GCSH_RAT
ID GCSH_RAT Reviewed; 170 AA.
AC Q5I0P2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000305};
DE AltName: Full=Lipoic acid-containing protein;
DE Flags: Precursor;
GN Name=Gcsh {ECO:0000312|RGD:619946};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The H protein (GCSH) shuttles the methylamine group of glycine
CC from the P protein (GLDC) to the T protein (GCST) (By similarity).
CC {ECO:0000250|UniProtKB:P11183}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000250|UniProtKB:P23434};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000250|UniProtKB:P23434};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P
CC (GLDC), T (GCST), L (DLD) and H (GCSH). Interacts with GLDC (By
CC similarity). {ECO:0000250|UniProtKB:P11183}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P20821}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
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DR EMBL; BC088114; AAH88114.1; -; mRNA.
DR RefSeq; NP_598282.2; NM_133598.2.
DR AlphaFoldDB; Q5I0P2; -.
DR SMR; Q5I0P2; -.
DR STRING; 10116.ENSRNOP00000015967; -.
DR iPTMnet; Q5I0P2; -.
DR PhosphoSitePlus; Q5I0P2; -.
DR jPOST; Q5I0P2; -.
DR PaxDb; Q5I0P2; -.
DR PRIDE; Q5I0P2; -.
DR Ensembl; ENSRNOT00000015967; ENSRNOP00000015967; ENSRNOG00000011535.
DR GeneID; 171133; -.
DR KEGG; rno:171133; -.
DR UCSC; RGD:619946; rat.
DR CTD; 2653; -.
DR RGD; 619946; Gcsh.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_1_1_1; -.
DR InParanoid; Q5I0P2; -.
DR OMA; EHEWLSG; -.
DR OrthoDB; 1348095at2759; -.
DR PhylomeDB; Q5I0P2; -.
DR TreeFam; TF300258; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-6783984; Glycine degradation.
DR SABIO-RK; Q5I0P2; -.
DR PRO; PR:Q5I0P2; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000011535; Expressed in kidney and 20 other tissues.
DR Genevisible; Q5I0P2; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IC:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004047; F:aminomethyltransferase activity; IMP:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:RGD.
DR GO; GO:0009249; P:protein lipoylation; ISS:UniProtKB.
DR CDD; cd06848; GCS_H; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 2: Evidence at transcript level;
KW Lipoyl; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 46..170
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /id="PRO_0000010726"
FT DOMAIN 63..145
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 104
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23434,
FT ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 170 AA; 18485 MW; 6E4CD58F28CD26A5 CRC64;
MSLRVVRSVR AVACSLRIAL ASCPPRPWAP SAAAVRSLRT GSALLSVRKF TEKHEWVTAK
DGIGTVGISN FAQEALGDVV YCSLPEVGTK LKKQEEFGAL ESVKAASELY SPLSGEVTEV
NEALAENPGL VNKSCYEDGW LIKMTLSDPS ELDELMSEEA YEKYVKSIEE