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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
 
 
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