LipidDB-9606-01397

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-9606-01397

Entry Name

UniProt Accession

P43353; A3FMP9; Q53XL5; Q8N515; Q96CK8;

Theoretical PI

7.55

Molecular Weight

51839.7

Genbank Protein ID

AAA83428.1; ABN58743.1; AAP88834.1; BAF84194.1; EAW74680.1; AAH13584.1; AAH14168.2; AAH33099.1;

Genbank Nucleotide ID

U10868; EF411198; BT009832; AK291505; CH471076; BC013584; BC014168; BC033099;

Protein Name

Aldehyde dehydrogenase family 3 member B1

Protein Synonyms/Alias

1.2.1.5; Aldehyde dehydrogenase 7;

Gene Name

ALDH3B1

Gene Synonyms/Alias

ALDH7;

Created Date

01-NOV-1995

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
463	Canonical	VAMEAQGCSCTLL**	[1]	S-Palmitoylation
465	Canonical	MEAQGCSCTLL****	[1]	S-Farnesylation

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Kitamura T, Naganuma T, Abe K, Nakahara K, Ohno Y, Kihara A. Substratespecificity, plasma membrane localization, and lipid modification of the aldehydedehydrogenase ALDH3B1. Biochim Biophys Acta. 2013 Aug;1831(8):1395-401. doi:10.1016/j.bbalip.2013.05.007. Epub 2013 May 27.[PMID:23721920]

Functional Description

Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde. Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. May not metabolize short chain aldehydes. May use both NADP(+) and NAD(+) as cofactors. May have a protective role against the cytotoxicity induced by lipid peroxidation.

Sequence Annotation

Nucleotide-binding: 188 193 NAD.
Active site: 210 210
Active site: 244 244
Modified residue: 1 1 N-acetylmethionine.

Protein Length

468 AA.

Protein Sequence
(Canonical)

MDPLGDTLRR LREAFHAGRT RPAEFRAAQL QGLGRFLQEN KQLLHDALAQ DLHKSAFESE  60
VSEVAISQGE VTLALRNLRA WMKDERVPKN LATQLDSAFI RKEPFGLVLI IAPWNYPLNL  120
TLVPLVGALA AGNCVVLKPS EISKNVEKIL AEVLPQYVDQ SCFAVVLGGP QETGQLLEHR  180
FDYIFFTGSP RVGKIVMTAA AKHLTPVTLE LGGKNPCYVD DNCDPQTVAN RVAWFRYFNA  240
GQTCVAPDYV LCSPEMQERL LPALQSTITR FYGDDPQSSP NLGRIINQKQ FQRLRALLGC  300
GRVAIGGQSD ESDRYIAPTV LVDVQEMEPV MQEEIFGPIL PIVNVQSLDE AIEFINRREK  360
PLALYAFSNS SQVVKRVLTQ TSSGGFCGND GFMHMTLASL PFGGVGASGM GRYHGKFSFD  420
TFSHHRACLL RSPGMEKLNA LRYPPQSPRR LRMLLVAMEA QGCSCTLL               468
MDPLGDTLRR LREAFHAGRT RPAEFRAAQL QGLGRFLQEN KQLLHDALAQ DLHKSAFESE  60
VSEVAISQGE VTLALRNLRA WMKDERVPKN LATQLDSAFI RKEPFGLVLI IAPWNYPLNL  120
TLVPLVGALA AGNCVVLKPS EISKNVEKIL AEVLPQYVDQ SCFAVVLGGP QETGQLLEHR  180
FDYIFFTGSP RVGKIVMTAA AKHLTPVTLE LGGKNPCYVD DNCDPQTVAN RVAWFRYFNA  240
GQTCVAPDYV LCSPEMQERL LPALQSTITR FYGDDPQSSP NLGRIINQKQ FQRLRALLGC  300
GRVAIGGQSD ESDRYIAPTV LVDVQEMEPV MQEEIFGPIL PIVNVQSLDE AIEFINRREK  360
PLALYAFSNS SQVVKRVLTQ TSSGGFCGND GFMHMTLASL PFGGVGASGM GRYHGKFSFD  420
TFSHHRACLL RSPGMEKLNA LRYPPQSPRR LRMLLVAMEA QGCSCTLL               468

FASTA
(Canonical)

>LipidDB-9606-01397|P43353
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL

Gene Ontology

GO:0005737; C:cytoplasm; IDA:MGI
GO:0005829; C:cytosol; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0031982; C:vesicle; IDA:UniProtKB
GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:ProtInc
GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:MGI
GO:0006066; P:alcohol metabolic process; TAS:ProtInc
GO:0046185; P:aldehyde catabolic process; IDA:MGI
GO:0034599; P:cellular response to oxidative stress; IDA:MGI
GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway
GO:0006629; P:lipid metabolic process; TAS:ProtInc
GO:0055114; P:oxidation-reduction process; IDA:MGI

Interpro

InterPro; IPR016161; Ald_DH/histidinol_DH
InterPro; IPR016163; Ald_DH_C
InterPro; IPR016160; Ald_DH_CS_CYS
InterPro; IPR029510; Ald_DH_CS_GLU
InterPro; IPR016162; Ald_DH_N
InterPro; IPR015590; Aldehyde_DH_dom
InterPro; IPR012394; Aldehyde_DH_NAD(P)

Pfam

Pfam; PF00171; Aldedh;

SMART

PROSITE

PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS;
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU;

PRINTS