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Q06HQ7 (PLB1_MONDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase B1, membrane-associated

Short name=Phospholipase B
Alternative name(s):
Phospholipase B/lipase
Short name=PLB/LIP

Including the following 2 domains:

  1. Phospholipase A2
    EC=3.1.1.4
  2. Lysophospholipase
    EC=3.1.1.5
Gene names
Name:PLB1
Synonyms:PLB
OrganismMonodelphis domestica (Gray short-tailed opossum) [Reference proteome]
Taxonomic identifier13616 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDidelphimorphiaDidelphidaeMonodelphis

Protein attributes

Sequence length1474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Membrane-associated phospholipase. Exhibits a calcium-independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids By similarity.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by diisopropyl fluorophosphate By similarity.

Subcellular location

Apical cell membrane; Single-pass type I membrane protein By similarity. Note: Present in the intestinal brush border membranes By similarity.

Domain

Repeat 2 contains the catalytic domain By similarity.

Post-translational modification

Undergoes proteolytic cleavage in the ileum By similarity.

Sequence similarities

Belongs to the 'GDSL' lipolytic enzyme family. Phospholipase B1 subfamily.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipase A2 activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 14741452Phospholipase B1, membrane-associated
PRO_0000324384

Regions

Topological domain23 – 14321410Extracellular Potential
Transmembrane1433 – 145321Helical; Potential
Topological domain1454 – 147421Cytoplasmic Potential
Repeat36 – 3503151
Repeat365 – 7103462
Repeat711 – 10693593
Repeat1079 – 14173394
Region36 – 141713824 X 308-326 AA approximate repeats
Region1418 – 146144Necessary for membrane localization By similarity

Sites

Active site4031Nucleophile By similarity
Active site13611 By similarity
Active site13641 By similarity
Binding site4771Substrate; via amide nitrogen By similarity
Binding site5161Substrate By similarity

Amino acid modifications

Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation7111N-linked (GlcNAc...) Potential
Glycosylation8131N-linked (GlcNAc...) Potential
Glycosylation10701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q06HQ7 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: B22844CD69B35A60

FASTA1,474165,157
        10         20         30         40         50         60 
MRLQPSLLLL ALLLLKVTTI QATLGNNSWE EQTWPEGLKN FPFPCRPEEI PFSPPSESVH 

        70         80         90        100        110        120 
SLRISDIRVV GAIGNLETTP DAKMVLKRQK WIERNQMQTC MQVMTVLSDF IKKFSPSVLP 

       130        140        150        160        170        180 
LLCPSREKVL PRMRNEDLGP QARELVQHMK KNQKLNFRND WKLINVFFNA QSQCHPCSSS 

       190        200        210        220        230        240 
QKEGNMTSSM QELIRLLDYL QKEVPKAFVN LVDISELGNS IQSNNQENGP RDINEVCECP 

       250        260        270        280        290        300 
QEPSRLTTAV QRWYYQNSWE KLLTSGRYDT KDTFTVIYQS FLHEMEPSVF PIKQTSGSSL 

       310        320        330        340        350        360 
KKLSTALAVS LWNGMIDPTG KKEEFFTTGQ RIPVKCPTQK HPYLFTYRNN NKLSSTPEIK 

       370        380        390        400        410        420 
RISETREGTE IRCPDMDPSN AVPTSVHHLR PADIKVIGAL GDSLTAGNGA GSTPGNILDV 

       430        440        450        460        470        480 
LTQYRGLSWS IGGNENISTV TTLANILREF NPSLIGFSTG TGNQNSAAAF LNQAVAGATS 

       490        500        510        520        530        540 
ETLPSQARRL VDLMKENKRI NFQDDWKIVT LFIGGNDLCD SCSDPPRYSS QNFTAHIGKA 

       550        560        570        580        590        600 
LDILHAEVPR VFVNLVTVLS IVSLRELYQE ESINCPRVIL RSLCPCVLKF KDNSTELTTL 

       610        620        630        640        650        660 
IELNKQYQEE THRLVDSGRY DTRDDFTVVL QPFLEQVPMP KTPEGLPDSS FFAPDCFHFH 

       670        680        690        700        710        720 
SKAHARVARS LWNNMLEPVG EKKKEENLEN IVDLICPSES QPYLRTYKNS NYTYPTATPT 

       730        740        750        760        770        780 
SSPKPDYGSQ LWCEDRAPSA SFPTSVHALK PADIQVVAAV GDSLTAGNGI GSKPDDLPDV 

       790        800        810        820        830        840 
ITQYRGLSYS AGGDASLESV TTLPNILREF NMNLTGFAVG VGSADDANAF LNQAVPGAKA 

       850        860        870        880        890        900 
EGLKKQVQTL VQKMKSDPRI NFQRDWKVIT LLIGTTDLCD YCTDSNLYSA TNFSAYLRDA 

       910        920        930        940        950        960 
LDFLHREVPR ALVNLVDFMN PIIFRQVFLG NQDKCPMTQA CSLCNCLLTV REDSPELARM 

       970        980        990       1000       1010       1020 
KEVVKVYQTK IRELVESGRY DTREDFTIVL QPFLEEVKLA FQDGIPDVSF FAPDCIHPNQ 

      1030       1040       1050       1060       1070       1080 
KFHSQLSRAL WNNMLQPLGK KMDFLDLTAD TTLSCPSLEE PFLRTYRNSN YTYPANPAIE 

      1090       1100       1110       1120       1130       1140 
NWGSDFLCPE QGSSNSAPSS VHQLRPADIK VVAALGDSLT TAVGAGAKNN SNWSTAWRGL 

      1150       1160       1170       1180       1190       1200 
SWSIGGDGTL ETHTTLPNIL KKFNPHLHGF STGTQEEAAG LNVAVEGAIA QDMPSQARIL 

      1210       1220       1230       1240       1250       1260 
VDRMKNSSEI NLDQDWKLIT IFVGSNDLCQ YCENPEAHSV KNYVQSLQQA LDIFYKELPR 

      1270       1280       1290       1300       1310       1320 
AFINVVEIME LVGLRQIQGE KCAVTTQSIC PCFGRSLDNS PELQEMKNIN RHFQSGSSLI 

      1330       1340       1350       1360       1370       1380 
TYHHQYMERE DFAVVVQPFF QSTVVPLDDK GKPDLSFFSV DCFHFSERGH AEMAIALWNN 

      1390       1400       1410       1420       1430       1440 
MLEPVGQKQT YNNFTHSRTK VKCPTSENPY FFTMRNSGLL RKEASHKTPS VPFWAVLVAA 

      1450       1460       1470 
AASFIVGVVL VMLWRTKKCS RREERPISLV ATVF 

« Hide

References

[1]"Dietary cholesterol increases intestinal phospholipase B gene expression in laboratory opossums."
Chan J., Kushwaha R.S., Gluhak-Heinrich J., Donalson L.M., VandeBerg J.F., VandeBerg J.L.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ875604 mRNA. Translation: ABI74623.1.
RefSeqNP_001070653.1. NM_001077185.1.
UniGeneMdm.186.

3D structure databases

ProteinModelPortalQ06HQ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING13616.ENSMODP00000019434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID768082.
KEGGmdo:768082.

Organism-specific databases

CTD5350.

Phylogenomic databases

eggNOGNOG311176.
HOGENOMHOG000115574.
HOVERGENHBG108263.
InParanoidQ06HQ7.
KOK14621.

Family and domain databases

Gene3D3.40.50.1110. 6 hits.
InterProIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamPF00657. Lipase_GDSL. 3 hits.
[Graphical view]
PROSITEPS01098. LIPASE_GDSL_SER. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLB1_MONDO
AccessionPrimary (citable) accession number: Q06HQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 31, 2006
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families