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Database: UniProt/SWISS-PROT
Entry: ALDH2_PIG
LinkDB: ALDH2_PIG
Original site: ALDH2_PIG 
ID   ALDH2_PIG               Reviewed;         521 AA.
AC   Q2XQV4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   13-FEB-2019, entry version 94.
DE   RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 2;
DE   AltName: Full=ALDH-E2;
DE   Flags: Precursor;
GN   Name=ALDH2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ji Y., Bennett B.M.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is capable of converting retinaldehyde to retinoic acid.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; DQ266356; ABB70228.1; -; mRNA.
DR   RefSeq; NP_001038076.1; NM_001044611.2.
DR   UniGene; Ssc.11147; -.
DR   ProteinModelPortal; Q2XQV4; -.
DR   SMR; Q2XQV4; -.
DR   STRING; 9823.ENSSSCP00000010556; -.
DR   PaxDb; Q2XQV4; -.
DR   PeptideAtlas; Q2XQV4; -.
DR   PRIDE; Q2XQV4; -.
DR   Ensembl; ENSSSCT00000055390; ENSSSCP00000053451; ENSSSCG00000009889.
DR   GeneID; 733685; -.
DR   KEGG; ssc:733685; -.
DR   CTD; 217; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   eggNOG; COG1012; LUCA.
DR   GeneTree; ENSGT00940000156240; -.
DR   HOGENOM; HOG000271505; -.
DR   HOVERGEN; HBG000097; -.
DR   InParanoid; Q2XQV4; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   OrthoDB; 153834at2759; -.
DR   TreeFam; TF300455; -.
DR   Reactome; R-SSC-71384; Ethanol oxidation.
DR   UniPathway; UPA00780; UER00768.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Bgee; ENSSSCG00000009889; Expressed in 6 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q2XQV4; baseline and differential.
DR   Genevisible; Q2XQV4; SS.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IBA:GO_Central.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Mitochondrion; NAD; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     21       Mitochondrion. {ECO:0000250}.
FT   CHAIN        22    521       Aldehyde dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000312492.
FT   NP_BIND     266    271       NAD. {ECO:0000250}.
FT   ACT_SITE    289    289       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   ACT_SITE    323    323       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10007, ECO:0000255|PROSITE-
FT                                ProRule:PRU10008}.
FT   SITE        190    190       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P20000}.
FT   MOD_RES      56     56       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES      77     77       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     163    163       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     372    372       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     379    379       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     387    387       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     430    430       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     432    432       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     445    445       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
FT   MOD_RES     455    455       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P47738}.
SQ   SEQUENCE   521 AA;  56921 MW;  12913E10ECD560A7 CRC64;
     MLRPAALAAA RLVLRQGRRL LSAAPTQAVP APNQQPEIFY NQIFINNEWH DAISKKTFPT
     VNPSTGDVIC HVAEGDKEDV DRAVEAARAA FQLGSPWRRL DASDRGRLLN RLADLIERDR
     TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTLPIDGD YFSYTRHEPV
     GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVSEQTPL TALYVANLIK EAGFPPGVVN
     IVPGYGPTAG AAIASHEDVD KVAFTGSTEV GHLIQVAAGK SNLKRVTLEL GGKSPNIIMS
     DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYAEFV ERSVARARSR VVGNPFDSRT
     EQGPQIDETQ FKKILGYIKS GKEEGAKLLC GGGAAADRGY FIQPTVFGDV QDGMTIAKEE
     IFGPVMQILK FKTIEEVIGR ANNSKYGLAA AVFTKDLDKA NYLSQALQAG TVWVNCYDVF
     GAQSPFGGYK LSGSGRELGE YGLQAYTEVK TVTVKVPQKN S
//
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