| Identification |
|---|
| HMDB Protein ID
| CDBP01676 |
| Secondary Accession Numbers
| Not Available |
| Name
| Lecithin retinol acyltransferase |
| Description
| Not Available |
| Synonyms
|
- Phosphatidylcholine--retinol O-acyltransferase
|
| Gene Name
| LRAT |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in phosphatidylcholine-retinol O-acyltransfera |
| Specific Function
| Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments.
|
| GO Classification
|
| Biological Process |
| small molecule metabolic process |
| embryo development |
| retinol metabolic process |
| retinoid metabolic process |
| steroid metabolic process |
| visual perception |
| vitamin A metabolic process |
| response to stimulus |
| Cellular Component |
| endoplasmic reticulum membrane |
| perinuclear region of cytoplasm |
| multivesicular body |
| integral to membrane |
| rough endoplasmic reticulum |
| Molecular Function |
| transferase activity, transferring acyl groups |
| retinol binding |
| phosphatidylcholine-retinol O-acyltransferase activity |
| retinoic acid binding |
|
| Cellular Location
|
- Cytoplasm
- perinuclear region
- Endoplasmic reticulum membrane
- Single-pass membrane protein
- Endosome
- Rough endoplasmic reticulum
- multivesicular body
|
| Pathways
|
| Name | SMPDB/Pathwhiz | KEGG | | Vitamin digestion and absorption | Not Available |  | | Retinol Metabolism |    |  | | Vitamin A Deficiency |    | Not Available |
|
| Gene Properties |
|---|
| Chromosome Location
| 4 |
| Locus
| 4q32.1 |
| SNPs
| LRAT |
| Gene Sequence
|
>693 bp
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCAAGGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGCACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
|
| Protein Properties |
|---|
| Number of Residues
| 230 |
| Molecular Weight
| 25702.635 |
| Theoretical pI
| 7.46 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Lecithin retinol acyltransferase
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
|
| External Links |
|---|
| GenBank ID Protein
| 4240391 |
| UniProtKB/Swiss-Prot ID
| O95237 |
| UniProtKB/Swiss-Prot Entry Name
| LRAT_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AF071510 |
| GeneCard ID
| LRAT |
| GenAtlas ID
| LRAT |
| HGNC ID
| HGNC:6685 |
| References |
|---|
| General References
| Not Available |