Search Results

Overview

Uniprot IDP00325
Protein NameAll-trans-retinol dehydrogenase [NAD(+)] ADH1B
Gene NameADH1B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 LFTPQCGKCRVCKNP
105 CGKCRVCKNPESNYC
11 AGKVIKCKAAVLWEV
114 PESNYCLKNDLGNPR
136 RRFTCRGKPIHHFLG
169 DAASPLEKVCLIGCG
20 AVLWEVKKPFSIEDV
213 LSAVMGCKAAGAARI
227 IIAVDINKDKFAKAK
229 AVDINKDKFAKAKEL
234 KDKFAKAKELGATEC
248 CINPQDYKKPIQEVL
249 INPQDYKKPIQEVLK
316 LLTGRTWKGAVYGGF
324 GAVYGGFKSKEGIPK
326 VYGGFKSKEGIPKLV
33 DVEVAPPKAYEVRIK
331 KSKEGIPKLVADFMA
339 LVADFMAKKFSLDAL
340 VADFMAKKFSLDALI
355 THVLPFEKINEGFDL
367 FDLLHSGKSIRTVLT
40 KAYEVRIKMVAVGIC
6 **MSTAGKVIKCKAA
89 TTVKPGDKVIPLFTP

Function

Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed:15369820, PubMed:16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed:15369820)

Protein Sequence

10 MSTAGKVIKC 20 KAAVLWEVKK 30 PFSIEDVEVA 40 PPKAYEVRIK 50 MVAVGICHTD 60 DHVVSGNLVT 70 PLPVILGHEA 80 AGIVESVGEG 90 VTTVKPGDKV 100 IPLFTPQCGK 110 CRVCKNPESN 120 YCLKNDLGNP 130 RGTLQDGTRR 140 FTCRGKPIHH 150 FLGTSTFSQY 160 TVVDENAVAK 170 IDAASPLEKV 180 CLIGCGFSTG 190 YGSAVNVAKV 200 TPGSTCAVFG 210 LGGVGLSAVM 220 GCKAAGAARI 230 IAVDINKDKF 240 AKAKELGATE 250 CINPQDYKKP 260 IQEVLKEMTD 270 GGVDFSFEVI 280 GRLDTMMASL 290 LCCHEACGTS 300 VIVGVPPASQ 310 NLSINPMLLL 320 TGRTWKGAVY 330 GGFKSKEGIP 340 KLVADFMAKK 350 FSLDALITHV 360 LPFEKINEGF 370 DLLHSGKSIR TVLTF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Molecular Function GO:0004022 alcohol dehydrogenase (NAD+) activity
Molecular Function GO:0004745 all-trans-retinol dehydrogenase (NAD+) activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0042573 retinoic acid metabolic process
Biological Process GO:0001523 retinoid metabolic process
Biological Process GO:0042572 retinol metabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.