HSC20_MOUSE
ID HSC20_MOUSE Reviewed; 234 AA.
AC Q8K3A0; Q3V294;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB;
DE Contains:
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB, mitochondrial;
DE Short=C-HSC20 {ECO:0000250|UniProtKB:Q8IWL3};
DE Contains:
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic;
GN Name=Hscb; Synonyms=Hsc20;
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=Embryonic stem cell;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=32634119; DOI=10.1172/jci135479;
RA Crispin A., Guo C., Chen C., Campagna D.R., Schmidt P.J., Lichtenstein D.,
RA Cao C., Sendamarai A.K., Hildick-Smith G.J., Huston N.C., Boudreaux J.,
RA Bottomley S.S., Heeney M.M., Paw B.H., Fleming M.D., Ducamp S.;
RT "Mutations in the iron-sulfur cluster biogenesis protein HSCB cause
RT congenital sideroblastic anemia.";
RL J. Clin. Invest. 130:5245-5256(2020).
CC -!- FUNCTION: Acts as a co-chaperone in iron-sulfur cluster assembly in
CC both mitochondria and the cytoplasm. Required for incorporation of
CC iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of
CC succinate dehydrogenase that is involved in complex II of the
CC mitochondrial electron transport chain. Recruited to SDHB by
CC interaction with SDHAF1 which first binds SDHB and then recruits the
CC iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through
CC direct binding to HSC20. Also mediates complex formation between
CC components of the cytosolic iron-sulfur biogenesis pathway and the CIA
CC targeting complex composed of CIAO1, DIPK1B/FAM69B and MMS19 by binding
CC directly to the scaffold protein ISCU and to CIAO1. This facilitates
CC iron-sulfur cluster insertion into a number of cytoplasmic and nuclear
CC proteins including POLD1, ELP3, DPYD and PPAT (By similarity). Plays an
CC essential role in hematopoiesis (PubMed:32634119).
CC {ECO:0000250|UniProtKB:Q8IWL3, ECO:0000269|PubMed:32634119}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Self-interacts. Interacts with ISCU and HSPA9 to form an iron-
CC sulfur transfer complex. Interacts with SDHAF1 (via the first LYR
CC motif); the interaction recruits the iron-sulfur transfer complex
CC composed of HSC20, HSPA9 and ISCU and mediates the incorporation of
CC iron-sulfur clusters into SDHB which also interacts with HSC20.
CC Interacts with the cytoplasmic form of ISCU and with CIA complex member
CC CIAO1 (via LYR motif). {ECO:0000250|UniProtKB:Q8IWL3}.
CC -!- SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB,
CC cytoplasmic]: Cytoplasm {ECO:0000250|UniProtKB:Q8IWL3}.
CC -!- SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB,
CC mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:Q8IWL3}.
CC -!- DISRUPTION PHENOTYPE: Knockout of the gene is embryonic lethal.
CC Specific loss of the gene in erythroblasts is also lethal due to
CC anemia. {ECO:0000269|PubMed:32634119}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK131961; BAE20904.1; -; mRNA.
DR EMBL; BC027641; AAH27641.1; ALT_INIT; mRNA.
DR CCDS; CCDS51613.1; -.
DR RefSeq; NP_705799.2; NM_153571.2.
DR AlphaFoldDB; Q8K3A0; -.
DR SMR; Q8K3A0; -.
DR BioGRID; 221552; 2.
DR STRING; 10090.ENSMUSP00000062811; -.
DR iPTMnet; Q8K3A0; -.
DR PhosphoSitePlus; Q8K3A0; -.
DR REPRODUCTION-2DPAGE; IPI00170051; -.
DR REPRODUCTION-2DPAGE; Q8K3A0; -.
DR EPD; Q8K3A0; -.
DR MaxQB; Q8K3A0; -.
DR PaxDb; Q8K3A0; -.
DR PeptideAtlas; Q8K3A0; -.
DR PRIDE; Q8K3A0; -.
DR ProteomicsDB; 273275; -.
DR GeneID; 100900; -.
DR KEGG; mmu:100900; -.
DR UCSC; uc008yrv.2; mouse.
DR CTD; 150274; -.
DR MGI; MGI:2141135; Hscb.
DR eggNOG; KOG3192; Eukaryota.
DR InParanoid; Q8K3A0; -.
DR OrthoDB; 1129824at2759; -.
DR PhylomeDB; Q8K3A0; -.
DR TreeFam; TF319992; -.
DR Reactome; R-MMU-1268020; Mitochondrial protein import.
DR Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR UniPathway; UPA00266; -.
DR BioGRID-ORCS; 100900; 30 hits in 74 CRISPR screens.
DR ChiTaRS; Hscb; mouse.
DR PRO; PR:Q8K3A0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K3A0; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISO:MGI.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0060215; P:primitive hemopoiesis; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.1280.20; -; 1.
DR HAMAP; MF_00682; HscB; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR040682; HscB_4_cys.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR14021; PTHR14021; 1.
DR Pfam; PF18256; HscB_4_cys; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF47144; SSF47144; 1.
DR TIGRFAMs; TIGR00714; hscB; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Metal-binding; Mitochondrion; Reference proteome.
FT CHAIN 1..234
FT /note="Iron-sulfur cluster co-chaperone protein HscB,
FT cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IWL3"
FT /id="PRO_0000446243"
FT CHAIN 30..234
FT /note="Iron-sulfur cluster co-chaperone protein HscB,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007263"
FT DOMAIN 71..143
FT /note="J"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q8IWL3"
FT BINDING 43
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q8IWL3"
FT BINDING 57
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q8IWL3"
FT BINDING 60
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q8IWL3"
FT CONFLICT 49
FT /note="A -> V (in Ref. 1; BAE20904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26645 MW; AA9544500EC4F59B CRC64;
MWGCGARALL GVWEVRLAGF LGRRLLGSNA AAGKSIAPQC WNCGHAREAG CGDEFFCSHC
RALQPPDPTR DYFSLMNCNR SFRVDVTKLQ HRYQQLQRLV HPDFFSQKSQ TEKHFSDKHS
TLVNDAYKTL QAPLTRGLYL LKLQGIEIPE GTDYKADSQF LVEIMEINER LADAQSEAAM
EEIEATVRAK QKEFTDNINS AFEQGDFEKA KELLTKMRYF SNIEEKIKLS KTPL
