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L2HDH_MOUSE
ID   L2HDH_MOUSE             Reviewed;         464 AA.
AC   Q91YP0; Q3TH61; Q3U7Z0; Q3ULY6;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial;
DE            EC=1.1.99.2;
DE   AltName: Full=Duranin;
DE   Flags: Precursor;
GN   Name=L2hgdh;
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=C57BL/6J; TISSUE=Amnion, Bone marrow, and Mammary gland;
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   STRAIN=FVB/N; TISSUE=Mammary tumor;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC   and Testis;
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).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-174, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC         Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000305}.
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DR   EMBL; AK145228; BAE26312.1; -; mRNA.
DR   EMBL; AK152450; BAE31229.1; -; mRNA.
DR   EMBL; AK168429; BAE40337.1; -; mRNA.
DR   EMBL; BC016226; AAH16226.1; -; mRNA.
DR   CCDS; CCDS25953.1; -.
DR   RefSeq; NP_663418.1; NM_145443.2.
DR   AlphaFoldDB; Q91YP0; -.
DR   SMR; Q91YP0; -.
DR   STRING; 10090.ENSMUSP00000021370; -.
DR   iPTMnet; Q91YP0; -.
DR   PhosphoSitePlus; Q91YP0; -.
DR   SwissPalm; Q91YP0; -.
DR   EPD; Q91YP0; -.
DR   jPOST; Q91YP0; -.
DR   MaxQB; Q91YP0; -.
DR   PaxDb; Q91YP0; -.
DR   PeptideAtlas; Q91YP0; -.
DR   PRIDE; Q91YP0; -.
DR   ProteomicsDB; 264823; -.
DR   Antibodypedia; 47264; 190 antibodies from 26 providers.
DR   DNASU; 217666; -.
DR   Ensembl; ENSMUST00000021370; ENSMUSP00000021370; ENSMUSG00000020988.
DR   GeneID; 217666; -.
DR   KEGG; mmu:217666; -.
DR   UCSC; uc011ynb.1; mouse.
DR   CTD; 79944; -.
DR   MGI; MGI:2384968; L2hgdh.
DR   VEuPathDB; HostDB:ENSMUSG00000020988; -.
DR   eggNOG; KOG2665; Eukaryota.
DR   GeneTree; ENSGT00490000043421; -.
DR   HOGENOM; CLU_024775_0_0_1; -.
DR   InParanoid; Q91YP0; -.
DR   OMA; GVHFTRM; -.
DR   OrthoDB; 1310154at2759; -.
DR   PhylomeDB; Q91YP0; -.
DR   TreeFam; TF105922; -.
DR   Reactome; R-MMU-880009; Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
DR   BioGRID-ORCS; 217666; 2 hits in 69 CRISPR screens.
DR   ChiTaRS; L2hgdh; mouse.
DR   PRO; PR:Q91YP0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q91YP0; protein.
DR   Bgee; ENSMUSG00000020988; Expressed in right kidney and 237 other tissues.
DR   ExpressionAtlas; Q91YP0; baseline and differential.
DR   Genevisible; Q91YP0; MM.
DR   GO; GO:0016021; C:integral component of membrane; ISS:HGNC-UCL.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; ISS:HGNC-UCL.
DR   GO; GO:0044281; P:small molecule metabolic process; ISS:HGNC-UCL.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..464
FT                   /note="L-2-hydroxyglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000228130"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        184
FT                   /note="M -> I (in Ref. 1; BAE31229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="R -> K (in Ref. 1; BAE26312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="I -> V (in Ref. 1; BAE26312)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="E -> G (in Ref. 1; BAE31229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="L -> P (in Ref. 1; BAE40337)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  50899 MW;  27270B28FCCC3762 CRC64;
     MWPTLRYVGG VCGLARYCVA GGFLRASGPA SGVPGLLCGG GRRSSSTSSF DIVIVGGGIV
     GLASARTLIL KHPGLSIGVV EKEKDLALHQ TGHNSGVIHS GIYYKPESLK AKLCVEGAAL
     IYEYCNLKGI PYRQCGKLIV AVEQEEIPRL QALYERGLQN GVEGLRLIQQ EDIKKKEPYC
     RGLMAIDCPY TGIVNYQQVA LSFAQDFQEA GGSILRDFEV KGIEIAKENS SRSKDGMNYP
     IAVKNSKGKE IRCRYVVTCA GLYSDRISEL SGCNPDPQIV PFRGDYLVLK PEKGYLVKGN
     IYPVPDSRFP FLGVHFTPRL DGTIWLGPNA VLAFKREGYR PFDFDARDVM EVILKSGFIN
     LVFQHFSYGV NEMYKACFLS ETVKHLQKFI PEITISDVLR GPAGVRAQAL DRDGNLVEDF
     VFDGGTGEIA DRVLHVRNAP SPAATSSLAI SRMIAEEAQQ RFKL
 
 
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