AL1A2_MOUSE
ID AL1A2_MOUSE Reviewed; 518 AA.
AC Q62148; Q6DI79;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Retinal dehydrogenase 2;
DE Short=RALDH 2 {ECO:0000303|PubMed:8797830};
DE Short=RalDH2 {ECO:0000303|PubMed:8797830};
DE EC=1.2.1.36 {ECO:0000269|PubMed:8797830};
DE AltName: Full=Aldehyde dehydrogenase family 1 member A2;
DE AltName: Full=Retinaldehyde-specific dehydrogenase type 2;
DE Short=RALDH(II);
GN Name=Aldh1a2; Synonyms=Aldh1a7, Raldh2 {ECO:0000303|PubMed:8797830};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=C3H/He;
RX PubMed=8797830; DOI=10.1111/j.1432-1033.1996.0015h.x;
RA Zhao D., McCaffery P., Ivins K.J., Neve R.L., Hogan P., Chin W.W.,
RA Draeger U.C.;
RT "Molecular identification of a major retinoic-acid-synthesizing enzyme, a
RT retinaldehyde-specific dehydrogenase.";
RL Eur. J. Biochem. 240:15-22(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-518.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts retinaldehyde to retinoic acid (PubMed:8797830).
CC Recognizes as substrates free retinal and cellular retinol-binding
CC protein-bound retinal (By similarity). Lacks activity with
CC benzaldehyde, acetaldehyde and octanal (PubMed:8797830). Displays
CC complete lack of activity with citral (By similarity).
CC {ECO:0000250|UniProtKB:Q63639, ECO:0000269|PubMed:8797830}.
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:0000269|PubMed:8797830};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:8797830}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O94788}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA67666.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X99273; CAA67666.1; ALT_INIT; mRNA.
DR EMBL; BC075704; AAH75704.1; -; mRNA.
DR EMBL; AK078553; BAC37332.1; ALT_INIT; mRNA.
DR CCDS; CCDS52852.1; -.
DR PIR; S74224; S74224.
DR RefSeq; NP_033048.2; NM_009022.4.
DR AlphaFoldDB; Q62148; -.
DR SMR; Q62148; -.
DR BioGRID; 202578; 1.
DR STRING; 10090.ENSMUSP00000034723; -.
DR iPTMnet; Q62148; -.
DR PhosphoSitePlus; Q62148; -.
DR REPRODUCTION-2DPAGE; IPI00122212; -.
DR REPRODUCTION-2DPAGE; Q62148; -.
DR EPD; Q62148; -.
DR jPOST; Q62148; -.
DR MaxQB; Q62148; -.
DR PaxDb; Q62148; -.
DR PeptideAtlas; Q62148; -.
DR PRIDE; Q62148; -.
DR ProteomicsDB; 285805; -.
DR Antibodypedia; 2127; 377 antibodies from 32 providers.
DR DNASU; 19378; -.
DR Ensembl; ENSMUST00000034723; ENSMUSP00000034723; ENSMUSG00000013584.
DR GeneID; 19378; -.
DR KEGG; mmu:19378; -.
DR UCSC; uc009qox.2; mouse.
DR CTD; 8854; -.
DR MGI; MGI:107928; Aldh1a2.
DR VEuPathDB; HostDB:ENSMUSG00000013584; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000158898; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q62148; -.
DR OMA; RKAFEKW; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q62148; -.
DR TreeFam; TF300455; -.
DR BRENDA; 1.2.1.36; 3474.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 19378; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Aldh1a2; mouse.
DR PRO; PR:Q62148; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q62148; protein.
DR Bgee; ENSMUSG00000013584; Expressed in associated mesenchyme of midgut and 284 other tissues.
DR Genevisible; Q62148; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016918; F:retinal binding; ISO:MGI.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:MGI.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB.
DR GO; GO:0009855; P:determination of bilateral symmetry; IMP:MGI.
DR GO; GO:0031076; P:embryonic camera-type eye development; IGI:MGI.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0060324; P:face development; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007507; P:heart development; TAS:DFLAT.
DR GO; GO:0001947; P:heart looping; TAS:DFLAT.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0014032; P:neural crest cell development; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0031016; P:pancreas development; IMP:MGI.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR GO; GO:1905562; P:regulation of vascular endothelial cell proliferation; IMP:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IDA:MGI.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; ISO:MGI.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:MGI.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI.
DR GO; GO:0090242; P:retinoic acid receptor signaling pathway involved in somitogenesis; IMP:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:DFLAT.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0035799; P:ureter maturation; IMP:MGI.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..518
FT /note="Retinal dehydrogenase 2"
FT /id="PRO_0000056423"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 184..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 210..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 366..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT SITE 187
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O94788"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94788"
SQ SEQUENCE 518 AA; 56626 MW; 2BC35B5C90046ABC CRC64;
MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVCNP
ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRATL
ATMESLNGGK PFLQAFYIDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC
GQIIPWNFPL LMFTWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP
GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG SPFDPTTEQG
PQIDKKQYNK VLELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG
PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALMV SSAMQAGTVW INCYNALNAQ
SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS
