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O46559

- LIPC_RABIT

UniProt

O46559 - LIPC_RABIT

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Protein

Hepatic triacylglycerol lipase

Gene
LIPC
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin By similarity.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681Nucleophile By similarity
Active sitei194 – 1941Charge relay system By similarity
Active sitei279 – 2791Charge relay system By similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. triglyceride lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatic triacylglycerol lipase (EC:3.1.1.3)
Short name:
HL
Short name:
Hepatic lipase
Alternative name(s):
Lipase member C
Gene namesi
Name:LIPC
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. high-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

HDL, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 By similarityAdd
BLAST
Chaini23 – 499477Hepatic triacylglycerol lipasePRO_0000233341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi397 – 3971N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001411.

Structurei

3D structure databases

ProteinModelPortaliO46559.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini352 – 486135PLATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni181 – 19313Heparin-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Contains 1 PLAT domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG81747.
HOGENOMiHOG000038553.
HOVERGENiHBG002259.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR002333. Lipase_hep.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PTHR11610:SF2. PTHR11610:SF2. 1 hit.
PfamiPF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSiPR00824. HEPLIPASE.
PR00821. TAGLIPASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O46559-1 [UniParc]FASTAAdd to Basket

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MGSPLCVPIF LAVCILIQSS THGQSLRPEP FGRRARVTAT KKTLLETETR    50
FLLFKDKANK GCQIRLHHAD TLQECGFNSS LPLVMIVHGW SVDGLLESWI 100
WQMVAALKSQ PARPVNVGLV DWISLAHSHY AVAVRNARLV GQEVAALLQW 150
LEESAPFSRS NVHLIGYSLG AHVAGFAGSY ISGKHKIGRI TGLDAAGPLF 200
EGTSASDRLS PDDATFVDAI HTFTREHMGL SVGIKQPVGH YDFYPNGGSF 250
QPGCHFLELY KHIAQHGLNA LSQTIKCAHE RSVHLFIDSL LHPSMQSTAY 300
QCSDMDSFSQ GLCLGCTKGR CNTLGYHIRQ EPLSKGKRLF LVTQAQSPFR 350
VYHYQFKIQF INQIEKPLEP TFTMSLLGTK EEMQKIPITL GEGITSNKTY 400
SFLITLNLDI GELMVIKFKW ENSAVWANVW NTVQTIIPWG IKPRNSGLIL 450
KTIRVKAGET QQRMTFCSEN MDDLQLHPTQ EKNFVRCEVN PKKLKLKIK 499
Length:499
Mass (Da):55,814
Last modified:June 1, 1998 - v1
Checksum:i4DA7D65EE815A0A5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041202 mRNA. Translation: AAB96786.1.
RefSeqiNP_001075501.1. NM_001082032.1.
UniGeneiOcu.2193.

Genome annotation databases

GeneIDi100008678.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041202 mRNA. Translation: AAB96786.1 .
RefSeqi NP_001075501.1. NM_001082032.1.
UniGenei Ocu.2193.

3D structure databases

ProteinModelPortali O46559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000001411.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008678.

Organism-specific databases

CTDi 3990.

Phylogenomic databases

eggNOGi NOG81747.
HOGENOMi HOG000038553.
HOVERGENi HBG002259.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000734. Lipase.
IPR002333. Lipase_hep.
IPR008976. Lipase_LipOase.
IPR013818. Lipase_N.
IPR016272. Lipoprotein_lipase_LIPH.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11610. PTHR11610. 1 hit.
PTHR11610:SF2. PTHR11610:SF2. 1 hit.
Pfami PF00151. Lipase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSi PR00824. HEPLIPASE.
PR00821. TAGLIPASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49723. SSF49723. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Rabbit hepatic lipase cDNA sequence: low activity is associated with low messenger RNA levels."
    Warren R.J., Ebert D.L., Mitchell A., Barter P.J.
    J. Lipid Res. 32:1333-1339(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Warren R.J., Ebert D.L., Mitchell A., Barter P.J.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiLIPC_RABIT
AccessioniPrimary (citable) accession number: O46559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 80 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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