4):2242-8.The S. mansoni protein SmDMT1B complements a homologous mutation in S. cerevisiae. SmDMT1A complements a yeast fet3 fet4 double mutant.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
SGD Disease Papers (4)
UniProtKB:P38993 · SGD:S000004662PMID:15105274 Xu X, et al. (2004) Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Ann N Y Acad Sci 1012:299-305
UniProtKB:P38993 · SGD:S000004662PMID:9811853 Davis-Kaplan SR, et al. (1998) Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: an unexpected role for intracellular chloride channels. Proc Natl Acad Sci U S A 95(23):13641-5
PMID:7708696 Yuan DS, et al. (1995) The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc Natl Acad Sci U S A 92(7):2632-6
PMID:15147898 Southron JL, et al. (2004) Complementation of Saccharomyces cerevisiae ccc2 mutant by a putative P1B-ATPase from Brassica napus supports a copper-transporting function. FEBS Lett 566(1-3):218-22
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