Ghitm
entrez
66092
canonical
uniprot
Q91VC9
canonical
ensembl
ENSMUSG00000041028
resolver
ensp
ENSMUSP00000046212
resolver
ensp
ENSMUSP00000129712
resolver
ensp
ENSMUSP00000311003
resolver
enst
ENSMUST00000042564
resolver
enst
ENSMUST00000165649
resolver
genesymbol
Ghitm
resolver
genesymbol_syn
Mics1
resolver
uniprot
Q3TGB7
resolver
uniprot
Q3UA74
resolver
uniprot
Q8N9T5
resolver
uniprot_entry
GHITM_MOUSE
resolver
uniprot_sec
Q3TGB7
resolver
uniprot_sec
Q3UA74
resolver
uniprot_sec
Q8N9T5
resolver
amino_acid_sequence
MLAARLVCLRTLPSRVFQPTFITKASPLVKNSITKNQWLVTPSREYATKTRIRTHRGKTGQELKEAALEPSMEKIFKIDQMGRWFVAGGAAVGLGALCYYGLGMSNEIGAIEKAVIWPQYVKDRIHSTYMYLAGSIGLTALSALAVARTPALMNFMMTGSWVTIGATFAAMIGAGMLVHSISYEQSPGPKHLAWMLHSGVMGAVVAPLTILGGPLLLRAAWYTAGIVGGLSTVAMCAPSEKFLNMGAPLGVGLGLVFASSLGSMFLPPTSVAGATLYSVAMYGGLVLFSMFLLYDTQKVIKRAEITPMYGAQKYDPINSMLTIYMDTLNIFMRVATMLATGSNRKK
uniprot
proteins
function
FUNCTION: Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport (PubMed:35715207). Mediates proton-dependent calcium efflux from mitochondrion (By similarity). Also functions as an electroneutral mitochondrial proton/potassium exchanger (PubMed:35715207). Required for the mitochondrial tubular network and cristae organization (PubMed:35715207). Involved in apoptotic release of cytochrome c (By similarity). Inhibits AFG3L2 proteolytic activity, stimulating respiration and stabilizing respiratory enzymes in actively respiring mitochondria (By similarity). However, when mitochondria become hyperpolarized, GHITM loses its inhibitory activity toward AFG3L2 and the now active AFG3L2 turns first on GHITM and, if hyperpolarization persists, on other proteins of the mitochondria, leading to a broad remodeling of the mitochondrial proteome (By similarity). {ECO:0000250|UniProtKB:Q9H3K2, ECO:0000269|PubMed:35715207}.
uniprot
proteins
mass_dalton
37275
uniprot
proteins
mutagenesis
MUTAGEN 326; /note="D->R: Impaired protein stability. Skeletal muscle mitochondria are swollen, exhibiting a disrupted cristae structure."; /evidence="ECO:0000269|PubMed:35715207
uniprot
proteins
post_translational_modification
PTM: Undergoes AFG3L2-mediated proteolytic degradation, upon hyperpolarization of mitochondria. {ECO:0000250|UniProtKB:Q9H3K2}.
uniprot
proteins
protein_family
BI1 family
uniprot
proteins
pubmed
11416014
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
35715207
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H3K2}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 84..104; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 127..147; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 161..181; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 192..212; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 215..235; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 246..266; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 273..293; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins