ISCAP_ARATH
ID ISCAP_ARATH Reviewed; 180 AA.
AC Q9XIK3; Q6NM99;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Iron-sulfur assembly protein IscA, chloroplastic;
DE AltName: Full=Plastid SufA-like protein;
DE AltName: Full=Protein scaffold protein AtCpIscA;
DE Flags: Precursor;
GN Name=ISCA; OrderedLocusNames=At1g10500; ORFNames=T10O24.11;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=15888686; DOI=10.1104/pp.104.058602;
RA Abdel-Ghany S.E., Ye H., Garifullina G.F., Zhang L., Pilon-Smits E.A.H.,
RA Pilon M.;
RT "Iron-sulfur cluster biogenesis in chloroplasts. Involvement of the
RT scaffold protein CpIscA.";
RL Plant Physiol. 138:161-172(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the assembly of chloroplastic iron-sulfur
CC proteins. Is able to transfer iron-sulfur clusters to apo-ferredoxin.
CC {ECO:0000269|PubMed:15888686}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per dimer. The dimer may bind additional iron
CC ions. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; may form tetramers and higher multimers.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15888686}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression level in green,
CC photosynthetic tissues. {ECO:0000269|PubMed:15888686}.
CC -!- SIMILARITY: Belongs to the HesB/IscA family. Ycf83 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39571.1; 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; AY971959; AAY40769.1; -; mRNA.
DR EMBL; AC007067; AAD39571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28586.1; -; Genomic_DNA.
DR EMBL; BT010894; AAR24672.1; -; mRNA.
DR EMBL; BT011763; AAS65934.1; -; mRNA.
DR PIR; F86238; F86238.
DR RefSeq; NP_172520.1; NM_100924.3.
DR AlphaFoldDB; Q9XIK3; -.
DR SMR; Q9XIK3; -.
DR STRING; 3702.AT1G10500.1; -.
DR PaxDb; Q9XIK3; -.
DR PRIDE; Q9XIK3; -.
DR ProteomicsDB; 247134; -.
DR EnsemblPlants; AT1G10500.1; AT1G10500.1; AT1G10500.
DR GeneID; 837590; -.
DR Gramene; AT1G10500.1; AT1G10500.1; AT1G10500.
DR KEGG; ath:AT1G10500; -.
DR Araport; AT1G10500; -.
DR TAIR; locus:2194594; AT1G10500.
DR eggNOG; KOG1120; Eukaryota.
DR HOGENOM; CLU_069054_3_0_1; -.
DR InParanoid; Q9XIK3; -.
DR OMA; FSAITTH; -.
DR OrthoDB; 1360948at2759; -.
DR PhylomeDB; Q9XIK3; -.
DR PRO; PR:Q9XIK3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIK3; baseline and differential.
DR Genevisible; Q9XIK3; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
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 InterPro; IPR031108; ISCA_plant_cyanobact.
DR PANTHER; PTHR47265; PTHR47265; 1.
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 Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..180
FT /note="Iron-sulfur assembly protein IscA, chloroplastic"
FT /id="PRO_0000077033"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0AAC8"
SQ SEQUENCE 180 AA; 19337 MW; FAF5D859F06B7AFF CRC64;
MAFATGITTS SNPTFLGLKI SNTSLRSVVS CNSISFPSLS YVNLNLNRRN RLSVRSASVP
AAPAMEGLKP AISLSENALK HLSKMRSERG EDLCLRIGVK QGGCSGMSYT MDFENRANAR
PDDSTIEYQG FTIVCDPKSM LFLFGMQLDY SDALIGGGFS FSNPNATQTC GCGKSFAAEM