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ID AL1A1_HUMAN Reviewed; 501 AA.
AC P00352; O00768; Q5SYR1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 05-APR-2011, entry version 126.
DE RecName: Full=Retinal dehydrogenase 1;
DE Short=RALDH 1;
DE Short=RalDH1;
DE EC=1.2.1.36;
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1;
DE AltName: Full=Aldehyde dehydrogenase, cytosolic;
GN Name=ALDH1A1; Synonyms=ALDC, ALDH1, PUMB1;
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 [GENOMIC DNA].
RX MEDLINE=90077427; PubMed=2591967; DOI=10.1016/0888-7543(89)90127-4;
RA Hsu L.C., Chang W.-C., Yoshida A.;
RT "Genomic structure of the human cytosolic aldehyde dehydrogenase
RT gene.";
RL Genomics 5:857-865(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-121.
RC TISSUE=Liver;
RX MEDLINE=94027752; PubMed=8214422;
RX DOI=10.1111/j.1530-0277.1993.tb00849.x;
RA Zheng C.F., Wang T.T., Weiner H.;
RT "Cloning and expression of the full-length cDNAS encoding human liver
RT class 1 and class 2 aldehyde dehydrogenase.";
RL Alcohol. Clin. Exp. Res. 17:828-831(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Ramana K.V., Xiao T., Ansari N.H.;
RT "Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from
RT human lens cDNA library.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-177.
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX MEDLINE=93263033; PubMed=8493914;
RA Yoshida A., Hsu L.C., Yanagawa Y.;
RT "Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal
RT response, retinal oxidation and implication in testicular
RT feminization.";
RL Adv. Exp. Med. Biol. 328:37-44(1993).
RN [10]
RP PROTEIN SEQUENCE OF 2-501, AND ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX MEDLINE=84208019; PubMed=6723659;
RX DOI=10.1111/j.1432-1033.1984.tb08150.x;
RA Hempel J., von Bahr-Lindstroem H., Joernvall H.;
RT "Aldehyde dehydrogenase from human liver. Primary structure of the
RT cytoplasmic isoenzyme.";
RL Eur. J. Biochem. 141:21-35(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
RX MEDLINE=85252089; PubMed=4015823; DOI=10.1016/0741-8329(85)90024-2;
RA Yoshida A., Ikawa M., Hsu L.C., Tani K.;
RT "Molecular abnormality and cDNA cloning of human aldehyde
RT dehydrogenases.";
RL Alcohol 2:103-106(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
RC TISSUE=Liver;
RX MEDLINE=85216574; PubMed=2987944; DOI=10.1073/pnas.82.11.3771;
RA Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
RT "Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
RN [13]
RP PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, AND
RP NAD-BINDING SITE CYS-456.
RX MEDLINE=88050861; PubMed=3676276; DOI=10.1021/bi00392a015;
RA Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R.;
RT "Active site of human liver aldehyde dehydrogenase.";
RL Biochemistry 26:5679-5684(1987).
RN [14]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte;
RX MEDLINE=89377753; PubMed=2776714;
RA Agarwal D.P., Cohn P., Goedde H.W., Hempel J.;
RT "Aldehyde dehydrogenase from human erythrocytes: structural
RT relationship to the liver cytosolic isozyme.";
RL Enzyme 42:47-52(1989).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252;
RP LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds free retinal and cellular retinol-binding protein-
CC bound retinal. Can convert/oxidize retinaldehyde to retinoic acid
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/aldh1a1/";
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DR EMBL; M31994; AAA51692.1; -; Genomic_DNA.
DR EMBL; M31982; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31983; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31984; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31985; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31986; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31987; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31988; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31989; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31990; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31991; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; M31992; AAA51692.1; JOINED; Genomic_DNA.
DR EMBL; AF003341; AAC51652.1; -; mRNA.
DR EMBL; AY390731; AAR92229.1; -; mRNA.
DR EMBL; BT006921; AAP35567.1; -; mRNA.
DR EMBL; AY338497; AAP88039.1; -; Genomic_DNA.
DR EMBL; AL591031; CAI12257.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62543.1; -; Genomic_DNA.
DR EMBL; BC001505; AAH01505.1; -; mRNA.
DR EMBL; S61235; AAD13925.1; -; Genomic_DNA.
DR EMBL; M26761; AAA35518.1; -; mRNA.
DR EMBL; K03000; AAA51695.1; -; mRNA.
DR IPI; IPI00218914; -.
DR PIR; A33371; DEHUE1.
DR RefSeq; NP_000680.2; NM_000689.3.
DR UniGene; Hs.76392; -.
DR ProteinModelPortal; P00352; -.
DR SMR; P00352; 8-501.
DR IntAct; P00352; 4.
DR STRING; P00352; -.
DR PhosphoSite; P00352; -.
DR SWISS-2DPAGE; P00352; -.
DR Cornea-2DPAGE; P00352; -.
DR DOSAC-COBS-2DPAGE; P00352; -.
DR REPRODUCTION-2DPAGE; IPI00218914; -.
DR REPRODUCTION-2DPAGE; P00352; -.
DR UCD-2DPAGE; P00352; -.
DR PeptideAtlas; P00352; -.
DR PRIDE; P00352; -.
DR Ensembl; ENST00000297785; ENSP00000297785; ENSG00000165092.
DR GeneID; 216; -.
DR KEGG; hsa:216; -.
DR UCSC; uc004ajd.1; human.
DR CTD; 216; -.
DR GeneCards; GC09M045338; -.
DR H-InvDB; HIX0008099; -.
DR HGNC; HGNC:402; ALDH1A1.
DR HPA; CAB020690; -.
DR HPA; HPA002123; -.
DR MIM; 100640; gene.
DR neXtProt; NX_P00352; -.
DR PharmGKB; PA24692; -.
DR eggNOG; prNOG13758; -.
DR HOGENOM; HBG752218; -.
DR HOVERGEN; HBG000097; -.
DR InParanoid; P00352; -.
DR OMA; VNCYSVV; -.
DR OrthoDB; EOG4Z8XW6; -.
DR PhylomeDB; P00352; -.
DR BRENDA; 1.2.1.36; 247.
DR Reactome; REACT_13433; Biological oxidations.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB00162; Vitamin A.
DR NextBio; 874; -.
DR ArrayExpress; P00352; -.
DR Bgee; P00352; -.
DR CleanEx; HS_ALDH1A1; -.
DR Genevestigator; P00352; -.
DR GermOnline; ENSG00000165092; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; TAS:Reactome.
DR GO; GO:0005497; F:androgen binding; TAS:ProtInc.
DR GO; GO:0005099; F:Ras GTPase activator activity; TAS:UniProtKB.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IEA:EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; TAS:ProtInc.
DR GO; GO:0006069; P:ethanol oxidation; TAS:Reactome.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW NAD; Oxidoreductase; Polymorphism.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 501 Retinal dehydrogenase 1.
FT /FTId=PRO_0000056415.
FT NP_BIND 246 251 NAD (By similarity).
FT ACT_SITE 269 269 Proton acceptor.
FT ACT_SITE 303 303 Nucleophile.
FT BINDING 456 456 NAD.
FT SITE 170 170 Transition state stabilizer (By
FT similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 91 91 N6-acetyllysine.
FT MOD_RES 128 128 N6-acetyllysine.
FT MOD_RES 252 252 N6-acetyllysine.
FT MOD_RES 353 353 N6-acetyllysine.
FT MOD_RES 367 367 N6-acetyllysine.
FT MOD_RES 410 410 N6-acetyllysine.
FT MOD_RES 419 419 N6-acetyllysine.
FT MOD_RES 435 435 N6-acetyllysine.
FT MOD_RES 495 495 N6-acetyllysine.
FT VARIANT 121 121 N -> S (in dbSNP:rs1049981).
FT /FTId=VAR_048901.
FT VARIANT 125 125 G -> R (in dbSNP:rs11554423).
FT /FTId=VAR_048902.
FT VARIANT 177 177 I -> F (in dbSNP:rs8187929).
FT /FTId=VAR_017778.
FT CONFLICT 162 162 V -> I (in Ref. 11; AAA35518 and 12;
FT AAA51695).
SQ SEQUENCE 501 AA; 54862 MW; B26464DC7168348E CRC64;
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV
DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL
NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI
GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID
KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES
GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR
ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE
YGFHEYTEVK TVTVKISQKN S
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