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O54728 (PLB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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:Phlpb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.1 Ref.2 Ref.4

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by diisopropyl fluorophosphate.

Subcellular location

Apical cell membrane; Single-pass type I membrane protein. Note: Present in the intestinal brush border membranes. Ref.1 Ref.2

Tissue specificity

Expressed in the ileum mucosa, Paneth cells spermatocytes, spermatids and sperm (at protein level). Expressed in the ileum, jejunum, esophagus and testis. Ref.1 Ref.3

Domain

Repeat 2 contains the catalytic domain.

Post-translational modification

Undergoes proteolytic cleavage in the ileum.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 14501427Phospholipase B1, membrane-associated
PRO_0000324386

Regions

Topological domain24 – 14221399Extracellular Potential
Transmembrane1423 – 144321Helical; Potential
Topological domain1444 – 14507Cytoplasmic Potential
Repeat41 – 3513111
Repeat366 – 7113462
Repeat712 – 10583473
Repeat1068 – 14073404
Region41 – 140713674 X 308-326 AA approximate repeats
Region1408 – 145043Necessary for membrane localization
Coiled coil590 – 61728 Potential

Sites

Active site4041Nucleophile By similarity
Active site13511 By similarity
Active site13541 By similarity
Binding site4781Substrate; via amide nitrogen By similarity
Binding site5171Substrate By similarity

Amino acid modifications

Glycosylation8011N-linked (GlcNAc...) Potential
Glycosylation10591N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis4041S → A or C: Loss of activity. Ref.4
Mutagenesis4141S → A: Decrease in activity. Ref.4
Mutagenesis4291S → A: Decrease in activity. Ref.4
Mutagenesis4591S → A: Decrease in activity. Ref.4
Mutagenesis5181D → A or V: Loss of activity. Ref.4
Mutagenesis5181D → E or N: Decrease in activity. Ref.4
Mutagenesis6591H → A: Loss of activity. Ref.4
Mutagenesis6651H → A: Slight effect on activity. Ref.4
Mutagenesis6861H → A: No effect on activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O54728 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 4555898C8FD91F45

FASTA1,450161,089
        10         20         30         40         50         60 
MESWPGVSLV GLLLLLLLGQ GPSQIHGSSG ENTSQPQQVF RTLKNFSFPC KPKKLELSVL 

        70         80         90        100        110        120 
SKSVHSLRPS DIKLVAAIGN LETPPAPGSG VVNMEKPQSL ESELQNVCIG IMTALSDIIR 

       130        140        150        160        170        180 
HFNPSVLMPT CSPGKGTAGH TTIAEDLWIQ AKELVRHLKD NPELDFEKDW KLITVLFSNT 

       190        200        210        220        230        240 
SQCHLCSSDQ QKRHLMKHME MLSGVLDYLH REVPRAFVNL VDLSEVLTMA QQHQETGFSP 

       250        260        270        280        290        300 
APEICKCSEE ITKLSKAVMQ WSYQEAWEDL LASSKFNKHE TFAVVFQSFF SEVELPLERP 

       310        320        330        340        350        360 
SPQDSTTLAL RIWNSMMEPV GRKDGTLNEA ERKTMKCPSQ ESPYLFTYRN SNYQARQLKP 

       370        380        390        400        410        420 
IGKFQMKEGT KFTCPDKDPS DSIPTTVHRL RPADIKVIGA MGDSLTAGNG AGSSPGNVLD 

       430        440        450        460        470        480 
VLTQYRGLSW SVGGDETIET VTTLANILRE FNPSLKGFSV GTGKENTPRA SFNQAVAGAK 

       490        500        510        520        530        540 
SDGLAAQAKK LVSLMKDDKT INFQEDWKII TVFIGGNDLC GSCNNLARFS PQTFTDNIKT 

       550        560        570        580        590        600 
ALDILHAEVP RAFVNMVSVI EITPLRELFN EPKVSCPRMI LRSLCPCVLN LGENSAELAQ 

       610        620        630        640        650        660 
LVERNRQYQE ETGKLIESGR YDTRDDFTVV LQPMFENVVM PRTLEGLPDS SFFAPDCFHF 

       670        680        690        700        710        720 
NVKTHARSAI ALWKNMLEPV GRKTRHQNFE IKVPIMCPNQ TSPFLSTTKN SNLGHGTSMS 

       730        740        750        760        770        780 
CEEKAPSASP PTSVHTLRPA DIQVVAALGD SVTAGNGISS QEGDLADVTT QYRGLSYSAG 

       790        800        810        820        830        840 
GDKFLENVTT LPNILREFNG NLTGYSVGTG DVNSASAFLN QAVPGAKAEN LASQVQTLIQ 

       850        860        870        880        890        900 
KMKNDTRVNF HQDWKVITVM IGASDLCDFC KDSNRYSAAN FSDHLRNALD ILHKEVPRAL 

       910        920        930        940        950        960 
VNLVDFMNPS IIRQVFLKNP DKCPVNQTSV LCNCVLTPGE DSHELARLEA FTKSYQSSML 

       970        980        990       1000       1010       1020 
QLVESGRYDT REDFSVVLQP FLFNIRLPIL ENGNPDTSFF APDCILLSQK FHTQLARALW 

      1030       1040       1050       1060       1070       1080 
ANMLEPLGKK MDTLDPKELI ALACPTKDKP FLRTFRNSNY TYPIKPAIEN WGSDFLCTEQ 

      1090       1100       1110       1120       1130       1140 
SPSSKVPTSV HELRPSDIKV VAAMGDFLTT ATGARPSESS SLDTPWRGLS WSIGGDGTLE 

      1150       1160       1170       1180       1190       1200 
THTTLPNILK KFNPSILGFS TGTLENTAGL NVAEEGARAQ DMPAQAQALV KKMKSTPTIN 

      1210       1220       1230       1240       1250       1260 
IQEDWKLITL LIGNNDLCLY CEDPENYSTR EYVKYIQHAL DIFYEELPRV FINVVEVMEL 

      1270       1280       1290       1300       1310       1320 
SGLLHDQGGK CAMPLAVQKN CSCLKRSQNL MAMQELKKVN GNLQSALSEL SYWHRYMQRE 

      1330       1340       1350       1360       1370       1380 
DFAVTVQPFF RNTFVPLDER GGLDLTFFSE DCFHFSVRGH AEMAIALWNN MLEPVGKKTT 

      1390       1400       1410       1420       1430       1440 
SNNFTYNRTK LKCPSPENPF LYTVRNSQIL LDKAKENSNT LYWAVPVAAV GGLVVGILGM 

      1450 
MLWRTVRLVQ 

« Hide

References

[1]"Identification of functional domains of rat intestinal phospholipase B/lipase. Its cDNA cloning, expression, and tissue distribution."
Takemori H., Zolotaryov F.N., Ting L., Urbain T., Komatsubara T., Hatano O., Okamoto M., Tojo H.
J. Biol. Chem. 273:2222-2231(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Ileal mucosa.
[2]"Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes."
Tojo H., Ichida T., Okamoto M.
J. Biol. Chem. 273:2214-2221(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 368-380 AND 529-559, FUNCTION, SUBCELLULAR LOCATION.
[3]"Further characterization of a novel phospholipase B (phospholipase A2-lysophospholipase) from intestinal brush-border membranes."
Pind S., Kuksis A.
Biochem. Cell Biol. 69:346-357(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Identification of essential residues for catalysis of rat intestinal phospholipase B/lipase."
Lu T., Ito M., Tchoua U., Takemori H., Okamoto M., Tojo H.
Biochemistry 40:7133-7139(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-404; SER-414; SER-429; SER-459; ASP-518; HIS-659; HIS-665 AND HIS-686.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63648 mRNA. Translation: BAA23813.1.
RefSeqNP_620253.1. NM_138898.1.
UniGeneRn.91079.

3D structure databases

ProteinModelPortalO54728.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000057888.

PTM databases

PhosphoSiteO54728.

Proteomic databases

PaxDbO54728.
PRIDEO54728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID192259.
KEGGrno:192259.

Organism-specific databases

CTD151056.
RGD621565. Plb1.

Phylogenomic databases

eggNOGNOG311176.
HOGENOMHOG000115574.
HOVERGENHBG108263.
InParanoidO54728.
KOK14621.
PhylomeDBO54728.

Gene expression databases

GenevestigatorO54728.

Family and domain databases

Gene3D3.40.50.1110. 5 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...

Other

NextBio622930.
PROO54728.

Entry information

Entry namePLB1_RAT
AccessionPrimary (citable) accession number: O54728
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 78 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