O54728 · PLB1_RAT
- ProteinPhospholipase B1, membrane-associated
- GenePlb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1450 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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)
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)
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H+This reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H+ + 2 hexadecanoate + sn-glycerol 3-phosphocholineThis reaction proceeds in the forward direction.
- 1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholineThis reaction proceeds in the forward direction.
- 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H+ + octadecanoateThis reaction proceeds in the forward direction.
- 1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H+This reaction proceeds in the forward direction.
- 1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H+ + hexadecanoateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H+This reaction proceeds in the forward direction.
- 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H+This reaction proceeds in the forward direction.
- 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H+This reaction proceeds in the forward direction.
- 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H+This reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H+This reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H+This reaction proceeds in the forward direction.
Activity regulation
Up-regulated by bile acids such as deoxycholate (PubMed:9442064, PubMed:9442065).
Inhibited by diisopropyl fluorophosphate (PubMed:9442064, PubMed:9442065).
Inhibited by diisopropyl fluorophosphate (PubMed:9442064, PubMed:9442065).
pH Dependence
Optimum pH is 8-9.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 404 | |||||
Sequence: S | ||||||
Active site | 518 | |||||
Sequence: D | ||||||
Active site | 659 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | brush border membrane | |
Molecular Function | calcium-independent phospholipase A2 activity | |
Molecular Function | lysophospholipase activity | |
Molecular Function | phospholipase A2 activity | |
Molecular Function | retinyl-palmitate esterase activity | |
Molecular Function | triglyceride lipase activity | |
Biological Process | diacylglycerol catabolic process | |
Biological Process | phosphatidylcholine catabolic process | |
Biological Process | phosphatidylethanolamine catabolic process | |
Biological Process | phosphatidylglycerol catabolic process | |
Biological Process | phospholipid metabolic process | |
Biological Process | positive regulation of acrosome reaction | |
Biological Process | retinol metabolic process | |
Biological Process | triglyceride catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePhospholipase B1, membrane-associated
- Short namesPhospholipase B
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO54728
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Single-pass type I membrane protein
Note: Present in the intestinal brush border membranes.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 28-1422 | Extracellular | ||||
Sequence: SSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLY | ||||||
Transmembrane | 1423-1443 | Helical | ||||
Sequence: WAVPVAAVGGLVVGILGMMLW | ||||||
Topological domain | 1444-1450 | Cytoplasmic | ||||
Sequence: RTVRLVQ |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 404 | Loss of PLA2, lysophospholipase and lipase activities. | ||||
Sequence: S → A or C | ||||||
Mutagenesis | 414 | No effect on lysophospholipase to PLA2 activity ratio. | ||||
Sequence: S → A | ||||||
Mutagenesis | 429 | No effect on activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 459 | Decrease in PLA2, lysophospholipase and lipase activities. | ||||
Sequence: S → A | ||||||
Mutagenesis | 518 | Loss of PLA2, lysophospholipase and lipase activities. | ||||
Sequence: D → A or V | ||||||
Mutagenesis | 518 | Impairs PLA2, lysophospholipase and lipase activities. | ||||
Sequence: D → E or N | ||||||
Mutagenesis | 659 | Loss of PLA2, lysophospholipase and lipase activities. | ||||
Sequence: H → A | ||||||
Mutagenesis | 665 | Impairs PLA2, lysophospholipase and lipase activities. | ||||
Sequence: H → A | ||||||
Mutagenesis | 686 | No effect on activity. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MESWPGVSLVGLLLLLLLGQGPSQIHG | ||||||
Chain | PRO_0000324386 | 28-1450 | Phospholipase B1, membrane-associated | |||
Sequence: SSGENTSQPQQVFRTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNSQILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ | ||||||
Glycosylation | 32 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 45 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 179 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 699 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 787 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 801 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 844 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 880 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 926 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1059 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1280 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1383 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1387 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Undergoes proteolytic cleavage in the ileum.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the ileum mucosa, Paneth cells spermatocytes, spermatids and sperm (at protein level). Expressed in the ileum, jejunum, esophagus and testis.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 41-351 | 1 | ||||
Sequence: RTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNS | ||||||
Region | 41-1407 | 4 X 308-326 AA approximate repeats | ||||
Sequence: RTLKNFSFPCKPKKLELSVLSKSVHSLRPSDIKLVAAIGNLETPPAPGSGVVNMEKPQSLESELQNVCIGIMTALSDIIRHFNPSVLMPTCSPGKGTAGHTTIAEDLWIQAKELVRHLKDNPELDFEKDWKLITVLFSNTSQCHLCSSDQQKRHLMKHMEMLSGVLDYLHREVPRAFVNLVDLSEVLTMAQQHQETGFSPAPEICKCSEEITKLSKAVMQWSYQEAWEDLLASSKFNKHETFAVVFQSFFSEVELPLERPSPQDSTTLALRIWNSMMEPVGRKDGTLNEAERKTMKCPSQESPYLFTYRNSNYQARQLKPIGKFQMKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNSNLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNSNYTYPIKPAIENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNS | ||||||
Repeat | 366-711 | 2 | ||||
Sequence: MKEGTKFTCPDKDPSDSIPTTVHRLRPADIKVIGAMGDSLTAGNGAGSSPGNVLDVLTQYRGLSWSVGGDETIETVTTLANILREFNPSLKGFSVGTGKENTPRASFNQAVAGAKSDGLAAQAKKLVSLMKDDKTINFQEDWKIITVFIGGNDLCGSCNNLARFSPQTFTDNIKTALDILHAEVPRAFVNMVSVIEITPLRELFNEPKVSCPRMILRSLCPCVLNLGENSAELAQLVERNRQYQEETGKLIESGRYDTRDDFTVVLQPMFENVVMPRTLEGLPDSSFFAPDCFHFNVKTHARSAIALWKNMLEPVGRKTRHQNFEIKVPIMCPNQTSPFLSTTKNS | ||||||
Region | 708-734 | Disordered | ||||
Sequence: TKNSNLGHGTSMSCEEKAPSASPPTSV | ||||||
Repeat | 712-1058 | 3 | ||||
Sequence: NLGHGTSMSCEEKAPSASPPTSVHTLRPADIQVVAALGDSVTAGNGISSQEGDLADVTTQYRGLSYSAGGDKFLENVTTLPNILREFNGNLTGYSVGTGDVNSASAFLNQAVPGAKAENLASQVQTLIQKMKNDTRVNFHQDWKVITVMIGASDLCDFCKDSNRYSAANFSDHLRNALDILHKEVPRALVNLVDFMNPSIIRQVFLKNPDKCPVNQTSVLCNCVLTPGEDSHELARLEAFTKSYQSSMLQLVESGRYDTREDFSVVLQPFLFNIRLPILENGNPDTSFFAPDCILLSQKFHTQLARALWANMLEPLGKKMDTLDPKELIALACPTKDKPFLRTFRNS | ||||||
Repeat | 1068-1407 | 4 | ||||
Sequence: IENWGSDFLCTEQSPSSKVPTSVHELRPSDIKVVAAMGDFLTTATGARPSESSSLDTPWRGLSWSIGGDGTLETHTTLPNILKKFNPSILGFSTGTLENTAGLNVAEEGARAQDMPAQAQALVKKMKSTPTINIQEDWKLITLLIGNNDLCLYCEDPENYSTREYVKYIQHALDIFYEELPRVFINVVEVMELSGLLHDQGGKCAMPLAVQKNCSCLKRSQNLMAMQELKKVNGNLQSALSELSYWHRYMQREDFAVTVQPFFRNTFVPLDERGGLDLTFFSEDCFHFSVRGHAEMAIALWNNMLEPVGKKTTSNNFTYNRTKLKCPSPENPFLYTVRNS | ||||||
Region | 1408-1450 | Necessary for membrane localization | ||||
Sequence: QILLDKAKENSNTLYWAVPVAAVGGLVVGILGMMLWRTVRLVQ |
Domain
Repeat 2 contains the catalytic domain.
Sequence similarities
Belongs to the 'GDSL' lipolytic enzyme family. Phospholipase B1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,450
- Mass (Da)161,089
- Last updated1998-06-01 v1
- Checksum4555898C8FD91F45
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6GKG0 | A0A8I6GKG0_RAT | Plb1 | 1396 | ||
F1M7W5 | F1M7W5_RAT | Plb1 | 1111 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D63648 EMBL· GenBank· DDBJ | BAA23813.1 EMBL· GenBank· DDBJ | mRNA |