HF101_ARATH
ID HF101_ARATH Reviewed; 532 AA.
AC Q6STH5; Q8LD16; Q9LK00;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fe-S cluster assembly factor HCF101, chloroplastic;
DE AltName: Full=Protein HIGH CHLOROPHYLL FLUORESCENCE 101;
DE Flags: Precursor;
GN Name=HCF101; OrderedLocusNames=At3g24430; ORFNames=K7M2.22;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=14645254; DOI=10.1074/jbc.m309246200;
RA Stockel J., Oelmuller R.;
RT "A novel protein for photosystem I biogenesis.";
RL J. Biol. Chem. 279:10243-10251(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14690502; DOI=10.1046/j.1365-313x.2003.01952.x;
RA Lezhneva L., Amann K., Meurer J.;
RT "The universally conserved HCF101 protein is involved in assembly of [4Fe-
RT 4S]-cluster-containing complexes in Arabidopsis thaliana chloroplasts.";
RL Plant J. 37:174-185(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF CYS-128; CYS-347 AND CYS-419.
RX PubMed=19817716; DOI=10.1042/bj20091290;
RA Schwenkert S., Netz D.J., Frazzon J., Pierik A.J., Bill E., Gross J.,
RA Lill R., Meurer J.;
RT "Chloroplast HCF101 is a scaffold protein for [4Fe-4S] cluster assembly.";
RL Biochem. J. 425:207-214(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-62, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-61, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Required for photosystem I (PSI) biosynthesis and assembly.
CC May serve as a chloroplast scaffold protein that specifically assembles
CC iron-sulfur (4Fe-4S) clusters and transfers them to the chloroplast PSI
CC and ferredoxin-thioredoxin (FTR) complexes. Can assemble a 4Fe-4S
CC cluster and transfer it to apoproteins in yeast cells. Probably not
CC required for assembly or stability of plastidic 2Fe-2S clusters.
CC {ECO:0000269|PubMed:14645254, ECO:0000269|PubMed:14690502,
CC ECO:0000269|PubMed:19817716}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:19817716};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:19817716};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:14645254, ECO:0000269|PubMed:14690502}.
CC -!- TISSUE SPECIFICITY: Expressed in aerial tissues exposed to light. Very
CC low expression in roots. {ECO:0000269|PubMed:14645254,
CC ECO:0000269|PubMed:14690502}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality when homozygous due to
CC impaired photosystem I (PSI). {ECO:0000269|PubMed:14645254,
CC ECO:0000269|PubMed:14690502}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ540304; CAD90253.1; -; mRNA.
DR EMBL; AY450358; AAR97892.1; -; mRNA.
DR EMBL; AP000382; BAB02944.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76897.1; -; Genomic_DNA.
DR EMBL; AK226386; BAE98532.1; -; mRNA.
DR EMBL; AY086264; AAM64337.1; -; mRNA.
DR RefSeq; NP_189086.1; NM_113350.3.
DR AlphaFoldDB; Q6STH5; -.
DR SMR; Q6STH5; -.
DR BioGRID; 7365; 3.
DR STRING; 3702.AT3G24430.1; -.
DR iPTMnet; Q6STH5; -.
DR PaxDb; Q6STH5; -.
DR PRIDE; Q6STH5; -.
DR ProteomicsDB; 230329; -.
DR EnsemblPlants; AT3G24430.1; AT3G24430.1; AT3G24430.
DR GeneID; 822033; -.
DR Gramene; AT3G24430.1; AT3G24430.1; AT3G24430.
DR KEGG; ath:AT3G24430; -.
DR Araport; AT3G24430; -.
DR TAIR; locus:2087148; AT3G24430.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_024839_1_2_1; -.
DR InParanoid; Q6STH5; -.
DR OMA; LQYSDIP; -.
DR OrthoDB; 1166096at2759; -.
DR PhylomeDB; Q6STH5; -.
DR PRO; PR:Q6STH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6STH5; baseline and differential.
DR Genevisible; Q6STH5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
DR Gene3D; 3.30.2020.30; -; 1.
DR Gene3D; 3.30.300.130; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR010376; GBBH-like_N.
DR InterPro; IPR038492; GBBH-like_N_sf.
DR InterPro; IPR002744; MIP18-like.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR000808; Mrp_CS.
DR InterPro; IPR044304; NUBPL-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR42961; PTHR42961; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR Pfam; PF06155; GBBH-like_N; 1.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01215; MRP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chloroplast; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 62..532
FT /note="Fe-S cluster assembly factor HCF101, chloroplastic"
FT /id="PRO_0000430161"
FT BINDING 184..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 62
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 128
FT /note="C->S: Loss of iron-sulfur (Fe-S) binding."
FT /evidence="ECO:0000269|PubMed:19817716"
FT MUTAGEN 347
FT /note="C->S: Loss of iron-sulfur (Fe-S) binding."
FT /evidence="ECO:0000269|PubMed:19817716"
FT MUTAGEN 419
FT /note="C->S: Loss of iron-sulfur (Fe-S) binding."
FT /evidence="ECO:0000269|PubMed:19817716"
FT CONFLICT 153
FT /note="V -> L (in Ref. 1; CAD90253 and 6; AAM64337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 57764 MW; 589D2B9C8C44BC91 CRC64;
MPLLHPQSLR HPSFEIQTQR RSNSTTRLLL SHKFLHSQAS IISISRTRIL KRVSQNLSVA
KAASAQASSS VGESVAQTSE KDVLKALSQI IDPDFGTDIV SCGFVKDLGI NEALGEVSFR
LELTTPACPV KDMFENKANE VVAALPWVKK VNVTMSAQPA KPIFAGQLPF GLSRISNIIA
VSSCKGGVGK STVAVNLAYT LAGMGARVGI FDADVYGPSL PTMVNPESRI LEMNPEKKTI
IPTEYMGVKL VSFGFAGQGR AIMRGPMVSG VINQLLTTTE WGELDYLVID MPPGTGDIQL
TLCQVAPLTA AVIVTTPQKL AFIDVAKGVR MFSKLKVPCV AVVENMCHFD ADGKRYYPFG
KGSGSEVVKQ FGIPHLFDLP IRPTLSASGD SGTPEVVSDP LSDVARTFQD LGVCVVQQCA
KIRQQVSTAV TYDKYLKAIR VKVPNSDEEF LLHPATVRRN DRSAQSVDEW TGEQKVLYGD
VAEDIEPEDI RPMGNYAVSI TWPDGFSQIA PYDQLEEIER LVDVPPLSPV EV
