ID G1TSF9_RABIT Unreviewed; 180 AA.
AC G1TSF9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glycine cleavage system H protein {ECO:0000256|RuleBase:RU364055};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000019975.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000019975.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000019975.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000019975.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: The H protein shuttles the methylamine group of glycine from
CC the P protein to the T protein. {ECO:0000256|RuleBase:RU364055}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU364055};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU364055};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364055}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU364055}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC ECO:0000256|RuleBase:RU364055}.
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DR RefSeq; XP_002723390.1; XM_002723344.2.
DR AlphaFoldDB; G1TSF9; -.
DR SMR; G1TSF9; -.
DR STRING; 9986.ENSOCUP00000019975; -.
DR PaxDb; 9986-ENSOCUP00000019975; -.
DR Ensembl; ENSOCUT00000022239.2; ENSOCUP00000019975.2; ENSOCUG00000023714.2.
DR GeneID; 100351120; -.
DR KEGG; ocu:100351120; -.
DR eggNOG; KOG3373; Eukaryota.
DR GeneTree; ENSGT00390000011666; -.
DR HOGENOM; CLU_097408_1_1_1; -.
DR InParanoid; G1TSF9; -.
DR OrthoDB; 52189at2759; -.
DR TreeFam; TF300258; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR HAMAP; MF_00272; GcvH; 1.
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 NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF43; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Mitochondrion {ECO:0000256|RuleBase:RU364055};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|RuleBase:RU364055}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..180
FT /note="Glycine cleavage system H protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023808641"
FT DOMAIN 66..147
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 107
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 180 AA; 19893 MW; 34728115BC141FDB CRC64;
MALRVVWSVR AATCRLLTAS APAEPCSPLP WWLWAGTVPT LGTGPALISV RKLTEKHEWI
TTENGSGTVG ISNFAQEALG DVVYCSLPEV GTKLKKQDEF GALESVKAAS ELYSPLSEVT
EIKEALAENP GLIHKSCYED GWLIKMTLSN PSELDELMSE EAYEKYIKSI EKLKWNPYMN
//
