Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A672FIH3 · A0A672FIH3_SALFA

Function

function

Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles. Also exhibits lysophospholipase activity. Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates. In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = 2,3-di-(9Z)-octadecenoyl-sn-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-octadecenoylglycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + butanoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • 1,3-di-(9Z-octadecenoyl)-glycerol + H2O = 3-(9Z-octadecenoyl)-sn-glycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = sn-glycero-3-phospho-L-serine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + hexadecanoate + H+
    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 = sn-glycerol 3-phosphocholine + a fatty acid + H+
    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.

Type
IDPosition(s)Description
Active site142Nucleophile
Active site168Charge relay system
Binding site182Ca2+ (UniProtKB | ChEBI)
Binding site187Ca2+ (UniProtKB | ChEBI)
Active site253Charge relay system

GO annotations

AspectTerm
Cellular Componenthigh-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionapolipoprotein binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionlysophospholipase activity
Molecular Functionmetal ion binding
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Biological Processfatty acid biosynthetic process
Biological Processtriglyceride catabolic 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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Blenniimorphae > Blenniiformes > Blennioidei > Blenniidae > Salariinae > Salarias

Accessions

  • Primary accession
    A0A672FIH3

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain326-458PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    472
  • Mass (Da)
    53,912
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    8E4BA862D6027099C06122809112668A
QRKWNHLLLWKVIYNMVKEPYVSSSDFSLFLGDDDTCTLDPLQLHTLTSCGFNSSNPLIIITHGWSVDGIMENWVNMLAQVLKTHLGDINVIITDWMSLACQHYPKAAQSTRTIGKDIAHLLQVLQQEYQYPLRKAHLIGYSLGAHISGFAGSYLEGPEKIGRITGLDPAGPFFEGMSPTDRLSPDDAEFVDAIHTFTRERMGLSVGIKQDVAHYDFYPNGGHFQPGCELTHILKQIAHHGVLDLQQTVKCAHERAVRLFMDSILNKDKQSKGYRCSNSEAFDKGLCLDCRKNRCNTLGYYIKKVRTGTPKRLFLKTGGQMPYKLYHYQFRIQFINQMADIEPSLTIFLTGTKDESGELTFTPESIAGNTSFSFLVALERDLGELMMLRMRWERSDMLKTTWSDMLNIILWGVQEEKPWLSVGRISVKSGETQERTFFCAMANDGQHIEKSQDKDFVRCQEQTPKLHRRKHN

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A672FIW5A0A672FIW5_SALFAlipc522
A0A672FDH0A0A672FDH0_SALFAlipc464
A0A672FE65A0A672FE65_SALFAlipc417
A0A672FE85A0A672FE85_SALFAlipc487
A0A672FBL2A0A672FBL2_SALFAlipc497
A0A672FBW9A0A672FBW9_SALFAlipc490

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help