SARDH_MOUSE
ID SARDH_MOUSE Reviewed; 919 AA.
AC Q99LB7;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sarcosine dehydrogenase, mitochondrial {ECO:0000305};
DE Short=SarDH;
DE EC=1.5.8.3 {ECO:0000250|UniProtKB:Q64380};
DE Flags: Precursor;
GN Name=Sardh {ECO:0000312|MGI:MGI:2183102};
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=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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, 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 [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-38; LYS-174; LYS-278; LYS-378;
RP LYS-392; LYS-535; LYS-803; LYS-885 AND LYS-905, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-560; LYS-776; LYS-803;
RP LYS-885 AND LYS-905, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 -!- FUNCTION: Catalyzes the last step of the oxidative degradation of
CC choline to glycine. Converts sarcosine into glycine.
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + H(+) +
CC oxidized [electron-transfer flavoprotein] + sarcosine = (6R)-5,10-
CC methylenetetrahydrofolyl-(gamma-L-Glu)(n) + glycine + reduced
CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:19793, Rhea:RHEA-
CC COMP:10685, Rhea:RHEA-COMP:10686, Rhea:RHEA-COMP:13257, Rhea:RHEA-
CC COMP:14738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:136572,
CC ChEBI:CHEBI:141005; EC=1.5.8.3;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19794;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q64380};
CC Note=Binds 1 FAD covalently per monomer.
CC {ECO:0000250|UniProtKB:Q64380};
CC -!- PATHWAY: Amine and polyamine degradation; sarcosine degradation;
CC formaldehyde and glycine from sarcosine: step 1/1.
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q64380}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; BC003456; AAH03456.1; -; mRNA.
DR CCDS; CCDS15826.1; -.
DR RefSeq; NP_619606.1; NM_138665.2.
DR RefSeq; XP_006497851.1; XM_006497788.3.
DR RefSeq; XP_006497852.1; XM_006497789.3.
DR AlphaFoldDB; Q99LB7; -.
DR SMR; Q99LB7; -.
DR BioGRID; 228656; 1.
DR STRING; 10090.ENSMUSP00000099950; -.
DR iPTMnet; Q99LB7; -.
DR PhosphoSitePlus; Q99LB7; -.
DR SwissPalm; Q99LB7; -.
DR jPOST; Q99LB7; -.
DR MaxQB; Q99LB7; -.
DR PaxDb; Q99LB7; -.
DR PRIDE; Q99LB7; -.
DR ProteomicsDB; 253397; -.
DR Antibodypedia; 31926; 67 antibodies from 17 providers.
DR DNASU; 192166; -.
DR Ensembl; ENSMUST00000102886; ENSMUSP00000099950; ENSMUSG00000009614.
DR GeneID; 192166; -.
DR KEGG; mmu:192166; -.
DR UCSC; uc008ixg.2; mouse.
DR CTD; 1757; -.
DR MGI; MGI:2183102; Sardh.
DR VEuPathDB; HostDB:ENSMUSG00000009614; -.
DR eggNOG; KOG2844; Eukaryota.
DR GeneTree; ENSGT00940000157589; -.
DR HOGENOM; CLU_007884_11_4_1; -.
DR InParanoid; Q99LB7; -.
DR OMA; PMKHAYI; -.
DR OrthoDB; 813396at2759; -.
DR PhylomeDB; Q99LB7; -.
DR TreeFam; TF314735; -.
DR Reactome; R-MMU-6798163; Choline catabolism.
DR UniPathway; UPA00292; UER00398.
DR BioGRID-ORCS; 192166; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sardh; mouse.
DR PRO; PR:Q99LB7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99LB7; protein.
DR Bgee; ENSMUSG00000009614; Expressed in left lobe of liver and 159 other tissues.
DR ExpressionAtlas; Q99LB7; baseline and differential.
DR Genevisible; Q99LB7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR GO; GO:0005542; F:folic acid binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008480; F:sarcosine dehydrogenase activity; ISO:MGI.
DR GO; GO:1901053; P:sarcosine catabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; ISO:MGI.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..919
FT /note="Sarcosine dehydrogenase, mitochondrial"
FT /id="PRO_0000010771"
FT MOD_RES 38
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 109
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 278
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 378
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 535
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 560
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 778
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL12"
FT MOD_RES 803
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 803
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 885
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 885
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 905
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 905
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 919 AA; 101682 MW; 4908ACB540C9D305 CRC64;
MASLSRVLRV AATCPRGRAA WNLGLQPLAT EARPTTEKSV PYQRTLKEEA QGASVVPQGP
SQPLPSTANV VVIGGGSLGC QTLYHLAKLG VGGAVLLERE RLTSGTTWHT AGLLWQLRPS
DVEVELLAHT RQVVSRDLEE ETGLHTGWIQ NGGLFIASNQ QRLNEYKRLM SLGKAYGIES
HVLSPAETKS LYPLMNVDDL YGTLYVPQDG TMDPAGTCTT LTRAAVARGA QVIENCAVTG
IRVRTDDFGV RRVAAVETEH GSIQTPCVVN CAGVWASKVG RMAGVKVPLV AMHHAYVVTE
RIEGIQNMPN VRDHDASVYL RLQGDALSVG GYEANPIFWE EVSDKFAFGL FDLDWDVFTQ
HIEGAINRVP VLEKTGIKST VCGPESFTPD HKPLMGEAPE LRGFFLGCGF NSAGMMLGGG
CGQELAHWIV HGRPEKDMYS YDIRRFHHSL TDHTRWIRER SHESYAKNYS VVFPHDEPLA
GRNMRRDPLH EELLGQGCVF QERQGWERPG WFNPQETAQV LDYDYYGAYG NQAHKDYTYS
RLLGDEYTFD FPPHHHMIQK ECLACRGAAA VFNMSYFGKF YLLGVDARKA ADWLFSADVN
RPPGSTVYTC MLNQRGGTES DLTVSRLAPG TQASPLVPAF EGDCYYLAVG GAVAQHNWSH
INTVLQDQEF RCQLMDSSED LGMLSIQGPA SRDILQDVLD ADLSNEAFPF STHQLVRAAG
HLVRAIRLSF VGELGWELHV PRASCLPVYR AVMAAGARHG LVNAGYRAID SLSIEKGYRH
WHADLRPDDS PLEAGLAFTC KLKTSVPFLG REALEKQRAT GLRRRLICLT VEEEVPMFGL
EAIWRNGQVV GHVRRADFGF TVNKTIAYGY IRDPSGGPVS LDFVKNGEYA LERMGVTYAA
QVHLKSPFDP DNKRVKGIY
