ID   AL1A2_HUMAN             Reviewed;         518 AA.
AC   O94788; B3KY52; Q2PJS6; Q8NHQ4; Q9UBR8; Q9UFY0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   07-JUL-2009, entry version 86.
DE   RecName: Full=Retinal dehydrogenase 2;
DE            Short=RALDH 2;
DE            Short=RalDH2;
DE            EC=1.2.1.36;
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=RALDH2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-348.
RX   MEDLINE=99038200; PubMed=9819382;
RA   Ono Y., Fukuhara N., Yoshie O.;
RT   "TAL1 and LIM-only proteins synergistically induce retinaldehyde
RT   dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by
RT   acting as cofactors for GATA3.";
RL   Mol. Cell. Biol. 18:6939-6950(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ILE-348.
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-50; VAL-110;
RP   ILE-348 AND LYS-436.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-518 (ISOFORMS 1/2), AND
RP   VARIANT ILE-348.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Recognizes as substrates free retinal and cellular
CC       retinol-binding protein-bound retinal. Does metabolize octanal and
CC       decanal but does not metabolize citral, benzaldehyde, acetaldehyde
CC       and propanal efficiently (By similarity).
CC   -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O94788-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O94788-2; Sequence=VSP_017363;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/aldh1a2/";
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DR   EMBL; AB015226; BAA34785.1; -; mRNA.
DR   EMBL; AB015227; BAA34786.1; ALT_INIT; mRNA.
DR   EMBL; AB015228; BAA34787.1; ALT_INIT; mRNA.
DR   EMBL; AK128709; BAG54714.1; -; mRNA.
DR   EMBL; DQ322171; ABC40749.1; -; Genomic_DNA.
DR   EMBL; BC030589; AAH30589.1; -; mRNA.
DR   EMBL; AL110299; CAB53740.2; -; mRNA.
DR   IPI; IPI00169288; -.
DR   IPI; IPI00216805; -.
DR   PIR; T14799; T14799.
DR   RefSeq; NP_003879.2; -.
DR   RefSeq; NP_733797.1; -.
DR   RefSeq; NP_733798.1; -.
DR   UniGene; Hs.708331; -.
DR   HSSP; Q63639; 1BI9.
DR   PhosphoSite; O94788; -.
DR   PRIDE; O94788; -.
DR   Ensembl; ENSG00000128918; Homo sapiens.
DR   GeneID; 8854; -.
DR   KEGG; hsa:8854; -.
DR   NMPDR; fig|9606.3.peg.10760; -.
DR   UCSC; uc002aew.1; human.
DR   UCSC; uc002aey.1; human.
DR   GeneCards; GC15M056032; -.
DR   H-InvDB; HIX0012280; -.
DR   HGNC; HGNC:15472; ALDH1A2.
DR   HPA; HPA010022; -.
DR   MIM; 603687; gene.
DR   PharmGKB; PA24693; -.
DR   HOGENOM; O94788; -.
DR   HOVERGEN; O94788; -.
DR   OMA; O94788; HVGIDKI.
DR   BRENDA; 1.2.1.36; 247.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB00755; Tretinoin.
DR   DrugBank; DB00162; Vitamin A.
DR   NextBio; 33241; -.
DR   ArrayExpress; O94788; -.
DR   Bgee; O94788; -.
DR   CleanEx; HS_ALDH1A2; -.
DR   GermOnline; ENSG00000128918; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0016918; F:retinal binding; ISS:UniProtKB.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0021915; P:neural tube development; IMP:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0034097; P:response to cytokine stimulus; IDA:UniProtKB.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm; NAD;
KW   Oxidoreductase; Phosphoprotein; Polymorphism.
FT   CHAIN         1    518       Retinal dehydrogenase 2.
FT                                /FTId=PRO_0000056422.
FT   NP_BIND     263    268       NAD (By similarity).
FT   ACT_SITE    286    286       Proton acceptor (By similarity).
FT   ACT_SITE    320    320       Nucleophile (By similarity).
FT   SITE        187    187       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     122    122       Phosphothreonine (By similarity).
FT   VAR_SEQ     229    266       Missing (in isoform 2).
FT                                /FTId=VSP_017363.
FT   VARIANT      50     50       E -> G (in dbSNP:rs34266719).
FT                                /FTId=VAR_025439.
FT   VARIANT     110    110       A -> V.
FT                                /FTId=VAR_025440.
FT   VARIANT     348    348       V -> I (in dbSNP:rs4646626).
FT                                /FTId=VAR_025441.
FT   VARIANT     436    436       E -> K.
FT                                /FTId=VAR_025442.
SQ   SEQUENCE   518 AA;  56724 MW;  AAEE7A886951373F CRC64;
     MTSSKIEMPG EVKADPAALM ASLHLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVYNP
     ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRAVL
     ATMESLNGGK PFLQAFYVDL QGVIKTFRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC
     GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVINILP
     GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
     LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVRRS VERAKRRVVG SPFDPTTEQG
     PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG
     PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ
     SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS
//