位置:首页 > 蛋白库 > SDHF1_MOUSE
SDHF1_MOUSE
ID   SDHF1_MOUSE             Reviewed;         118 AA.
AC   Q3U276; B2RVF8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Succinate dehydrogenase assembly factor 1, mitochondrial {ECO:0000250|UniProtKB:A6NFY7};
DE            Short=SDH assembly factor 1 {ECO:0000250|UniProtKB:A6NFY7};
DE            Short=SDHAF1 {ECO:0000250|UniProtKB:A6NFY7};
DE   AltName: Full=LYR motif-containing protein 8 {ECO:0000250|UniProtKB:A6NFY7};
GN   Name=Sdhaf1 {ECO:0000250|UniProtKB:A6NFY7};
GN   Synonyms=Lyrm8 {ECO:0000250|UniProtKB:A6NFY7};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Liver, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Promotes maturation of the iron-sulfur
CC       protein subunit Sdhb of the SDH catalytic dimer, protecting it from the
CC       deleterious effects of oxidants. May act together with SDHAF3.
CC       Contributes to iron-sulfur cluster incorporation into SDHB by binding
CC       to SDHB and recruiting the iron-sulfur transfer complex formed by
CC       HSC20, HSPA9 and ISCU through direct binding to HSC20.
CC       {ECO:0000250|UniProtKB:A6NFY7}.
CC   -!- SUBUNIT: Interacts with SDHB within an SDHA-SDHB subcomplex. Also
CC       interacts with the iron-sulfur transfer complex formed by HSC20, HSPA9
CC       and ISCU through direct binding to HSC20. Binding of SDHAF1 to SDHB
CC       precedes and is necessary for recruitment of the iron-sulfur transfer
CC       complex by SDHAF1. {ECO:0000250|UniProtKB:Q3E785}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:A6NFY7}.
CC   -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF1 subfamily.
CC       {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; AK155437; BAE33266.1; -; mRNA.
DR   EMBL; BC147173; AAI47174.1; -; mRNA.
DR   EMBL; BC147174; AAI47175.1; -; mRNA.
DR   CCDS; CCDS39881.1; -.
DR   RefSeq; NP_001028312.2; NM_001033140.3.
DR   AlphaFoldDB; Q3U276; -.
DR   SMR; Q3U276; -.
DR   STRING; 10090.ENSMUSP00000096185; -.
DR   PhosphoSitePlus; Q3U276; -.
DR   EPD; Q3U276; -.
DR   MaxQB; Q3U276; -.
DR   PaxDb; Q3U276; -.
DR   PeptideAtlas; Q3U276; -.
DR   PRIDE; Q3U276; -.
DR   ProteomicsDB; 253432; -.
DR   Antibodypedia; 44606; 199 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000098586; ENSMUSP00000096185; ENSMUSG00000074211.
DR   GeneID; 68332; -.
DR   KEGG; mmu:68332; -.
DR   UCSC; uc009ged.1; mouse.
DR   CTD; 644096; -.
DR   MGI; MGI:1915582; Sdhaf1.
DR   VEuPathDB; HostDB:ENSMUSG00000074211; -.
DR   eggNOG; KOG4620; Eukaryota.
DR   GeneTree; ENSGT00940000157289; -.
DR   HOGENOM; CLU_154777_0_1_1; -.
DR   InParanoid; Q3U276; -.
DR   OMA; FRENARI; -.
DR   OrthoDB; 1638205at2759; -.
DR   PhylomeDB; Q3U276; -.
DR   TreeFam; TF344152; -.
DR   BioGRID-ORCS; 68332; 2 hits in 38 CRISPR screens.
DR   PRO; PR:Q3U276; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3U276; protein.
DR   Bgee; ENSMUSG00000074211; Expressed in ileal epithelium and 233 other tissues.
DR   Genevisible; Q3U276; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; ISS:UniProtKB.
DR   CDD; cd20268; Complex1_LYR_SDHAF1_LYRM8; 1.
DR   InterPro; IPR008011; Complex1_LYR_dom.
DR   InterPro; IPR045295; Complex1_LYR_SDHAF1_LYRM8.
DR   Pfam; PF05347; Complex1_LYR; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Mitochondrion; Reference proteome; Repeat.
FT   CHAIN           1..118
FT                   /note="Succinate dehydrogenase assembly factor 1,
FT                   mitochondrial"
FT                   /id="PRO_0000327917"
FT   REGION          53..65
FT                   /note="Interaction with SDHB"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
FT   REGION          68..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           14..16
FT                   /note="LYR motif 1; required for interaction with HSC20"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
FT   MOTIF           53..55
FT                   /note="LYR motif 2; not required for interaction with
FT                   HSC20"
FT                   /evidence="ECO:0000250|UniProtKB:A6NFY7"
SQ   SEQUENCE   118 AA;  13142 MW;  C1491206E577BCFA CRC64;
     MSRPSRLQRQ VLSLYRELLR AGRGTPGAEA RVRAEFRQHA SLPRTDVLRI EYLYRRGRRQ
     LQLLRSGHAT AMGTFVRPRG PAEEPGDATA PGTRLDDGGA PKNSCEDTGA RETRSDGR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024