ISCA1_DROME
ID ISCA1_DROME Reviewed; 130 AA.
AC Q8T3X9; M9PJN7; Q9VXR0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial;
DE AltName: Full=Lethal (1) G0136 {ECO:0000312|FlyBase:FBgn0026666};
DE AltName: Full=Putative magnetoreceptor subunit MagR {ECO:0000303|PubMed:26569474};
DE Flags: Precursor;
GN Name=MagR {ECO:0000303|PubMed:26569474, ECO:0000312|FlyBase:FBgn0026666};
GN Synonyms=Isca1 {ECO:0000305}, l(1)G0136 {ECO:0000312|FlyBase:FBgn0026666};
GN ORFNames=CG8198 {ECO:0000312|FlyBase:FBgn0026666};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL90184.1};
RN [1] {ECO:0000312|EMBL:AAF48498.2, ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|EMBL:AAF48498.2, ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION.
RX PubMed=22885802; DOI=10.1039/c2mt20065a;
RA Mandilaras K., Missirlis F.;
RT "Genes for iron metabolism influence circadian rhythms in Drosophila
RT melanogaster.";
RL Metallomics 4:928-936(2012).
RN [5]
RP INTERACTION WITH CRY, AND TISSUE SPECIFICITY.
RX PubMed=26569474; DOI=10.1038/nmat4484;
RA Qin S., Yin H., Yang C., Dou Y., Liu Z., Zhang P., Yu H., Huang Y.,
RA Feng J., Hao J., Hao J., Deng L., Yan X., Dong X., Zhao Z., Jiang T.,
RA Wang H.W., Luo S.J., Xie C.;
RT "A magnetic protein biocompass.";
RL Nat. Mater. 15:217-226(2016).
CC -!- FUNCTION: Involved in the assembly of mitochondrial iron-sulfur
CC proteins. Probably involved in the binding of an intermediate of Fe/S
CC cluster assembly (By similarity). Required for maintenance of circadian
CC rhythms under constant darkness (PubMed:22885802).
CC {ECO:0000250|UniProtKB:Q9BUE6, ECO:0000269|PubMed:22885802}.
CC -!- SUBUNIT: Interacts with cry. {ECO:0000269|PubMed:26569474}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8T3X9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8T3X9-2; Sequence=VSP_058044;
CC -!- TISSUE SPECIFICITY: Detected in head. {ECO:0000269|PubMed:26569474}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; AE003500; AAF48498.2; -; Genomic_DNA.
DR EMBL; AE014298; AGB95421.1; -; Genomic_DNA.
DR EMBL; AY089446; AAL90184.1; -; mRNA.
DR RefSeq; NP_001259579.1; NM_001272650.1. [Q8T3X9-2]
DR RefSeq; NP_573062.1; NM_132834.2. [Q8T3X9-1]
DR AlphaFoldDB; Q8T3X9; -.
DR SMR; Q8T3X9; -.
DR IntAct; Q8T3X9; 2.
DR STRING; 7227.FBpp0304862; -.
DR PaxDb; Q8T3X9; -.
DR PRIDE; Q8T3X9; -.
DR DNASU; 32513; -.
DR EnsemblMetazoa; FBtr0074084; FBpp0073900; FBgn0026666. [Q8T3X9-1]
DR EnsemblMetazoa; FBtr0332613; FBpp0304862; FBgn0026666. [Q8T3X9-2]
DR GeneID; 32513; -.
DR KEGG; dme:Dmel_CG8198; -.
DR UCSC; CG8198-RA; d. melanogaster. [Q8T3X9-1]
DR CTD; 32513; -.
DR FlyBase; FBgn0026666; MagR.
DR VEuPathDB; VectorBase:FBgn0026666; -.
DR eggNOG; KOG1120; Eukaryota.
DR GeneTree; ENSGT00490000043385; -.
DR InParanoid; Q8T3X9; -.
DR OMA; YQLYFDE; -.
DR PhylomeDB; Q8T3X9; -.
DR Reactome; R-DME-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR BioGRID-ORCS; 32513; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32513; -.
DR PRO; PR:Q8T3X9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026666; Expressed in mouthpart and 22 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IBA:GO_Central.
DR GO; GO:0071000; P:response to magnetism; IDA:FlyBase.
DR Gene3D; 2.60.300.12; -; 1.
DR InterPro; IPR000361; FeS_biogenesis.
DR InterPro; IPR016092; FeS_cluster_insertion.
DR InterPro; IPR017870; FeS_cluster_insertion_CS.
DR InterPro; IPR035903; HesB-like_dom_sf.
DR Pfam; PF01521; Fe-S_biosyn; 1.
DR SUPFAM; SSF89360; SSF89360; 1.
DR TIGRFAMs; TIGR00049; TIGR00049; 1.
DR PROSITE; PS01152; HESB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..130
FT /note="Iron-sulfur cluster assembly 1 homolog,
FT mitochondrial"
FT /id="PRO_0000435362"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 124
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT VAR_SEQ 71
FT /note="K -> KA (in isoform 2)"
FT /id="VSP_058044"
SQ SEQUENCE 130 AA; 14140 MW; 9A17BE2A200A40BF CRC64;
MATRVVATAT VRAVKGRKLI PTRAALTLTP AAVLRIKTLL QDKPDMVGLK VGVRQRGCNG
LSYTLDYASQ KDKLDEEVVQ DGVKVFIDKK AQLSLLGTEM DFVESKLSSE FVFNNPNIKG
TCGCGESFSM
