HSCB_ARATH
ID HSCB_ARATH Reviewed; 252 AA.
AC Q8L7K4; Q9FNG7;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB homolog {ECO:0000305};
DE Short=AtHscB {ECO:0000303|PubMed:19865480};
DE Flags: Precursor;
GN Name=HSCB {ECO:0000303|PubMed:19865480};
GN OrderedLocusNames=At5g06410 {ECO:0000312|Araport:AT5G06410};
GN ORFNames=MHF15.7 {ECO:0000312|EMBL:BAB08963.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, INTERACTION WITH HSP70-9/HSCA1 AND ISU1, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19865480; DOI=10.1371/journal.pone.0007662;
RA Xu X.M., Lin H., Latijnhouwers M., Moeller S.G.;
RT "Dual localized AtHscB involved in iron sulfur protein biogenesis in
RT Arabidopsis.";
RL PLoS ONE 4:E7662-E7662(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27655366; DOI=10.1007/s11103-016-0537-9;
RA Leaden L., Pagani M.A., Balparda M., Busi M.V., Gomez-Casati D.F.;
RT "Altered levels of AtHSCB disrupts iron translocation from roots to
RT shoots.";
RL Plant Mol. Biol. 92:613-628(2016).
CC -!- FUNCTION: Co-chaperone required for the assembly of iron-sulfur [Fe-S]
CC clusters in both mitochondria and cytosol (PubMed:19865480). Required
CC for the activity of iron-sulfur proteins such as aconitase and
CC succinate dehydrogenase (PubMed:19865480). Involved in iron homeostasis
CC and may take part in the control of iron translocation from roots to
CC shoots (PubMed:27655366). {ECO:0000269|PubMed:19865480,
CC ECO:0000269|PubMed:27655366}.
CC -!- SUBUNIT: Interacts with ISU1 and HSP70-9/HSCA1.
CC {ECO:0000269|PubMed:19865480}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19865480}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:19865480}.
CC -!- DISRUPTION PHENOTYPE: Floral stems lacking the epicuticular wax layer,
CC distorted leaf trichomes, and under-developed siliques with shrunked
CC and non-viable seeds (PubMed:19865480). Strong reduction of the
CC activity of iron-sulfur proteins such as aconitase and succinate
CC dehydrogenase (PubMed:19865480). {ECO:0000269|PubMed:19865480}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08963.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006700; BAB08963.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91011.1; -; Genomic_DNA.
DR EMBL; AY128407; AAM91610.1; -; mRNA.
DR EMBL; BT000065; AAN15384.1; -; mRNA.
DR RefSeq; NP_196259.2; NM_120724.3.
DR AlphaFoldDB; Q8L7K4; -.
DR SMR; Q8L7K4; -.
DR IntAct; Q8L7K4; 1.
DR STRING; 3702.AT5G06410.1; -.
DR SwissPalm; Q8L7K4; -.
DR PaxDb; Q8L7K4; -.
DR PRIDE; Q8L7K4; -.
DR ProteomicsDB; 193285; -.
DR EnsemblPlants; AT5G06410.1; AT5G06410.1; AT5G06410.
DR GeneID; 830529; -.
DR Gramene; AT5G06410.1; AT5G06410.1; AT5G06410.
DR KEGG; ath:AT5G06410; -.
DR Araport; AT5G06410; -.
DR TAIR; locus:2164310; AT5G06410.
DR eggNOG; KOG3192; Eukaryota.
DR HOGENOM; CLU_068529_0_0_1; -.
DR InParanoid; Q8L7K4; -.
DR OMA; SCRCIQP; -.
DR OrthoDB; 1129824at2759; -.
DR PhylomeDB; Q8L7K4; -.
DR PRO; PR:Q8L7K4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7K4; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.1280.20; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
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; PF07743; HSCB_C; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF47144; SSF47144; 1.
DR TIGRFAMs; TIGR00714; hscB; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..252
FT /note="Iron-sulfur cluster co-chaperone protein HscB
FT homolog"
FT /id="PRO_0000446286"
FT DOMAIN 93..165
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ SEQUENCE 252 AA; 28931 MW; 2A47F10344FDF188 CRC64;
MKKTKTMVAS ISTLIRRTYP STNQCNSLAT IQSQTQLPRE SLQHHSSAEG RLRFSGRVFC
SESGAGCWNC GEKAAFLFCN SCRSIQPVDD SVDYFQIFGL EKKYEIDPGS LEGKYKDWQK
KLHPDLVHNK SKKERDYAAE QSAKVTEACR TLTKRLSRAM YIMKLNGVNV NEEETITDPT
LLMEIMELRE AISEADDSTS LNQIRSQVQE KLKQWSDSFV EAFESQKFDD AVKCIQRMTY
YERACEEILK KL
