SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O54728

- PLB1_RAT

UniProt

O54728 - PLB1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Phospholipase B1, membrane-associated
Gene
Plb1, Phlpb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.
Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.

Enzyme regulationi

Inhibited by diisopropyl fluorophosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei404 – 4041Nucleophile By similarity
Binding sitei478 – 4781Substrate; via amide nitrogen By similarity
Binding sitei517 – 5171Substrate By similarity
Active sitei1351 – 13511 By similarity
Active sitei1354 – 13541 By similarity

GO - Molecular functioni

  1. lysophospholipase activity Source: RGD
  2. phospholipase A2 activity Source: RGD
  3. retinyl-palmitate esterase activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. phospholipid metabolic process Source: RGD
  3. retinol metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase B1, membrane-associated
Short name:
Phospholipase B
Alternative name(s):
Phospholipase B/lipase
Short name:
PLB/LIP
Including the following 2 domains:
Phospholipase A2 (EC:3.1.1.4)
Lysophospholipase (EC:3.1.1.5)
Gene namesi
Name:Plb1
Synonyms:Phlpb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621565. Plb1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 14221399Extracellular Reviewed prediction
Add
BLAST
Transmembranei1423 – 144321Helical; Reviewed prediction
Add
BLAST
Topological domaini1444 – 14507Cytoplasmic Reviewed prediction

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. brush border membrane Source: RGD
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi404 – 4041S → A or C: Loss of activity. 1 Publication
Mutagenesisi414 – 4141S → A: Decrease in activity. 1 Publication
Mutagenesisi429 – 4291S → A: Decrease in activity. 1 Publication
Mutagenesisi459 – 4591S → A: Decrease in activity. 1 Publication
Mutagenesisi518 – 5181D → A or V: Loss of activity. 1 Publication
Mutagenesisi518 – 5181D → E or N: Decrease in activity. 1 Publication
Mutagenesisi659 – 6591H → A: Loss of activity. 1 Publication
Mutagenesisi665 – 6651H → A: Slight effect on activity. 1 Publication
Mutagenesisi686 – 6861H → A: No effect on activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 14501427Phospholipase B1, membrane-associated
PRO_0000324386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi801 – 8011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1059 – 10591N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Undergoes proteolytic cleavage in the ileum.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO54728.
PRIDEiO54728.

PTM databases

PhosphoSiteiO54728.

Expressioni

Tissue specificityi

Expressed in the ileum mucosa, Paneth cells spermatocytes, spermatids and sperm (at protein level). Expressed in the ileum, jejunum, esophagus and testis.2 Publications

Gene expression databases

GenevestigatoriO54728.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000057888.

Structurei

3D structure databases

ProteinModelPortaliO54728.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati41 – 3513111
Add
BLAST
Repeati366 – 7113462
Add
BLAST
Repeati712 – 10583473
Add
BLAST
Repeati1068 – 14073404
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 140713674 X 308-326 AA approximate repeats
Add
BLAST
Regioni1408 – 145043Necessary for membrane localization
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili590 – 61728 Reviewed prediction
Add
BLAST

Domaini

Repeat 2 contains the catalytic domain.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311176.
HOGENOMiHOG000115574.
HOVERGENiHBG108263.
InParanoidiO54728.
KOiK14621.
PhylomeDBiO54728.

Family and domain databases

Gene3Di3.40.50.1110. 5 hits.
InterProiIPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 3 hits.
[Graphical view]
PROSITEiPS01098. LIPASE_GDSL_SER. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54728-1 [UniParc]FASTAAdd to Basket

« Hide

MESWPGVSLV GLLLLLLLGQ GPSQIHGSSG ENTSQPQQVF RTLKNFSFPC     50
KPKKLELSVL SKSVHSLRPS DIKLVAAIGN LETPPAPGSG VVNMEKPQSL 100
ESELQNVCIG IMTALSDIIR HFNPSVLMPT CSPGKGTAGH TTIAEDLWIQ 150
AKELVRHLKD NPELDFEKDW KLITVLFSNT SQCHLCSSDQ QKRHLMKHME 200
MLSGVLDYLH REVPRAFVNL VDLSEVLTMA QQHQETGFSP APEICKCSEE 250
ITKLSKAVMQ WSYQEAWEDL LASSKFNKHE TFAVVFQSFF SEVELPLERP 300
SPQDSTTLAL RIWNSMMEPV GRKDGTLNEA ERKTMKCPSQ ESPYLFTYRN 350
SNYQARQLKP IGKFQMKEGT KFTCPDKDPS DSIPTTVHRL RPADIKVIGA 400
MGDSLTAGNG AGSSPGNVLD VLTQYRGLSW SVGGDETIET VTTLANILRE 450
FNPSLKGFSV GTGKENTPRA SFNQAVAGAK SDGLAAQAKK LVSLMKDDKT 500
INFQEDWKII TVFIGGNDLC GSCNNLARFS PQTFTDNIKT ALDILHAEVP 550
RAFVNMVSVI EITPLRELFN EPKVSCPRMI LRSLCPCVLN LGENSAELAQ 600
LVERNRQYQE ETGKLIESGR YDTRDDFTVV LQPMFENVVM PRTLEGLPDS 650
SFFAPDCFHF NVKTHARSAI ALWKNMLEPV GRKTRHQNFE IKVPIMCPNQ 700
TSPFLSTTKN SNLGHGTSMS CEEKAPSASP PTSVHTLRPA DIQVVAALGD 750
SVTAGNGISS QEGDLADVTT QYRGLSYSAG GDKFLENVTT LPNILREFNG 800
NLTGYSVGTG DVNSASAFLN QAVPGAKAEN LASQVQTLIQ KMKNDTRVNF 850
HQDWKVITVM IGASDLCDFC KDSNRYSAAN FSDHLRNALD ILHKEVPRAL 900
VNLVDFMNPS IIRQVFLKNP DKCPVNQTSV LCNCVLTPGE DSHELARLEA 950
FTKSYQSSML QLVESGRYDT REDFSVVLQP FLFNIRLPIL ENGNPDTSFF 1000
APDCILLSQK FHTQLARALW ANMLEPLGKK MDTLDPKELI ALACPTKDKP 1050
FLRTFRNSNY TYPIKPAIEN WGSDFLCTEQ SPSSKVPTSV HELRPSDIKV 1100
VAAMGDFLTT ATGARPSESS SLDTPWRGLS WSIGGDGTLE THTTLPNILK 1150
KFNPSILGFS TGTLENTAGL NVAEEGARAQ DMPAQAQALV KKMKSTPTIN 1200
IQEDWKLITL LIGNNDLCLY CEDPENYSTR EYVKYIQHAL DIFYEELPRV 1250
FINVVEVMEL SGLLHDQGGK CAMPLAVQKN CSCLKRSQNL MAMQELKKVN 1300
GNLQSALSEL SYWHRYMQRE DFAVTVQPFF RNTFVPLDER GGLDLTFFSE 1350
DCFHFSVRGH AEMAIALWNN MLEPVGKKTT SNNFTYNRTK LKCPSPENPF 1400
LYTVRNSQIL LDKAKENSNT LYWAVPVAAV GGLVVGILGM MLWRTVRLVQ 1450
Length:1,450
Mass (Da):161,089
Last modified:June 1, 1998 - v1
Checksum:i4555898C8FD91F45
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63648 mRNA. Translation: BAA23813.1.
RefSeqiNP_620253.1. NM_138898.1.
UniGeneiRn.91079.

Genome annotation databases

GeneIDi192259.
KEGGirno:192259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63648 mRNA. Translation: BAA23813.1 .
RefSeqi NP_620253.1. NM_138898.1.
UniGenei Rn.91079.

3D structure databases

ProteinModelPortali O54728.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000057888.

PTM databases

PhosphoSitei O54728.

Proteomic databases

PaxDbi O54728.
PRIDEi O54728.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 192259.
KEGGi rno:192259.

Organism-specific databases

CTDi 151056.
RGDi 621565. Plb1.

Phylogenomic databases

eggNOGi NOG311176.
HOGENOMi HOG000115574.
HOVERGENi HBG108263.
InParanoidi O54728.
KOi K14621.
PhylomeDBi O54728.

Miscellaneous databases

NextBioi 622930.
PROi O54728.

Gene expression databases

Genevestigatori O54728.

Family and domain databases

Gene3Di 3.40.50.1110. 5 hits.
InterProi IPR001087. Lipase_GDSL.
IPR008265. Lipase_GDSL_AS.
IPR013831. SGNH_hydro-type_esterase_dom.
[Graphical view ]
Pfami PF00657. Lipase_GDSL. 3 hits.
[Graphical view ]
PROSITEi PS01098. LIPASE_GDSL_SER. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPLB1_RAT
AccessioniPrimary (citable) accession number: O54728
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi