ID   ISCA2_MOUSE             Reviewed;         154 AA.
AC   Q9DCB8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Iron-sulfur cluster assembly 2 homolog, mitochondrial;
DE   AltName: Full=HESB-like domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Isca2; Synonyms=Hbld1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in the maturation of mitochondrial 4Fe-4S proteins
CC       functioning late in the iron-sulfur cluster assembly pathway. May be
CC       involved in the binding of an intermediate of Fe/S cluster assembly.
CC       {ECO:0000250|UniProtKB:Q86U28}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q86U28}.
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB22467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK002936; BAB22467.1; ALT_INIT; mRNA.
DR   CCDS; CCDS49111.1; -.
DR   RefSeq; NP_083139.1; NM_028863.1.
DR   AlphaFoldDB; Q9DCB8; -.
DR   SMR; Q9DCB8; -.
DR   BioGRID; 216661; 1.
DR   STRING; 10090.ENSMUSP00000021667; -.
DR   iPTMnet; Q9DCB8; -.
DR   PhosphoSitePlus; Q9DCB8; -.
DR   EPD; Q9DCB8; -.
DR   jPOST; Q9DCB8; -.
DR   MaxQB; Q9DCB8; -.
DR   PaxDb; Q9DCB8; -.
DR   PeptideAtlas; Q9DCB8; -.
DR   PRIDE; Q9DCB8; -.
DR   ProteomicsDB; 267009; -.
DR   Antibodypedia; 25630; 159 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000021667; ENSMUSP00000021667; ENSMUSG00000021241.
DR   GeneID; 74316; -.
DR   KEGG; mmu:74316; -.
DR   UCSC; uc007ofu.2; mouse.
DR   CTD; 122961; -.
DR   MGI; MGI:1921566; Isca2.
DR   VEuPathDB; HostDB:ENSMUSG00000021241; -.
DR   eggNOG; KOG1119; Eukaryota.
DR   GeneTree; ENSGT00390000005700; -.
DR   HOGENOM; CLU_069054_1_4_1; -.
DR   InParanoid; Q9DCB8; -.
DR   OMA; SLDYCTG; -.
DR   OrthoDB; 1360948at2759; -.
DR   PhylomeDB; Q9DCB8; -.
DR   TreeFam; TF314519; -.
DR   Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   BioGRID-ORCS; 74316; 26 hits in 75 CRISPR screens.
DR   ChiTaRS; Isca2; mouse.
DR   PRO; PR:Q9DCB8; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9DCB8; protein.
DR   Bgee; ENSMUSG00000021241; Expressed in brown adipose tissue and 255 other tissues.
DR   ExpressionAtlas; Q9DCB8; baseline and differential.
DR   Genevisible; Q9DCB8; MM.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   GO; GO:0106035; P:protein maturation by [4Fe-4S] 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   1: Evidence at protein level;
KW   Iron; Iron-sulfur; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           9..154
FT                   /note="Iron-sulfur cluster assembly 2 homolog,
FT                   mitochondrial"
FT                   /id="PRO_0000277589"
FT   BINDING         79
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         144
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ   SEQUENCE   154 AA;  16718 MW;  00A8B69FBB7AC282 CRC64;
     MAASRALSLT AEAVRAVIPR RSGRLLAVFP RLLTRWETTS SIPEAGEGQI RLTDSCVQRL
     LEITEGSEFL RLQVEGGGCS GFQYKFSLDT VINPDDRVFE QGGARVVVDS DSLAFVKGAQ
     VDFSQELIRS SFQVLNNPQA QQGCSCGSSF SVKV