ID F7H8D6_CALJA Unreviewed; 488 AA.
AC F7H8D6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Retinal dehydrogenase 2 {ECO:0000256|ARBA:ARBA00041052};
DE EC=1.2.1.36 {ECO:0000256|ARBA:ARBA00039134};
DE AltName: Full=Aldehyde dehydrogenase family 1 member A2 {ECO:0000256|ARBA:ARBA00041636};
DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2 {ECO:0000256|ARBA:ARBA00043059};
GN Name=ALDH1A2 {ECO:0000313|Ensembl:ENSCJAP00000048483.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000048483.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000048483.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000048483.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate;
CC Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000256|ARBA:ARBA00036070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16178;
CC Evidence={ECO:0000256|ARBA:ARBA00036070};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-13,14-dihydroretinal + H2O + NAD(+) = all-
CC trans-13,14-dihydroretinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:75119,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:194182, ChEBI:CHEBI:194183;
CC Evidence={ECO:0000256|ARBA:ARBA00035998};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75120;
CC Evidence={ECO:0000256|ARBA:ARBA00035998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000256|ARBA:ARBA00035919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000256|ARBA:ARBA00035919};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000256|ARBA:ARBA00004891}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR AlphaFoldDB; F7H8D6; -.
DR Ensembl; ENSCJAT00000061248.3; ENSCJAP00000048483.2; ENSCJAG00000002282.5.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000158898; -.
DR TreeFam; TF300455; -.
DR Proteomes; UP000008225; Chromosome 10.
DR Bgee; ENSCJAG00000002282; Expressed in ovary and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF102; RETINAL DEHYDROGENASE 2; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 16..479
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 53413 MW; 7E233876125554CB CRC64;
TEGGTWAAKI FINNEWQNSE SGRVFPVYNP ATGEQVCEVQ EADKADIDKA VQAARLAFSL
GSVWRRMDAS ERGRLLDKLA DLVERDRAVL ATMESLNGGK PFLQAFYVDL QGVIKTLRYY
AGWADKIHGM TIPVDGDYFT FTRHEPIGVC GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK
PAEQTPLSAL YMGALIKEAG FPPGVINILP GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL
IQEAAGRSNL KRVTLELGGK SPNIIFADAD LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE
SIYEEFVRRS VERAKRRIVG SPFDPTTEQG PQIDKKQYNK ILELIQSGVA EGAKLECGGK
GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG PVQEILRFKT MDEVIERANN SDFGLVAAVF
TNDINKALTV SSAMQAGTVW INCYNALNAQ SPFGGFKMSG NGREMGEFGL REYSEVKTVT
VKIPQKNS
//
