ALDH18A1
entrez
5832
canonical
uniprot
P54886
canonical
ensembl
ENSG00000059573
resolver
ensp
ENSP00000360265
resolver
ensp
ENSP00000360268
resolver
ensp
ENSP00000549438
resolver
ensp
ENSP00000549440
resolver
ensp
ENSP00000601992
resolver
ensp
ENSP00000601993
resolver
genesymbol
ALDH18A1
resolver
genesymbol_syn
GSAS
resolver
genesymbol_syn
P5CS
resolver
genesymbol_syn
PYCS
resolver
hgnc
HGNC:9722
resolver
uniprot
B2R5Q4
resolver
uniprot
B7Z350
resolver
uniprot
B7Z5X8
resolver
uniprot
B7ZLP1
resolver
uniprot
D3DR44
resolver
uniprot
O95952
resolver
uniprot
Q3KQU2
resolver
uniprot
Q5T566
resolver
uniprot
Q5T567
resolver
uniprot
Q9UM72
resolver
uniprot_entry
P5CS_HUMAN
resolver
uniprot_sec
B2R5Q4
resolver
uniprot_sec
B7Z350
resolver
uniprot_sec
B7Z5X8
resolver
uniprot_sec
B7ZLP1
resolver
uniprot_sec
D3DR44
resolver
uniprot_sec
O95952
resolver
uniprot_sec
Q3KQU2
resolver
uniprot_sec
Q5T566
resolver
uniprot_sec
Q5T567
resolver
uniprot_sec
Q9UM72
resolver
activity_regulation
ACTIVITY REGULATION: Isoform Short: Inhibited by L-ornithine with a Ki of approximately 0.25 mm. Isoform Long: Insensitive to ornithine inhibition. This is due to the two amino acid insert which abolishes feedback inhibition of P5CS activity by L-ornithine. {ECO:0000269|PubMed:10037775}.
uniprot
proteins
amino_acid_sequence
MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKSFAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAVAFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQYSICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNVISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTKSRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAGPTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAAPLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIFESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTREEVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRLVRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSEVKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVFWNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSLKYLHENLPIPQRNTN
uniprot
proteins
disease_involvement
DISEASE: Cutis laxa, autosomal recessive, 3A (ARCL3A) [MIM:219150]: A syndrome characterized by facial dysmorphism with a progeroid appearance, large and late-closing fontanel, cutis laxa, joint hyperlaxity, athetoid movements and hyperreflexia, pre- and postnatal growth retardation, intellectual deficit, developmental delay, and ophthalmologic abnormalities. {ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:18478038, ECO:0000269|PubMed:22170564, ECO:0000269|PubMed:24767728}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal dominant, 3 (ADCL3) [MIM:616603]: A form of cutis laxa, a connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema. ADCL3 patients manifest thin skin with visible veins and wrinkles, cataract or corneal clouding, moderate intellectual disability, muscular hypotonia with brisk muscle reflexes, clenched fingers, and pre- and postnatal growth retardation. {ECO:0000269|PubMed:26320891}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 9A, autosomal dominant (SPG9A) [MIM:601162]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG9A patients have gait difficulties, motor neuropathy, and dysarthria. Additional variable features include cerebellar signs, cataract, pes cavus, and urinary urgency. {ECO:0000269|PubMed:26026163, ECO:0000269|PubMed:26297558}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 9B, autosomal recessive (SPG9B) [MIM:616586]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG9B is a complex form characterized by delayed psychomotor development, intellectual disability, and severe motor impairment. Dysmorphic facial features, tremor, and urinary incontinence are variably observed in SPG9B patients. {ECO:0000269|PubMed:26026163}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.2.1.41
uniprot
proteins
ec_number
2.7.2.11
uniprot
proteins
function
FUNCTION: Bifunctional enzyme that converts glutamate to glutamate 5-semialdehyde, an intermediate in the biosynthesis of proline, ornithine and arginine. {ECO:0000269|PubMed:10037775, ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:26297558, ECO:0000269|PubMed:26320891, ECO:0000269|PubMed:39506109}.
uniprot
proteins
mass_dalton
87302
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="K->A: No effect on punctate pattern in the mitochondria; when associated with A-247 and A-311."; /evidence="ECO:0000269|PubMed:32770108"; MUTAGEN 247; /note="D->A: No effect on punctate pattern in the mitochondria; when associated with A-76 and A-311."; /evidence="ECO:0000269|PubMed:32770108"; MUTAGEN 311; /note="K->A: No effect on punctate pattern in the mitochondria; when associated with A-247 and A-247."; /evidence="ECO:0000269|PubMed:32770108"; MUTAGEN 612; /note="C->A: Catalytically inactive; no effect on filament formation; no effect on punctate pattern in the mitochondria."; /evidence="ECO:0000269|PubMed:32770108, ECO:0000269|PubMed:39506109
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000269|PubMed:26297558}.; PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. {ECO:0000269|PubMed:26297558}.
uniprot
proteins
protein_family
Glutamate 5-kinase family; Gamma-glutamyl phosphate reductase family
uniprot
proteins
pubmed
10037775
uniprot
proteins
pubmed
11092761
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18478038
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22170564
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24767728
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26026163
uniprot
proteins
pubmed
26297558
uniprot
proteins
pubmed
26320891
uniprot
proteins
pubmed
32770108
uniprot
proteins
pubmed
39506109
uniprot
proteins
pubmed
8761662
uniprot
proteins
sequence_length
795
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26297558, ECO:0000269|PubMed:26320891}. Mitochondrion matrix {ECO:0000269|PubMed:32770108}. Note=Exhibits puncta-like structures inside mitochondria under nutrient stress (PubMed:32770108). When cellular dependence on oxidative phosphorylation increases, forms filaments, which may increase its activity, and is sequestered in a subset of atypical mitochondria that lack cristae and ATP synthase (PubMed:39506109). {ECO:0000269|PubMed:32770108, ECO:0000269|PubMed:39506109}.
uniprot
proteins