ATM1_CRYNH
ID ATM1_CRYNH Reviewed; 732 AA.
AC J9VWU3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Iron-sulfur clusters transporter ATM1, mitochondrial {ECO:0000303|PubMed:29089435};
DE EC=7.-.-.- {ECO:0000250|UniProtKB:P40416};
DE Flags: Precursor;
GN Name=ATM1 {ECO:0000303|PubMed:29089435}; ORFNames=CNAG_04358;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2]
RP INDUCTION.
RX PubMed=21819456; DOI=10.1111/j.1365-2958.2011.07794.x;
RA Ding C., Yin J., Tovar E.M., Fitzpatrick D.A., Higgins D.G., Thiele D.J.;
RT "The copper regulon of the human fungal pathogen Cryptococcus neoformans
RT H99.";
RL Mol. Microbiol. 81:1560-1576(2011).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29089435; DOI=10.1128/mbio.01742-17;
RA Garcia-Santamarina S., Uzarska M.A., Festa R.A., Lill R., Thiele D.J.;
RT "Cryptococcus neoformans iron-sulfur protein biogenesis machinery is a
RT novel layer of protection against Cu stress.";
RL MBio 8:0-0(2017).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29420779; DOI=10.1093/mmy/myx073;
RA Do E., Park S., Li M.H., Wang J.M., Ding C., Kronstad J.W., Jung W.H.;
RT "The mitochondrial ABC transporter Atm1 plays a role in iron metabolism and
RT virulence in the human fungal pathogen Cryptococcus neoformans.";
RL Med. Mycol. 56:458-468(2018).
CC -!- FUNCTION: Performs an essential function in the generation of
CC cytoplasmic iron-sulfur proteins by mediating the ATP-dependent export
CC of mitochondrial Fe/S cluster precursors synthesized by NFS1 and other
CC mitochondrial proteins (PubMed:29089435, PubMed:29420779). Hydrolyzes
CC ATP (By similarity). Binds glutathione and may function by transporting
CC a glutathione-conjugated iron-sulfur compound (By similarity). Plays a
CC role during copper stress, in a manner dependent on the copper
CC metalloregulatory transcription factor CUF1 (PubMed:29089435).
CC {ECO:0000250|UniProtKB:P40416, ECO:0000269|PubMed:29089435,
CC ECO:0000269|PubMed:29420779}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40416}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:29089435, ECO:0000305|PubMed:29420779}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by CUF1 during copper
CC stress. {ECO:0000269|PubMed:21819456, ECO:0000269|PubMed:29089435}.
CC -!- DISRUPTION PHENOTYPE: Increases susceptibility to copper toxicity and
CC decreases fitness upon co-incubation with macrophage like cell lines
CC (PubMed:29089435). Increases RNA level of genes involved in iron uptake
CC (PubMed:29420779). Increases mitochondrial iron levels
CC (PubMed:29420779). Increases mitochondrial reactive oxygen species
CC (ROS) levels (PubMed:29420779). Increases mitochondrial complex I
CC activity (PubMed:29420779). Decreases cellular heme levels
CC (PubMed:29420779). Sensitive to hydrogen peroxide (PubMed:29420779).
CC Abolishes cell population growth on the non-fermentable carbon source
CC ethanol and acetate (PubMed:29420779). Decreases cell population growth
CC rate; growth rate improves in a low oxygen environment
CC (PubMed:29420779). Decreases virulence in a mouse intranasal infection
CC model (PubMed:29420779). {ECO:0000269|PubMed:29089435,
CC ECO:0000269|PubMed:29420779}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; CP003828; AFR97089.1; -; Genomic_DNA.
DR EMBL; CP003828; AGV14605.1; -; Genomic_DNA.
DR RefSeq; XP_012051758.1; XM_012196368.1.
DR RefSeq; XP_012051759.1; XM_012196369.1.
DR AlphaFoldDB; J9VWU3; -.
DR SMR; J9VWU3; -.
DR EnsemblFungi; AFR97089; AFR97089; CNAG_04358.
DR EnsemblFungi; AGV14605; AGV14605; CNAG_04358.
DR GeneID; 23887793; -.
DR VEuPathDB; FungiDB:CNAG_04358; -.
DR HOGENOM; CLU_000604_84_1_1; -.
DR Proteomes; UP000010091; Chromosome 9.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; IMP:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ion transport; Iron; Iron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Transit peptide;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..732
FT /note="Iron-sulfur clusters transporter ATM1,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449515"
FT TOPO_DOM 56..143
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 165..181
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 203..262
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 284
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 306..378
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 400..405
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 427..732
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 144..432
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 466..702
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 71..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311..315
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 374..377
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 424
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 499..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 732 AA; 80771 MW; 40C3511E4F4C1149 CRC64;
MGFGSCSRHA LFTPAAFSGS FTTMTTSCFK RVYTAQIHGG DALGKRLPSV SSFSGQLPRH
GLHRQSLAFF STSHRRQTSP PPSPRTTSQS PTVPSKASTT PPTSLNTSKP IATESQDKTD
WSIIVKLAGN IWPKNNPNVK FRVIGALTLL VAGKVLNVQV PFFFKTIVDS LNVPITESTT
VWVLAGASIA GYGAARILTT LFGELRNAVF ASVAQNAIRK VARETFEHLL NMDMKFHLER
QTGGLTRAID RGTKGISFIL SSIVFHVIPT ALEISMVCGI LSWKFGWDFA AVTAITMLLY
TWFTIKTTAW RTTFRKQANA ADNKGATVAV DSLINYEAVK SFNNEKYEVA QYDTTLKAYE
KASVKIATSL AALNSGQNFI FSSALTMMML LGAQGIVKGT MTVGDLVLVN QLVFQLSLPL
NFLGTVYREL RQSLIDMDVM FNLQSLNSAI KDTPTAKPLH LKGGEIEFRN VAFAYHPERP
IFRDLSFKIP AGQKVAIVGP SGCGKSTVFR LLFRFYDSNS GQILIDGQDI KTVTLDSLRR
SIGVVPQDTP LFHADILHNI RYGNLEATDE QVYEAARKAH VEGTIQRLPE KYATKVGERG
LMISGGEKQR LAVARVLLKD PPVLFFDEAT SALDVYTETE LMRNINSILT GQGKTSVFIA
HRLRTISDAD LIIVLQDGYV AEQGTHEQLL AMPGGVYHRL WQAQLTESTQ PTDEEIERQR
EELEVVDEKK KQ
