Q9P8P2 · PLB1_CRYNH
- ProteinPhospholipase B
- GenePLB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids637 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Exhibits phospholipase B (PLB), lysophospholipase (LPL) and lysophospholipase/transacylase (LPTA) activities.
Catalytic activity
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + a fatty acid + H+
Activity regulation
Inhibited by Fe3+ ion.
pH Dependence
Active only at acidic pHs.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | lysophospholipase activity | |
Molecular Function | phospholipase A2 activity | |
Biological Process | glycerophospholipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase B
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionQ9P8P2
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localizes to lipid rafts in the cell membrane prior to secretion.
Keywords
- Cellular component
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MSIATATFAFSLFATIAFA | ||||||
Chain | PRO_0000024636 | 20-637 | Phospholipase B | |||
Sequence: VPPETPRIELQAERGLGDKSYAPWQVDCPSNVTWIRNATTGLGSGERAYIEAREKLVQPVIEQMMAARGLETPPRTPNIGVALSGGGYRAMLTGLGGIMGMMNESTEASESETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLENLWNIDSNLVFPDDDKLSFYTELYTETNAKSDLGFPIQITDVWGLAIGSHVLPERYQLSNTPNLTFSSLPSVVSALGNASLPMPIIIAADRKRREAGELVIAENATVWEFTPYEFGSWAFGSQYKSPGAFTPIEYLGTSVDDGSPNGTCWKGFDQLSFVMGTSATLFNGAFLELNGTDSGLLTNLITAFLADLGEDQADISRIPNTFSNYNSGENPIYNLTYITLVDAGETNQNIPLEPLLVPTRDVDAIVAFDSSYDTDYIWPNGTALRTTYERAKVLAEHENTRVLMPEVPSMNGFVNGGYNSRPTFFGCNDTTTPLIIYVPSYPWSFAANTSTYQLSYENDEANEMLLNGMRSLTLNHSVPTWPTCFACALTDRSFMYTSENRSTTCQKCFDTWCWAGDDNTTEPATYEPVINSVPPWLVANNLSIGVADAPASNESTAGTASSGAAKADVSMGMVALAAGLGLML | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 56 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 231 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 314 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 343 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 387 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 433 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 481 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 553 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 572 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 594 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 606 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-572 | PLA2c | ||||
Sequence: DCPSNVTWIRNATTGLGSGERAYIEAREKLVQPVIEQMMAARGLETPPRTPNIGVALSGGGYRAMLTGLGGIMGMMNESTEASESETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLENLWNIDSNLVFPDDDKLSFYTELYTETNAKSDLGFPIQITDVWGLAIGSHVLPERYQLSNTPNLTFSSLPSVVSALGNASLPMPIIIAADRKRREAGELVIAENATVWEFTPYEFGSWAFGSQYKSPGAFTPIEYLGTSVDDGSPNGTCWKGFDQLSFVMGTSATLFNGAFLELNGTDSGLLTNLITAFLADLGEDQADISRIPNTFSNYNSGENPIYNLTYITLVDAGETNQNIPLEPLLVPTRDVDAIVAFDSSYDTDYIWPNGTALRTTYERAKVLAEHENTRVLMPEVPSMNGFVNGGYNSRPTFFGCNDTTTPLIIYVPSYPWSFAANTSTYQLSYENDEANEMLLNGMRSLTLNHSVPTWPTCFACALTDRSFMYTSENRSTTCQKCFDTWCWAGDDN |
Sequence similarities
Belongs to the lysophospholipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length637
- Mass (Da)68,818
- Last updated2013-02-06 v2
- Checksum7C052A69669B2276
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 6 | in Ref. 1; AAF65220 | ||||
Sequence: A → G | ||||||
Sequence conflict | 619 | in Ref. 1; AAF65220 | ||||
Sequence: K → N |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF223383 EMBL· GenBank· DDBJ | AAF65220.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP003831 EMBL· GenBank· DDBJ | AFR98312.2 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |