GCSP_MOUSE
ID GCSP_MOUSE Reviewed; 1025 AA.
AC Q91W43;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial {ECO:0000305};
DE EC=1.4.4.2 {ECO:0000250|UniProtKB:P23378};
DE AltName: Full=Glycine cleavage system P protein;
DE AltName: Full=Glycine decarboxylase {ECO:0000250|UniProtKB:P23378};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE Flags: Precursor;
GN Name=Gldc {ECO:0000312|MGI:MGI:1341155};
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 TISSUE=Eye, and Retina;
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 PROTEIN SEQUENCE OF 278-287; 606-615; 878-888 AND 933-942, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Liver;
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-452; LYS-519; LYS-653 AND
RP LYS-669, AND 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 -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein (GLDC) binds the alpha-amino group of glycine
CC through its pyridoxal phosphate cofactor; CO(2) is released and the
CC remaining methylamine moiety is then transferred to the lipoamide
CC cofactor of the H protein (GCSH) (By similarity).
CC {ECO:0000250|UniProtKB:P15505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2;
CC Evidence={ECO:0000250|UniProtKB:P15505};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P15505};
CC -!- ACTIVITY REGULATION: Stimulated by lipoic acid. Inhibited in presence
CC of methylamine (By similarity). {ECO:0000250|UniProtKB:P15505}.
CC -!- SUBUNIT: Interacts with GCSH (By similarity). Homodimer. The glycine
CC cleavage system is composed of four proteins: P (GLDC), T (GCST), L
CC (DLD) and H (GCSH) (By similarity). {ECO:0000250|UniProtKB:P15505}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P15505}.
CC -!- SIMILARITY: Belongs to the GcvP family. {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; BC017135; AAH17135.1; -; mRNA.
DR CCDS; CCDS37956.1; -.
DR RefSeq; NP_613061.1; NM_138595.2.
DR AlphaFoldDB; Q91W43; -.
DR SMR; Q91W43; -.
DR BioGRID; 222425; 8.
DR STRING; 10090.ENSMUSP00000025778; -.
DR iPTMnet; Q91W43; -.
DR PhosphoSitePlus; Q91W43; -.
DR SwissPalm; Q91W43; -.
DR jPOST; Q91W43; -.
DR MaxQB; Q91W43; -.
DR PaxDb; Q91W43; -.
DR PeptideAtlas; Q91W43; -.
DR PRIDE; Q91W43; -.
DR ProteomicsDB; 271204; -.
DR Antibodypedia; 9715; 204 antibodies from 31 providers.
DR DNASU; 104174; -.
DR Ensembl; ENSMUST00000025778; ENSMUSP00000025778; ENSMUSG00000024827.
DR GeneID; 104174; -.
DR KEGG; mmu:104174; -.
DR UCSC; uc008hej.2; mouse.
DR CTD; 2731; -.
DR MGI; MGI:1341155; Gldc.
DR VEuPathDB; HostDB:ENSMUSG00000024827; -.
DR eggNOG; KOG2040; Eukaryota.
DR GeneTree; ENSGT00390000017970; -.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; Q91W43; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 390348at2759; -.
DR PhylomeDB; Q91W43; -.
DR TreeFam; TF300678; -.
DR BRENDA; 1.4.1.27; 3474.
DR Reactome; R-MMU-6783984; Glycine degradation.
DR BioGRID-ORCS; 104174; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Gldc; mouse.
DR PRO; PR:Q91W43; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91W43; protein.
DR Bgee; ENSMUSG00000024827; Expressed in otic placode and 146 other tissues.
DR Genevisible; Q91W43; MM.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0070280; F:pyridoxal binding; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006546; P:glycine catabolic process; ISS:UniProtKB.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:1903442; P:response to lipoic acid; ISS:UniProtKB.
DR GO; GO:0036255; P:response to methylamine; ISS:UniProtKB.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW Pyridoxal phosphate; Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..1025
FT /note="Glycine dehydrogenase (decarboxylating),
FT mitochondrial"
FT /id="PRO_0000010741"
FT REGION 16..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 452
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 653
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 669
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 759
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15505"
SQ SEQUENCE 1025 AA; 113267 MW; BB4A1E3459FE3495 CRC64;
MQLCARAWGL RLGRGAGGGH RLARGTGLSW AQRSRDSSGG GGGGGGGDRG AAGASRLLER
LLPRHDDFSR RHIGPGDKDR REMLQALGLA SIDELIEKTV PASIRLKRPL KMEDPICENE
ILETLHAIAS KNQIWRSYIG MGYYNCSVPQ TILRNLLENS GWVTQYTPYQ PEVSQGRLES
LLNYQTMVSD ITGLDMANAS LLDEATAAAE AMQLCHRHNK RKKFFVDPRC HPQTIAVVQT
RAKYRGVLVE LKLPHEMDFS GKDVCGVLFQ YPDTEGKVED FTELVDRAHQ TGSLTCCATD
LLALCILRPP GEFGVDIALG NSQRFGVPLG YGGPHAAFFA VKENLVRMMP GRMVGVTRDA
TGKEVYRLAL QTREQHIRRD KATSNICTAQ ALLANMAAMF AIYHGSQGLK HIAKRVHNAT
LILSEGLKRA GHQLQHDLFF DTLKVQCGCS VKEVLGRAAQ RQINFRLFDD GTLGISLDET
VTEKDLDDLL WIFGCESSAE LVAEGMGEER RGLLGSSFKR TSPFLTHQVF NSYHSETNLV
RYMKKLENKD ISLVHSMIPL GSCTMKLNSS SELAPITWRE FANIHPFVPL DQAQGYQQLF
QGLEKDLCEI TGYDRVSFQP NSGAQGEYAG LATIRAYLDQ KGERHRTVCL IPKSAHGTNP
ASAHMAGMKI QPVEVDRYGN IDVAHLKAMV DQHKENLAAI MITYPSTNGV FEENIGDVCA
LIHQHGGQVY LDGANMNAQV GICRPGDFGS DVSHLNLHKT FCIPHGGGGP GMGPIGVKKH
LSPFLPSHPV ISIKPTEGTW PVGTVSAAPW GSSSILPISW AYIKMMGGKG LKEATEIAIL
NANYMAKRLE KHYRVLFRGA RGYVAHEFIL DTRPFKKSAN VEAVDVAKRL QDYGFHAPTM
SWPVAGTLMI EPTESEDKAE LDRFCDAMIS IRQEIADIEE GRIDPRVNPL KMSPHSLTCV
TSSCWDRPYS REVAAFPLPF VKPENKFWPT IARIDDIYGD QHLVCTCPPM EVYESPFSEQ
KRASS
