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ISAM1_ARATH
ID   ISAM1_ARATH             Reviewed;         137 AA.
AC   Q8LBM4; Q9SLE6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Iron-sulfur assembly protein IscA-like 1, mitochondrial;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g16710; ORFNames=T24I21.12;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   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   [5]
RP   IDENTIFICATION.
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).
CC   -!- FUNCTION: Involved in the assembly of mitochondrial iron-sulfur
CC       proteins. Probably involved in the binding of an intermediate of Fe/S
CC       cluster assembly (By similarity). {ECO:0000250}.
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: Mitochondrion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8LBM4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the HesB/IscA family. {ECO:0000305}.
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DR   EMBL; AC005825; AAD24604.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06528.1; -; Genomic_DNA.
DR   EMBL; BT004789; AAO44055.1; -; mRNA.
DR   EMBL; AY087119; AAM64677.1; -; mRNA.
DR   PIR; C84543; C84543.
DR   RefSeq; NP_179262.1; NM_127223.5. [Q8LBM4-1]
DR   AlphaFoldDB; Q8LBM4; -.
DR   SMR; Q8LBM4; -.
DR   BioGRID; 1529; 2.
DR   IntAct; Q8LBM4; 2.
DR   STRING; 3702.AT2G16710.3; -.
DR   SwissPalm; Q8LBM4; -.
DR   PaxDb; Q8LBM4; -.
DR   ProteomicsDB; 247296; -. [Q8LBM4-1]
DR   EnsemblPlants; AT2G16710.1; AT2G16710.1; AT2G16710. [Q8LBM4-1]
DR   GeneID; 816172; -.
DR   Gramene; AT2G16710.1; AT2G16710.1; AT2G16710. [Q8LBM4-1]
DR   KEGG; ath:AT2G16710; -.
DR   Araport; AT2G16710; -.
DR   eggNOG; KOG1120; Eukaryota.
DR   HOGENOM; CLU_069054_4_1_1; -.
DR   InParanoid; Q8LBM4; -.
DR   PhylomeDB; Q8LBM4; -.
DR   PRO; PR:Q8LBM4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8LBM4; baseline and differential.
DR   Genevisible; Q8LBM4; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR   GO; GO:0097428; P:protein maturation by iron-sulfur 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   2: Evidence at transcript level;
KW   Alternative splicing; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..137
FT                   /note="Iron-sulfur assembly protein IscA-like 1,
FT                   mitochondrial"
FT                   /id="PRO_0000223684"
FT   BINDING         54
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         118
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAC8"
FT   CONFLICT        6
FT                   /note="I -> V (in Ref. 4; AAM64677)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   137 AA;  14985 MW;  F80010A06663E314 CRC64;
     MKASQILAAA AARVGPALRK QVLTLTDEAA SRVHHLLQQR QKPFLRLGVK ARGCNGLSYT
     LNYADEKGKF DELVEEKGVR ILVEPKALMH VIGTKMDFVD DKLRSEFVFI NPNSQGQCGC
     GESFMTTSTS SAKQSAS
 
 
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