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Details on Person UniProt:P09848 LCT
| Class:Id | ReferenceGeneProduct:58683 |
|---|---|
| _chainChangeLog | signal peptide:1-19 added on Fri February 6 2015;propeptide:20-866 added on Fri February 6 2015;chain:867-1927 added on Fri February 6 2015;propeptide:20-866 removed on Fri May 6 2016;chain:867-1927 removed on Fri May 6 2016;propeptide:20-868 added on Fri May 6 2016;chain:869-1927 added on Fri May 6 2016 |
| _displayName | UniProt:P09848 LCT |
| _timestamp | 2026-02-20 22:23:26 |
| chain | signal peptide:1-19 propeptide:20-868 chain:869-1927 |
| checksum | 2FCD55CB47BBA35A |
| comment | FUNCTION Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose (PubMed:12594539, PubMed:16400612, PubMed:3929764, PubMed:9762914). The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other (PubMed:12594539, PubMed:3929764, PubMed:9762914).CATALYTIC ACTIVITY lactose + H2O = beta-D-galactose + D-glucoseCATALYTIC ACTIVITY phlorizin + H2O = phloretin + beta-D-glucoseCATALYTIC ACTIVITY D-cellobiose + H2O = beta-D-glucose + D-glucoseCATALYTIC ACTIVITY quercetin 4'-O-beta-D-glucoside + H2O = quercetin + beta-D-glucoseCATALYTIC ACTIVITY quercetin 3-O-beta-D-glucoside + H2O = quercetin + beta-D-glucoseCATALYTIC ACTIVITY kaempferol 3-O-beta-D-glucoside + H2O = kaempferol + beta-D-glucoseCATALYTIC ACTIVITY luteolin 7-O-beta-D-glucoside + H2O = luteolin + beta-D-glucoseCATALYTIC ACTIVITY luteolin 4'-O-beta-D-glucoside + H2O = luteolin + beta-D-glucoseCATALYTIC ACTIVITY (2S)-naringenin 7-O-beta-D-glucoside + H2O = (2S)-naringenin + beta-D-glucoseCATALYTIC ACTIVITY eriodictyol-7-O-beta-D-glucoside + H2O = (S)-eriodictyol + beta-D-glucoseCATALYTIC ACTIVITY apigenin 7-O-beta-D-glucoside + H2O = apigenin + beta-D-glucoseCATALYTIC ACTIVITY daidzein 7-O-beta-D-glucoside + H2O = daidzein + beta-D-glucose + H(+)CATALYTIC ACTIVITY genistein 7-O-beta-D-glucoside + H2O = genistein + beta-D-glucoseCATALYTIC ACTIVITY a beta-D-galactosyl-N-acylsphingosine + H2O = a ceramide + beta-D-galactose.CATALYTIC ACTIVITY beta-D-glucosyl-(1<->1')-N-hexadecanoylsphing-4-enine + H2O = N-hexadecanoylsphing-4-enine + beta-D-glucoseCATALYTIC ACTIVITY beta-D-galactosyl-(1<->1')-N-hexadecanoylsphing-4-enine + H2O = beta-D-galactose + N-hexadecanoylsphing-4-enineCATALYTIC ACTIVITY beta-D-galactosyl-(1<->1')-N-hexadecanoylsphinganine + H2O = beta-D-galactose + N-hexadecanoylsphinganineCATALYTIC ACTIVITY beta-D-glucosyl-(1<->1')-N-hexadecanoylsphinganine + H2O = N-hexadecanoylsphinganine + beta-D-glucoseSUBUNIT Homodimer.SUBCELLULAR LOCATION Brush border.TISSUE SPECIFICITY Specifically expressed in small intestine.DOMAIN The glycosyl hydrolase-1 3/region III carries the phlorizin hydrolase/glycosylceramidase activities.DOMAIN The glycosyl hydrolase-1 4/region IV carries the lactase activity.PTM N-glycosylated.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyl hydrolase 1 family.ONLINE INFORMATION Lactase entryONLINE INFORMATION Darwin's dessert - Issue 111 of November 2009 |
| description | recommendedName: fullName evidence="17"Lactase/phlorizin hydrolase alternativeName: fullName evidence="20"Lactase/glycosylceramidase domain recommendedName: fullName evidence="20"Lactase ecNumber evidence="7 8 11 13"3.2.1.108 /domain domain recommendedName: fullName evidence="2"Glycosylceramidase ecNumber evidence="2"3.2.1.62 alternativeName: fullName evidence="20"Phlorizin hydrolase /domain |
| geneName | LCT LPH |
| identifier | P09848 |
| isSequenceChanged | FALSE |
| keyword | Cell membrane Disease variant Glycoprotein Glycosidase Hydrolase Membrane Multifunctional enzyme Proteomics identification Reference proteome Signal Transmembrane Transmembrane helix Zymogen |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | LCT |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8997797] ENSEMBL:ENSG00000115850 LCT [Homo sapiens] |
| secondaryIdentifier | LPH_HUMAN Q4ZG58 |
| sequenceLength | 1927 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:189091] LCT [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:5657984] LCT G1363S [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:5657993] LCT R1587H [plasma membrane] [Homo sapiens] |
| (referenceSequence) | [ReplacedResidue:5657995] glycine 1363 replaced with L-serine [ReplacedResidue:5657998] L-arginine 1587 replaced with L-histidine |
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No pathways have been reviewed or authored by UniProt:P09848 LCT (58683)
