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O70320 (PLB1_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length1463 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 By similarity. Ref.2

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. Ref.1

Tissue specificity

Expressed in the epididymis, jejunum and ileon (at protein level). Ref.1 Ref.2 Ref.3

Domain

Repeat 2 contains the catalytic domain By similarity.

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 – 2020 Potential
Chain21 – 14631443Phospholipase B1, membrane-associated
PRO_0000324382

Regions

Topological domain21 – 14191399Extracellular Potential
Transmembrane1420 – 144021Helical; Potential
Topological domain1441 – 146323Cytoplasmic Potential
Repeat38 – 3463091
Repeat361 – 7063462
Repeat707 – 10533473
Repeat1063 – 14033414
Region38 – 140313664 X 308-326 AA approximate repeats
Region1404 – 145047Necessary for membrane localization By similarity

Sites

Active site3991Nucleophile By similarity
Active site13471 By similarity
Active site13501 By similarity
Binding site4731Substrate; via amide nitrogen By similarity
Binding site5121Substrate By similarity

Amino acid modifications

Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation7961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O70320 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 101C4969815F24B1

FASTA1,463162,176
        10         20         30         40         50         60 
MGLQPGVLLV GLLLLGQGIT QIHTSSGKST LEGQLWPETK KNFPFSCSPK KLGLNMPSES 

        70         80         90        100        110        120 
VHTLTPADIK LIAAIGDMET PPDSGAVNLD TSERTEKEPW RGCMGMMTVL SDIISHFNPS 

       130        140        150        160        170        180 
VLLPTCPPWR SAAVRGGVEE LRTQAEELVS SLKKNPQLDF QQDWKLINVF FSNASLCYLC 

       190        200        210        220        230        240 
PSAHENGPLM SNMDKLAGIL HYLHQEVPRA FVNLVDLFEV VAMPRWHQGT MLSRPSPEAC 

       250        260        270        280        290        300 
GCSGETSKLD TVVMQWSYQE TWDSLLASSS FNDQESFAVV FQPFFYEVSS PVEEPPSQDP 

       310        320        330        340        350        360 
TTLALSLWNN MMKPVGQKDE PFSTIERRPM KCPSQESPYL FTYRNSNYQS RLLKRQRQHK 

       370        380        390        400        410        420 
EREGTEIRCP DKDPSDSTPT SVHRLKPADI KVIGALGDSL TAGNGAGSRP GNILDVLTEY 

       430        440        450        460        470        480 
RGLSWSIGAD HNISSVTTLP NILREFNPSL KGFSTGTGKA NSVGAFFNQA VAGARAGDLI 

       490        500        510        520        530        540 
PQARTLVDLM KNHTSINFEE DWKIITVFIG GNDLCDFCSD PVTNSPENFT DNIRQALDIL 

       550        560        570        580        590        600 
HAEVPRAFVN MVKVLQIVNL RELYKDSRVS CPRLILRNLC RCVLLPDDNS TELESLIDIN 

       610        620        630        640        650        660 
KKYQERTHQL IESGRYDTRE DFTVVLQPFF EKVDIPKTSE GLPDNTSFAP DCFHFSSKTH 

       670        680        690        700        710        720 
ARAASALWKN MLEPVGQKTT QNNFENSIDI ICPNQAFPYL STYKNGIEGH GTWLTCRERT 

       730        740        750        760        770        780 
PSASPPTSVH ALRPADVRVV AALGDSLTAG SGIGSKPGDL ADVITQYRGL SYSSGGDGSL 

       790        800        810        820        830        840 
MNVTTLPNIL REFNSNLTGY AVGTGDASNT NAFLNQAVPG AKAEELMSQV KTLVQKMKDD 

       850        860        870        880        890        900 
PRINFHEDWK VITVLIGTND LCNHCTDLDL YSSANFFNHL LNALDILHRE VPRALVNLVD 

       910        920        930        940        950        960 
FMNPSIMRQV FLGNPDKCPV QQASILCNCV LSLRENSYEL ARMDALTRAY QSSMRELVES 

       970        980        990       1000       1010       1020 
GRYDTREDFS VVLQPFFLNI RLPILEDGRP DTSFFAPDCI NPGQKFHSQL SRALWVNMLE 

      1030       1040       1050       1060       1070       1080 
PVGSKTDTLD LTADISLPCP TQEEPFLRTP QNSDYTYPTK PAIENWGSDF LCTEWKPSNS 

      1090       1100       1110       1120       1130       1140 
VPTSVHKLQP ADIKVVAALG DSLTTAVGAR ASNSSDLLMS WRGLSWSIGG DGALETHTTL 

      1150       1160       1170       1180       1190       1200 
PNILKKFNPS IFGFSTGTLE ETAGFNVAVE EARARDMPAQ ARDLVERMKA STEINLEMDW 

      1210       1220       1230       1240       1250       1260 
KLITLFIGSN DLCHYCDNPE NHSAEEYVQH IRQALDILYE ELPRAFINVV DIIMELAGLH 

      1270       1280       1290       1300       1310       1320 
QGQGGHCTAL LPAQSTCSCL RHFPSSPVIQ ELKKVTWNLQ SDMSRLSYQE KYTQREDFAV 

      1330       1340       1350       1360       1370       1380 
VVQPFFQNTL IPLDKLGSTD PTFFSEDCLH FSERGHAEMA IALWNNMLEP VGHKTTFNNF 

      1390       1400       1410       1420       1430       1440 
TYNRTKLKCP STESPYLYTL QNSLSLPVQT EKASGVAPGI VSAAAAGGLL VGLIVGILAV 

      1450       1460 
SLWSSFRRRQ KKSPPESVPV ANF 

« Hide

References

[1]"Ectopic epididymal expression of guinea pig intestinal phospholipase B. Possible role in sperm maturation and activation by limited proteolytic digestion."
Delagebeaudeuf C., Gassama-Diagne A., Nauze M., Ragab A., Li R.Y., Capdevielle J., Ferrara P., Fauvel J., Chap H.
J. Biol. Chem. 273:13407-13414(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 396-402; 463-470 AND 895-904, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Strain: Crl:(BFA)BR.
Tissue: Intestine.
[2]"Purification of a new, calcium-independent, high molecular weight phospholipase A2/lysophospholipase (phospholipase B) from guinea pig intestinal brush-border membrane."
Gassama-Diagne A., Fauvel J., Chap H.
J. Biol. Chem. 264:9470-9475(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF045454 mRNA. Translation: AAC40129.1.
RefSeqNP_001166499.1. NM_001173028.1.

3D structure databases

ProteinModelPortalO70320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000009712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135633.

Organism-specific databases

CTD100135633.

Phylogenomic databases

eggNOGNOG311176.
HOGENOMHOG000115574.
HOVERGENHBG108263.
InParanoidO70320.

Family and domain databases

Gene3D3.40.50.1110. 4 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_CAVPO
AccessionPrimary (citable) accession number: O70320
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 69 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