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SDAF2_ARATH
ID   SDAF2_ARATH             Reviewed;         188 AA.
AC   Q9FI44; Q8LBK3;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000305};
DE            Short=SDH assembly factor 2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=SDHAF2; OrderedLocusNames=At5g51040 {ECO:0000312|Araport:AT5G51040};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(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;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23036115; DOI=10.1111/tpj.12041;
RA   Huang S., Taylor N.L., Stroher E., Fenske R., Millar A.H.;
RT   "Succinate dehydrogenase assembly factor 2 is needed for assembly and
RT   activity of mitochondrial complex II and for normal root elongation in
RT   Arabidopsis.";
RL   Plant J. 73:429-441(2013).
RN   [7]
RP   FUNCTION.
RX   PubMed=23154507; DOI=10.4161/psb.22815;
RA   Huang S., Millar A.H.;
RT   "Sequence diversity and conservation in factors influencing succinate
RT   dehydrogenase flavinylation.";
RL   Plant Signal. Behav. 8:E22815-E22815(2013).
CC   -!- FUNCTION: Plays an essential role in the assembly of succinate
CC       dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC       complex II) that is a component of both the tricarboxylic acid (TCA)
CC       cycle and the mitochondrial electron transport chain, and which couples
CC       the oxidation of succinate to fumarate with the reduction of ubiquinone
CC       (coenzyme Q) to ubiquinol (PubMed:23036115). Required for flavinylation
CC       (covalent attachment of FAD) of the flavoprotein subunit of the SDH
CC       catalytic dimer (PubMed:23036115, PubMed:23154507).
CC       {ECO:0000269|PubMed:23036115, ECO:0000269|PubMed:23154507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
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=Q9FI44-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Inhibition of primary root elongation and early
CC       lateral root emergence. {ECO:0000269|PubMed:23036115}.
CC   -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000305}.
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DR   EMBL; AB017063; BAB08750.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96024.1; -; Genomic_DNA.
DR   EMBL; BT025542; ABF58960.1; -; mRNA.
DR   EMBL; AK229201; BAF01071.1; -; mRNA.
DR   EMBL; AY087157; AAM64715.1; -; mRNA.
DR   RefSeq; NP_199917.1; NM_124483.3. [Q9FI44-1]
DR   AlphaFoldDB; Q9FI44; -.
DR   SMR; Q9FI44; -.
DR   STRING; 3702.AT5G51040.3; -.
DR   PaxDb; Q9FI44; -.
DR   PRIDE; Q9FI44; -.
DR   ProteomicsDB; 232922; -. [Q9FI44-1]
DR   EnsemblPlants; AT5G51040.1; AT5G51040.1; AT5G51040. [Q9FI44-1]
DR   GeneID; 835177; -.
DR   Gramene; AT5G51040.1; AT5G51040.1; AT5G51040. [Q9FI44-1]
DR   KEGG; ath:AT5G51040; -.
DR   Araport; AT5G51040; -.
DR   eggNOG; KOG3326; Eukaryota.
DR   PhylomeDB; Q9FI44; -.
DR   PRO; PR:Q9FI44; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FI44; baseline and differential.
DR   Genevisible; Q9FI44; AT.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR   GO; GO:0018293; P:protein-FAD linkage; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 1.10.150.250; -; 1.
DR   InterPro; IPR005631; SDH.
DR   InterPro; IPR036714; SDH_sf.
DR   Pfam; PF03937; Sdh5; 1.
DR   SUPFAM; SSF109910; SSF109910; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..188
FT                   /note="Succinate dehydrogenase assembly factor 2,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431760"
FT   CONFLICT        182
FT                   /note="A -> T (in Ref. 5; AAM64715)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21276 MW;  07F7DED3A815BBF7 CRC64;
     MATRKALINV HRIIRSTAVV GRSSIIPAAA NRSYPIIFRN GVDLGARFFC ENTASAQNFD
     IDLSNEENKR RTINRLLYRS KQRGFLELDL VLGNWVEENV NSMDENGVKS LIHVLNLENP
     DLWKWLTEQE QPPEAVSSNP VFSALHEKVM KNLNKHAAPE TRAAAGQPWV RGWDDFKRGR
     DAPISGNQ
 
 
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