A0A7K5NHR3 · A0A7K5NHR3_CHRMC

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine
    This reaction proceeds in the forward direction.
  • 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H+ + sn-glycero-3-phospho-L-serine
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H+ + hexadecanoate + sn-glycerol 3-phosphocholine
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    EC:3.1.1.32 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H+ + sn-glycerol 3-phosphocholine
    EC:3.1.1.5 (UniProtKB | ENZYME | Rhea)
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    EC:3.1.1.3 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site139Nucleophile
Active site165Charge relay system
Binding site179Ca2+ (UniProtKB | ChEBI)
Binding site184Ca2+ (UniProtKB | ChEBI)
Active site250Charge relay system

GO annotations

AspectTerm
Cellular Componenthigh-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionheparin binding
Molecular Functionlysophospholipase activity
Molecular Functionmetal ion binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Molecular Functiontriglyceride lipase activity
Biological Processlipid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hepatic triacylglycerol lipase
  • EC number
  • Alternative names
    • Lipase member C
    • Lysophospholipase
    • Phospholipase A1

Gene names

    • Name
      Lipc
    • ORF names
      CHRMAC_R05293

Organism names

Accessions

  • Primary accession
    A0A7K5NHR3

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain323-458PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    469
  • Mass (Da)
    53,588
  • Last updated
    2021-04-07 v1
  • Checksum
    2877A3EF8573859D
EALGSQSQHTRTKKDQQNFETKFRLYTDTNEEGCQIFFNQLETLDKCHFNASLPLVMIVHGWSVDGMLEGWIWKMAAALKSQHKQINVIIADWLTFAHQHYPIAVQNTRYIGQEIADFLEWLEESVQFSRSNAHLIGYSLGAHVSGFAGSFISGTNKIGRITGLDPAGPLFEGMSPTDRLSPDDANFVDAIHTFTKQHMGLSVGIKQPVAHFDFYPNGGTFQPGCHIMHVYNHIAQYGITGITQTVKCAHERSVHLFIDSLLHNDKQSTAYGCNDINTFNKGMCLSCRKNRCNTLGYNIREERLPKSRQLFLKTRAHMPFKVYHYQFKIHFINEIQDKQIDPTFTISLTGTKEDAKNLPIPLVEGISGNKTYSFLLTLDTDIGELIMIKFKWEGTAVWENIWDTVQTIIPWTKGTRRPGLIVKTIRVKAGETQQKMTFCSQSIDNVHLHPAQEKTFVRCEDRFRRQNRK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue469

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VYZF01000646
EMBL· GenBank· DDBJ
NWT41814.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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