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SDHF2_CAEBR
ID   SDHF2_CAEBR             Reviewed;         122 AA.
AC   A8XYZ2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDH assembly factor 2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDHAF2 {ECO:0000255|HAMAP-Rule:MF_03057};
GN   ORFNames=CBG20928;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. Required for flavinylation (covalent
CC       attachment of FAD) of the flavoprotein subunit of the SDH catalytic
CC       dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC   -!- SUBUNIT: Interacts with the flavoprotein subunit within the SDH
CC       catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
CC   -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
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DR   EMBL; HE600928; CAP37859.1; -; Genomic_DNA.
DR   RefSeq; XP_002631726.1; XM_002631680.1.
DR   AlphaFoldDB; A8XYZ2; -.
DR   SMR; A8XYZ2; -.
DR   STRING; 6238.CBG20928; -.
DR   EnsemblMetazoa; CBG20928.1; CBG20928.1; WBGene00039830.
DR   GeneID; 8573725; -.
DR   KEGG; cbr:CBG_20928; -.
DR   CTD; 8573725; -.
DR   WormBase; CBG20928; CBP20012; WBGene00039830; -.
DR   eggNOG; KOG3326; Eukaryota.
DR   HOGENOM; CLU_103054_1_0_1; -.
DR   InParanoid; A8XYZ2; -.
DR   OMA; HMEWDLF; -.
DR   OrthoDB; 1492851at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   HAMAP; MF_03057; SDHAF2; 1.
DR   InterPro; IPR005631; SDH.
DR   InterPro; IPR036714; SDH_sf.
DR   InterPro; IPR028882; SDHAF2.
DR   Pfam; PF03937; Sdh5; 1.
DR   SUPFAM; SSF109910; SSF109910; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Succinate dehydrogenase assembly factor 2,
FT                   mitochondrial"
FT                   /id="PRO_0000383184"
SQ   SEQUENCE   122 AA;  14205 MW;  DD3709B34D362CB5 CRC64;
     MTTLLGPITR RFLSATQIAR SLTRAEVPGE QLDAKRARLL YQSKKRGILE NDILLGNFAE
     ENLKKMSEPE LKAYDKLING EHMEWDLFYY LSNKKTPPED VEKCSVYQKV KKFVDEKRVP
     RS
 
 
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