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Retinal dehydrogenase 1 (RALDH 1) (RalDH1) (EC 1.2.1.-) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic)

 AL1A1_SHEEP             Reviewed;         501 AA.
P51977;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-FEB-2018, entry version 115.
RecName: Full=Retinal dehydrogenase 1 {ECO:0000305};
Short=RALDH 1 {ECO:0000305};
Short=RalDH1 {ECO:0000305};
EC=1.2.1.- {ECO:0000269|PubMed:26373694};
EC=1.2.1.36 {ECO:0000250|UniProtKB:P51647};
AltName: Full=Aldehyde dehydrogenase family 1 member A1 {ECO:0000303|PubMed:9862807};
AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000303|PubMed:7484410};
Name=ALDH1A1 {ECO:0000303|PubMed:9862807};
Synonyms=ALDH1 {ECO:0000303|PubMed:9862807};
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7484410;
Stayner C.K., Tweedie J.W.;
"Cloning and characterisation of the cDNA for sheep liver cytosolic
aldehyde dehydrogenase.";
Adv. Exp. Med. Biol. 372:61-66(1995).
[2]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT,
AND ACTIVE SITE.
PubMed=9862807; DOI=10.1016/S0969-2126(98)00152-X;
Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M.,
Baker E.N.;
"Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals
the basis for the retinal specificity of class 1 aldehyde
dehydrogenases.";
Structure 6:1541-1551(1998).
[3]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-501 IN COMPLEX WITH
DUOCARMYCIN ANALOG AND NAD, SUBUNIT, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=26373694; DOI=10.1002/anie.201505749;
Koch M.F., Harteis S., Blank I.D., Pestel G., Tietze L.F.,
Ochsenfeld C., Schneider S., Sieber S.A.;
"Structural, biochemical, and computational studies reveal the
mechanism of selective aldehyde dehydrogenase 1A1 inhibition by
cytotoxic duocarmycin analogues.";
Angew. Chem. Int. Ed. Engl. 54:13550-13554(2015).
-!- FUNCTION: Can convert/oxidize retinaldehyde to retinoic acid.
Binds free retinal and cellular retinol-binding protein-bound
retinal (By similarity). May have a broader specificity and
oxidize other aldehydes in vivo (PubMed:26373694).
{ECO:0000250|UniProtKB:P51647, ECO:0000269|PubMed:26373694}.
-!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH.
{ECO:0000250|UniProtKB:P51647}.
-!- ENZYME REGULATION: Inhibited by duocarmycin analogs.
{ECO:0000269|PubMed:26373694}.
-!- PATHWAY: Cofactor metabolism; retinol metabolism.
{ECO:0000250|UniProtKB:P51647}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26373694,
ECO:0000269|PubMed:9862807}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P48644}.
-!- PTM: The N-terminus is blocked most probably by acetylation.
{ECO:0000250|UniProtKB:P15437}.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
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EMBL; U12761; AAA85435.1; -; mRNA.
PIR; S78582; S14752.
RefSeq; NP_001009778.1; NM_001009778.1.
UniGene; Oar.873; -.
PDB; 1BXS; X-ray; 2.35 A; A/B/C/D=1-501.
PDB; 5ABM; X-ray; 1.70 A; A/B/C/D=2-501.
PDB; 5AC0; X-ray; 1.90 A; A/B=1-501.
PDB; 5AC1; X-ray; 2.08 A; A/B/C/D=1-501.
PDBsum; 1BXS; -.
PDBsum; 5ABM; -.
PDBsum; 5AC0; -.
PDBsum; 5AC1; -.
ProteinModelPortal; P51977; -.
SMR; P51977; -.
PRIDE; P51977; -.
Ensembl; ENSOART00000013815; ENSOARP00000013613; ENSOARG00000012705.
GeneID; 443343; -.
KEGG; oas:443343; -.
CTD; 216; -.
GeneTree; ENSGT00760000118999; -.
HOVERGEN; HBG000097; -.
KO; K07249; -.
OMA; GEWVKPV; -.
OrthoDB; EOG091G05E8; -.
UniPathway; UPA00912; -.
EvolutionaryTrace; P51977; -.
Proteomes; UP000002356; Chromosome 2.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; ISS:CAFA.
GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
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.
Pfam; PF00171; Aldedh; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; NAD;
Oxidoreductase; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P15437}.
CHAIN 2 501 Retinal dehydrogenase 1.
/FTId=PRO_0000056420.
NP_BIND 167 170 NAD. {ECO:0000244|PDB:1BXS}.
NP_BIND 193 196 NAD. {ECO:0000244|PDB:1BXS}.
NP_BIND 226 227 NAD. {ECO:0000244|PDB:1BXS}.
NP_BIND 246 247 NAD. {ECO:0000244|PDB:1BXS}.
NP_BIND 269 271 NAD. {ECO:0000250|UniProtKB:P00352}.
NP_BIND 349 353 NAD. {ECO:0000250|UniProtKB:P00352}.
NP_BIND 400 402 NAD. {ECO:0000244|PDB:1BXS}.
ACT_SITE 269 269 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10007, ECO:0000255|PROSITE-
ProRule:PRU10008}.
ACT_SITE 303 303 Nucleophile.
{ECO:0000303|PubMed:9862807}.
SITE 170 170 Transition state stabilizer.
{ECO:0000250|UniProtKB:P20000}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P15437}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 337 337 Phosphothreonine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 353 353 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 367 367 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 410 410 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 419 419 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
MOD_RES 495 495 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00352}.
STRAND 22 25 {ECO:0000244|PDB:5ABM}.
STRAND 28 30 {ECO:0000244|PDB:5ABM}.
STRAND 37 41 {ECO:0000244|PDB:5ABM}.
TURN 43 45 {ECO:0000244|PDB:5ABM}.
STRAND 48 53 {ECO:0000244|PDB:5ABM}.
HELIX 57 70 {ECO:0000244|PDB:5ABM}.
HELIX 76 79 {ECO:0000244|PDB:5ABM}.
HELIX 82 98 {ECO:0000244|PDB:5ABM}.
HELIX 100 111 {ECO:0000244|PDB:5ABM}.
HELIX 115 120 {ECO:0000244|PDB:5ABM}.
HELIX 122 136 {ECO:0000244|PDB:5ABM}.
HELIX 137 139 {ECO:0000244|PDB:5ABM}.
STRAND 142 145 {ECO:0000244|PDB:1BXS}.
STRAND 148 159 {ECO:0000244|PDB:5ABM}.
STRAND 162 166 {ECO:0000244|PDB:5ABM}.
STRAND 169 171 {ECO:0000244|PDB:5ABM}.
HELIX 172 185 {ECO:0000244|PDB:5ABM}.
STRAND 189 193 {ECO:0000244|PDB:5ABM}.
HELIX 200 212 {ECO:0000244|PDB:5ABM}.
STRAND 218 221 {ECO:0000244|PDB:5ABM}.
TURN 226 228 {ECO:0000244|PDB:5ABM}.
HELIX 229 234 {ECO:0000244|PDB:5ABM}.
STRAND 241 246 {ECO:0000244|PDB:5ABM}.
HELIX 248 260 {ECO:0000244|PDB:5ABM}.
STRAND 265 269 {ECO:0000244|PDB:5ABM}.
STRAND 275 278 {ECO:0000244|PDB:5ABM}.
HELIX 284 296 {ECO:0000244|PDB:5ABM}.
HELIX 297 300 {ECO:0000244|PDB:5ABM}.
STRAND 308 312 {ECO:0000244|PDB:5ABM}.
HELIX 313 327 {ECO:0000244|PDB:5ABM}.
HELIX 348 364 {ECO:0000244|PDB:5ABM}.
STRAND 367 370 {ECO:0000244|PDB:5ABM}.
STRAND 373 379 {ECO:0000244|PDB:5ABM}.
STRAND 385 389 {ECO:0000244|PDB:5ABM}.
HELIX 395 398 {ECO:0000244|PDB:5ABM}.
STRAND 403 411 {ECO:0000244|PDB:5ABM}.
HELIX 414 422 {ECO:0000244|PDB:5ABM}.
STRAND 428 433 {ECO:0000244|PDB:5ABM}.
HELIX 437 446 {ECO:0000244|PDB:5ABM}.
STRAND 450 455 {ECO:0000244|PDB:5ABM}.
HELIX 470 472 {ECO:0000244|PDB:5ABM}.
STRAND 473 475 {ECO:0000244|PDB:5ABM}.
HELIX 479 484 {ECO:0000244|PDB:5ABM}.
STRAND 487 495 {ECO:0000244|PDB:5ABM}.
SEQUENCE 501 AA; 54825 MW; 58B897197D621AB1 CRC64;
MSSSAMPDVP APLTNLQFKY TKIFINNEWH SSVSGKKFPV FNPATEEKLC EVEEGDKEDV
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLIERDR LLLATMEAMN GGKLFSNAYL
MDLGGCIKTL RYCAGWADKI QGRTIPMDGN FFTYTRSEPV GVCGQIIPWN FPLLMFLWKI
GPALSCGNTV VVKPAEQTPL TALHMGSLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
KVAFTGSTEV GKLIKEAAGK SNLKRVSLEL GGKSPCIVFA DADLDNAVEF AHQGVFYHQG
QCCIAASRLF VEESIYDEFV RRSVERAKKY VLGNPLTPGV SQGPQIDKEQ YEKILDLIES
GKKEGAKLEC GGGPWGNKGY FIQPTVFSDV TDDMRIAKEE IFGPVQQIMK FKSLDDVIKR
ANNTFYGLSA GIFTNDIDKA ITVSSALQSG TVWVNCYSVV SAQCPFGGFK MSGNGRELGE
YGFHEYTEVK TVTIKISQKN S


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