DDHD1
entrez
80821
canonical
uniprot
Q8NEL9
canonical
ensembl
ENSG00000100523
resolver
ensp
ENSP00000350401
resolver
ensp
ENSP00000378970
resolver
ensp
ENSP00000500986
resolver
ensp
ENSP00000577231
resolver
ensp
ENSP00000577232
resolver
ensp
ENSP00000577233
resolver
ensp
ENSP00000577234
resolver
ensp
ENSP00000577235
resolver
ensp
ENSP00000577236
resolver
ensp
ENSP00000591262
resolver
genesymbol
DDHD1
resolver
genesymbol_syn
KIAA1705
resolver
hgnc
HGNC:19714
resolver
uniprot
G5E9D1
resolver
uniprot
Q8WVH3
resolver
uniprot
Q96LL2
resolver
uniprot
Q9C0F8
resolver
uniprot_entry
DDHD1_HUMAN
resolver
uniprot_sec
G5E9D1
resolver
uniprot_sec
Q8WVH3
resolver
uniprot_sec
Q96LL2
resolver
uniprot_sec
Q9C0F8
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) can positively regulate phospholipase A1 activity. {ECO:0000269|PubMed:20359546}.
uniprot
proteins
amino_acid_sequence
MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLRGEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPPQQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQSTTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLNCFRGQQMQENFDIEVSKSIDGKDAVHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLKEIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPSFLNPAKEPTSVSENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAYFRLQESFFNLPQLLFPENVMQNKDNALVELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDDDAKPNLDPI
uniprot
proteins
disease_involvement
DISEASE: Spastic paraplegia 28, autosomal recessive (SPG28) [MIM:609340]: 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. Some SPG28 patients also have distal sensory impairment. {ECO:0000269|PubMed:23176821}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.1.111
uniprot
proteins
ec_number
3.1.1.118
uniprot
proteins
ec_number
3.1.1.32
uniprot
proteins
function
FUNCTION: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (Probable) (PubMed:20359546, PubMed:22922100). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (Probable) (PubMed:20359546). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology (PubMed:24599962). These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (PubMed:24599962). May play a regulatory role in spermatogenesis or sperm function (PubMed:24599962). {ECO:0000250|UniProtKB:Q80YA3, ECO:0000269|PubMed:20359546, ECO:0000269|PubMed:22922100, ECO:0000269|PubMed:24599962, ECO:0000303|PubMed:24599962, ECO:0000305|PubMed:37189713}.
uniprot
proteins
mass_dalton
100435
uniprot
proteins
mutagenesis
MUTAGEN 590; /note="L->S: No effect on homooligomer formation; when associated with S-593."; /evidence="ECO:0000269|PubMed:22922100"; MUTAGEN 593; /note="I->S: No effect on homooligomer formation; when associated with S-590."; /evidence="ECO:0000269|PubMed:22922100"; MUTAGEN 662; /note="D->A: Markedly decreased enzymatic activity."; /evidence="ECO:0000269|PubMed:22922100"; MUTAGEN 848; /note="D->A: Markedly decreased enzymatic activity."; /evidence="ECO:0000269|PubMed:22922100"; MUTAGEN 867; /note="H->A: Markedly decreased enzymatic activity."; /evidence="ECO:0000269|PubMed:22922100"; MUTAGEN 875; /note="D->A: No effect on enzymatic activity."; /evidence="ECO:0000269|PubMed:22922100
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000305|PubMed:37189713}.
uniprot
proteins
protein_family
PA-PLA1 family
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15623529
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20359546
uniprot
proteins
pubmed
22922100
uniprot
proteins
pubmed
23176821
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24599962
uniprot
proteins
pubmed
37189713
uniprot
proteins
pubmed
9488669
uniprot
proteins
sequence_length
900
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15623529}.
uniprot
proteins