Pnpla8
entrez
67452
canonical
uniprot
Q8K1N1
canonical
ensembl
ENSMUSG00000036257
resolver
ensp
ENSMUSP00000043286
resolver
ensp
ENSMUSP00000201723
resolver
enst
ENSMUST00000043082
resolver
genesymbol
Pnpla8
resolver
genesymbol_syn
Ipla22
resolver
genesymbol_syn
Ipla2g
resolver
uniprot
Q3TH33
resolver
uniprot
Q8VEC0
resolver
uniprot
Q9DC20
resolver
uniprot_entry
PLPL8_MOUSE
resolver
uniprot_sec
Q3TH33
resolver
uniprot_sec
Q8VEC0
resolver
uniprot_sec
Q9DC20
resolver
activity_regulation
ACTIVITY REGULATION: Calcium-independent phospholipase. {ECO:0000250|UniProtKB:Q9NP80}.
uniprot
proteins
amino_acid_sequence
MSINLTLDIYIYFLNNARSLCGKQRSKQLHFVCSKQYWRMNHVNVHREFHTSKKSCKWNRSEAHCSKHWHSPSNHGLHFGIVRLSTSAPKGLTKVSIHMSRIKSTLNSVSKAIFGSQNEMVTRLAQFKPSSRILRKVSDKGWLKQKNVKQAVESLKNYSDKSAGKNSLAEQKSYFADKEEDSGKHSLFHYTYGITTRFGESFSVLANHINSYFKSKGKMSQTKEDKQLQDKPDLEERKSSSPGPDTVADRPDSESPLEVKDKLSSPTQMPEAHPVSAKQSIANFLSRPTEGVQALVGGYIGGLVPKLKSDPKSPPEEQEVSAKTEQAVNKDKKAEEKKRVLLQQEKIIARVSIDNRTRALVQALRRTADPKLCITRVEELTFHLLEFPEGKGVAIKEKIIPYLLRLRQVKDETLQAAVREILALIGYVDPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTQNVIVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGQTPKAFVFRNYGHFPGTNSHYLGGCQYKMWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTSTYTSLKTKLSNVISSATDTEEVHIMLDGLLPSDTYFRFNPVICENIPLDESRDEKLDQLQLEGMKYIERNDQKMKKVAKILSQEKTTLQKINDWIKLKSDMYEGLPFFSKL
uniprot
proteins
ec_number
3.1.1.-
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
FUNCTION: Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors (PubMed:17923475, PubMed:28442572). Hydrolyzes phosphatidylethanolamine, phosphatidylcholine and probably phosphatidylinositol with a possible preference for the former. Also has a broad substrate specificity in terms of fatty acid moieties, hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal rates from either the sn-1 or sn-2 position in diacyl phosphatidylcholine. However, has a weak activity toward polyunsaturated fatty acids at the sn-2 position, and thereby favors the production of 2-arachidonoyl lysophosphatidylcholine, a key branch point metabolite in eicosanoid signaling. On the other hand, can produce arachidonic acid from the sn-1 position of diacyl phospholipid and from the sn-2 position of arachidonate-containing plasmalogen substrates. Therefore, plays an important role in the mobilization of arachidonic acid in response to cellular stimuli and the generation of lipid second messengers. Can also hydrolyze lysophosphatidylcholine (By similarity). In the mitochondrial compartment, catalyzes the hydrolysis and release of oxidized aliphatic chains from cardiolipin and integrates mitochondrial bioenergetics and signaling. It is essential for maintaining efficient bioenergetic mitochondrial function through tailoring mitochondrial membrane lipid metabolism and composition (PubMed:17923475, PubMed:28442572). {ECO:0000250|UniProtKB:Q9NP80, ECO:0000269|PubMed:17923475, ECO:0000269|PubMed:28442572}.
uniprot
proteins
mass_dalton
87381
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism. {ECO:0000269|PubMed:17923475, ECO:0000269|PubMed:28442572}.
uniprot
proteins
pubmed
10833412
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17213206
uniprot
proteins
pubmed
17923475
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28442572
uniprot
proteins
sequence_length
776
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5XTS1}. Mitochondrion membrane {ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:17923475}; Single-pass membrane protein {ECO:0000305}. Peroxisome membrane {ECO:0000269|PubMed:17213206}; Single-pass membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 469..489; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins