ISCA1_RAT
ID ISCA1_RAT Reviewed; 129 AA.
AC Q80W96;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial;
DE AltName: Full=HESB-like domain-containing protein 2;
DE AltName: Full=Iron-sulfur assembly protein IscA;
DE Flags: Precursor;
GN Name=Isca1; Synonyms=Hbld2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15262227; DOI=10.1016/j.bbapap.2004.05.004;
RA Cozar-Castellano I., del Valle Machargo M., Trujillo E., Arteaga M.F.,
RA Gonzalez T., Martin-Vasallo P., Avila J.;
RT "hIscA: a protein implicated in the biogenesis of iron-sulfur clusters.";
RL Biochim. Biophys. Acta 1700:179-188(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC functioning late in the iron-sulfur cluster assembly pathway. Probably
CC involved in the binding of an intermediate of Fe/S cluster assembly.
CC {ECO:0000250|UniProtKB:Q9BUE6}.
CC -!- SUBUNIT: Interacts with CRY2, but not with CRY1 (in vitro).
CC {ECO:0000250|UniProtKB:Q9BUE6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9BUE6}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR EMBL; AF508158; AAP29778.1; -; mRNA.
DR EMBL; BC070929; AAH70929.1; -; mRNA.
DR EMBL; BC078677; AAH78677.1; -; mRNA.
DR RefSeq; NP_853657.1; NM_181626.3.
DR AlphaFoldDB; Q80W96; -.
DR SMR; Q80W96; -.
DR STRING; 10116.ENSRNOP00000024781; -.
DR PaxDb; Q80W96; -.
DR PRIDE; Q80W96; -.
DR Ensembl; ENSRNOT00000117636; ENSRNOP00000078686; ENSRNOG00000018343.
DR GeneID; 290985; -.
DR KEGG; rno:290985; -.
DR UCSC; RGD:727792; rat.
DR CTD; 81689; -.
DR RGD; 727792; Isca1.
DR eggNOG; KOG1120; Eukaryota.
DR GeneTree; ENSGT00490000043385; -.
DR InParanoid; Q80W96; -.
DR OrthoDB; 1578799at2759; -.
DR PhylomeDB; Q80W96; -.
DR TreeFam; TF314956; -.
DR Reactome; R-RNO-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR PRO; PR:Q80W96; -.
DR Proteomes; UP000002494; Chromosome 17.
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:0050886; P:endocrine process; NAS:RGD.
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 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 2: Evidence at transcript level;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..129
FT /note="Iron-sulfur cluster assembly 1 homolog,
FT mitochondrial"
FT /id="PRO_0000042737"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ SEQUENCE 129 AA; 14149 MW; 2C3693C453688233 CRC64;
MSASLVRATV RAVSKRKLQP TRAALTLTPS AVNKIKQLLK DKPEHVGLKV GVRTRGCNGL
SYSLEYTKTK GDADEEVIQD GVRVFIEKKA QLTLLGTEMD YVEDKLSSEF VFNNPNIKGT
CGCGESFNV