GCSH_MOUSE
ID GCSH_MOUSE Reviewed; 170 AA.
AC Q91WK5; Q9CY75; Q9D197;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 144.
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|MGI:MGI:1915383};
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=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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 [6]
RP STRUCTURE BY NMR OF 41-170.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the GCV_H domain from mouse glycine.";
RL Submitted (AUG-2007) to the PDB data bank.
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; AK003788; BAB22996.2; -; mRNA.
DR EMBL; AK019983; BAB31951.1; -; mRNA.
DR EMBL; AK050373; BAC34217.1; -; mRNA.
DR EMBL; AC162858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11574.1; -; Genomic_DNA.
DR EMBL; BC014745; AAH14745.1; -; mRNA.
DR CCDS; CCDS22696.1; -.
DR RefSeq; NP_080848.1; NM_026572.3.
DR PDB; 2EDG; NMR; -; A=48-170.
DR PDBsum; 2EDG; -.
DR AlphaFoldDB; Q91WK5; -.
DR SMR; Q91WK5; -.
DR STRING; 10090.ENSMUSP00000037131; -.
DR iPTMnet; Q91WK5; -.
DR PhosphoSitePlus; Q91WK5; -.
DR EPD; Q91WK5; -.
DR jPOST; Q91WK5; -.
DR PaxDb; Q91WK5; -.
DR PeptideAtlas; Q91WK5; -.
DR PRIDE; Q91WK5; -.
DR ProteomicsDB; 267781; -.
DR DNASU; 68133; -.
DR Ensembl; ENSMUST00000040484; ENSMUSP00000037131; ENSMUSG00000034424.
DR GeneID; 68133; -.
DR KEGG; mmu:68133; -.
DR UCSC; uc009not.1; mouse.
DR CTD; 2653; -.
DR MGI; MGI:1915383; Gcsh.
DR VEuPathDB; HostDB:ENSMUSG00000034424; -.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_1_1_1; -.
DR InParanoid; Q91WK5; -.
DR OMA; YRDSHEW; -.
DR OrthoDB; 1348095at2759; -.
DR PhylomeDB; Q91WK5; -.
DR TreeFam; TF300258; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-6783984; Glycine degradation.
DR BioGRID-ORCS; 68133; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Gcsh; mouse.
DR EvolutionaryTrace; Q91WK5; -.
DR PRO; PR:Q91WK5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91WK5; protein.
DR Bgee; ENSMUSG00000034424; Expressed in morula and 107 other tissues.
DR Genevisible; Q91WK5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004047; F:aminomethyltransferase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000010724"
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"
FT CONFLICT 21
FT /note="T -> A (in Ref. 4; AAH14745)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> L (in Ref. 4; AAH14745)"
FT /evidence="ECO:0000305"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2EDG"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2EDG"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2EDG"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2EDG"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2EDG"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2EDG"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:2EDG"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2EDG"
SQ SEQUENCE 170 AA; 18637 MW; C0464972C79C00EA CRC64;
MSLQVSRSLR VVAYSLRTAL TFCSPRPCVP SAAAVRSLRT GSALLSVRKF TEKHEWITTE
EGIGTVGISN FAQEALGDVV YCSLPEVGTK LKKQEEFGAL ESVKAASELY SPLSGEVTEV
NEALAENPGL VNKSCYEDGW LIKMTLSDPS EMDELMSEEA YEKYVKSIEE
