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SDSL_MOUSE
ID   SDSL_MOUSE              Reviewed;         329 AA.
AC   Q8R238; Q8VI05;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Serine dehydratase-like;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE   AltName: Full=L-serine dehydratase/L-threonine deaminase;
DE   AltName: Full=L-threonine dehydratase;
DE            Short=TDH;
DE            EC=4.3.1.19;
DE   AltName: Full=SDH;
GN   Name=Sdsl; Synonyms=Sds;
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 [MRNA].
RC   STRAIN=C3H/HeJ;
RX   PubMed=12080145; DOI=10.1073/pnas.142287799;
RA   Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA   Brinton M.A.;
RT   "Positional cloning of the murine flavivirus resistance gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   TISSUE SPECIFICITY.
RX   PubMed=15757516; DOI=10.1186/1471-2164-6-32;
RA   Edgar A.J.;
RT   "Mice have a transcribed L-threonine aldolase/GLY1 gene, but the human GLY1
RT   gene is a non-processed pseudogene.";
RL   BMC Genomics 6:32-32(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Pancreas, Spleen, 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).
CC   -!- FUNCTION: Has low serine dehydratase and threonine dehydratase
CC       activity. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in liver.
CC       {ECO:0000269|PubMed:15757516}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL56988.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF328927; AAL56988.1; ALT_FRAME; mRNA.
DR   EMBL; BC022601; AAH22601.1; -; mRNA.
DR   CCDS; CCDS19618.1; -.
DR   RefSeq; NP_598663.2; NM_133902.2.
DR   RefSeq; XP_011246504.2; XM_011248202.2.
DR   RefSeq; XP_011246505.1; XM_011248203.2.
DR   AlphaFoldDB; Q8R238; -.
DR   SMR; Q8R238; -.
DR   BioGRID; 232990; 2.
DR   STRING; 10090.ENSMUSP00000058198; -.
DR   iPTMnet; Q8R238; -.
DR   PhosphoSitePlus; Q8R238; -.
DR   MaxQB; Q8R238; -.
DR   PaxDb; Q8R238; -.
DR   PeptideAtlas; Q8R238; -.
DR   PRIDE; Q8R238; -.
DR   ProteomicsDB; 255508; -.
DR   Antibodypedia; 31274; 300 antibodies from 26 providers.
DR   DNASU; 257635; -.
DR   Ensembl; ENSMUST00000031594; ENSMUSP00000031594; ENSMUSG00000029596.
DR   Ensembl; ENSMUST00000052258; ENSMUSP00000058198; ENSMUSG00000029596.
DR   GeneID; 257635; -.
DR   KEGG; mmu:257635; -.
DR   UCSC; uc008zhe.1; mouse.
DR   CTD; 113675; -.
DR   MGI; MGI:2182607; Sdsl.
DR   VEuPathDB; HostDB:ENSMUSG00000029596; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   GeneTree; ENSGT00940000160713; -.
DR   HOGENOM; CLU_021152_3_0_1; -.
DR   InParanoid; Q8R238; -.
DR   OMA; DALQPCG; -.
DR   OrthoDB; 1199679at2759; -.
DR   PhylomeDB; Q8R238; -.
DR   TreeFam; TF329014; -.
DR   Reactome; R-MMU-8849175; Threonine catabolism.
DR   BioGRID-ORCS; 257635; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Sdsl; mouse.
DR   PRO; PR:Q8R238; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8R238; protein.
DR   Bgee; ENSMUSG00000029596; Expressed in ileal epithelium and 133 other tissues.
DR   ExpressionAtlas; Q8R238; baseline and differential.
DR   Genevisible; Q8R238; MM.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Lipid metabolism; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..329
FT                   /note="Serine dehydratase-like"
FT                   /id="PRO_0000264625"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GA7"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  34732 MW;  A2F7FB869350B43B CRC64;
     MEGALAERVG AEPFHRVTPL LESWALSQVA GMPVFLKYEN VQIAGSFKIR GIGHFCQQMA
     KRGCRHLVCS SGGNAGIAAA YSARKLGIPV TIVLPEGTSV QVVRRLEGEG AEVQLTGKVW
     DEANVKAQEL ATRDGWVNVS PFDHPLIWEG HASLVRELKE SLGTPPGAVV LAVGGGGLLA
     GVTAGLLEVG WQHVPIVAME TRGAHSFNSA LQAGRPVTLP DITSVAKSLG AKTVAARTLE
     CAKECEVLSE VVEDREAVSA VQRFLDDERM LVEPACGAAL AAIYSGILWR LQAEGRLSSA
     LASVVVIVCG GNNISSQQLQ ELKIQLGCS
 
 
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