Plb1
entrez
192259
canonical
uniprot
O54728
canonical
ensembl
ENSRNOG00000026037
resolver
ensembl
ENSRNOG00055020289
resolver
ensembl
ENSRNOG00060012921
resolver
ensp
ENSRNOP00000057888
resolver
ensp
ENSRNOP00055028181
resolver
ensp
ENSRNOP00060017467
resolver
enst
ENSRNOT00000061176
resolver
enst
ENSRNOT00055034761
resolver
enst
ENSRNOT00060022051
resolver
genesymbol
Plb1
resolver
genesymbol_syn
Phlpb
resolver
uniprot_entry
PLB1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Up-regulated by bile acids such as deoxycholate (PubMed:9442064, PubMed:9442065). Inhibited by diisopropyl fluorophosphate (PubMed:9442064, PubMed:9442065). {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}.
uniprot
proteins
amino_acid_sequence
MESWPGVSLVGLLLLLLLGQGPSQIHGSSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ
uniprot
proteins
ec_number
3.1.1.3
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids (PubMed:11401559, PubMed:9442064, PubMed:9442065). Preferentially cleaves sn-2 ester bonds over sn-1 bonds (PubMed:9442064). Acts as a lipase toward glycerolipid substrates (PubMed:11401559, PubMed:9442064, PubMed:9442065). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (PubMed:11401559, PubMed:9442064, PubMed:9442065). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable). {ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065, ECO:0000305|PubMed:9442064}.
uniprot
proteins
mass_dalton
161089
uniprot
proteins
mutagenesis
MUTAGEN 404; /note="S->A,C: Loss of PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 414; /note="S->A: No effect on lysophospholipase to PLA2 activity ratio."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 429; /note="S->A: No effect on activity."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 459; /note="S->A: Decrease in PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 518; /note="D->A,V: Loss of PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 518; /note="D->E,N: Impairs PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 659; /note="H->A: Loss of PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 665; /note="H->A: Impairs PLA2, lysophospholipase and lipase activities."; /evidence="ECO:0000269|PubMed:11401559"; MUTAGEN 686; /note="H->A: No effect on activity."; /evidence="ECO:0000269|PubMed:11401559
uniprot
proteins
post_translational_modification
PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000269|PubMed:9442065}.
uniprot
proteins
protein_family
'GDSL' lipolytic enzyme family
uniprot
proteins
protein_family
Phospholipase B1 subfamily
uniprot
proteins
pubmed
11401559
uniprot
proteins
pubmed
1716922
uniprot
proteins
pubmed
9442064
uniprot
proteins
pubmed
9442065
uniprot
proteins
sequence_length
1450
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes.
uniprot
proteins
transmembrane_region
TRANSMEM 1423..1443; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins