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AL3A1_BOVIN
ID   AL3A1_BOVIN             Reviewed;         239 AA.
AC   P30907;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Aldehyde dehydrogenase, dimeric NADP-preferring;
DE            EC=1.2.1.5 {ECO:0000250|UniProtKB:P47739};
DE   AltName: Full=Aldehyde dehydrogenase 3;
DE   AltName: Full=Aldehyde dehydrogenase family 3 member A1;
DE   AltName: Full=Corneal 15.8 kDa protein;
DE   AltName: Full=Corneal protein 54;
DE            Short=bCP54;
DE   AltName: Full=Transparentin;
DE   Flags: Fragment;
GN   Name=ALDH3A1; Synonyms=ALDH3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cornea;
RX   PubMed=1842923; DOI=10.1101/gr.1.1.57;
RA   Cooper D.L., Baptist E.W.;
RT   "Degenerate oligonucleotide sequence-directed cross-species PCR cloning of
RT   the BCP 54/ALDH 3 cDNA: priming from inverted repeats and formation of
RT   tandem primer arrays.";
RL   PCR Methods Appl. 1:57-62(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-140.
RC   TISSUE=Cornea;
RX   PubMed=2016061; DOI=10.1016/0378-1119(91)90174-a;
RA   Cooper D.L., Baptist E.W., Enghild J.J., Isola N.R., Klintworth G.K.;
RT   "Bovine corneal protein 54K (BCP54) is a homologue of the tumor-associated
RT   (class 3) rat aldehyde dehydrogenase (RATALD).";
RL   Gene 98:201-207(1991).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2276277; DOI=10.3109/02713689008999573;
RA   Cooper D.L., Baptist E.W., Enghild J.J., Lee H., Isola N.R.,
RA   Klintworth G.K.;
RT   "Partial amino acid sequence determination of bovine corneal protein 54 K
RT   (BCP 54).";
RL   Curr. Eye Res. 9:781-786(1990).
CC   -!- FUNCTION: ALDHs play a major role in the detoxification of alcohol-
CC       derived acetaldehyde (Probable). They are involved in the metabolism of
CC       corticosteroids, biogenic amines, neurotransmitters, and lipid
CC       peroxidation (Probable). Oxidizes medium and long chain aldehydes into
CC       non-toxic fatty acids (By similarity). Preferentially oxidizes aromatic
CC       aldehyde substrates (By similarity). Comprises about 50 percent of
CC       corneal epithelial soluble proteins (By similarity). May play a role in
CC       preventing corneal damage caused by ultraviolet light (By similarity).
CC       {ECO:0000250|UniProtKB:P30838, ECO:0000250|UniProtKB:P47739,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.5;
CC         Evidence={ECO:0000250|UniProtKB:P47739};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC         Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P47739};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30838}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; S51969; AAB24736.2; -; mRNA.
DR   EMBL; M37384; AAA30468.1; -; mRNA.
DR   PIR; PS0412; PS0412.
DR   PIR; T01406; T01406.
DR   AlphaFoldDB; P30907; -.
DR   SMR; P30907; -.
DR   STRING; 9913.ENSBTAP00000028125; -.
DR   PaxDb; P30907; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   InParanoid; P30907; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; PTHR43570; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lipid metabolism; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           <1..>239
FT                   /note="Aldehyde dehydrogenase, dimeric NADP-preferring"
FT                   /id="PRO_0000056469"
FT   ACT_SITE        30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   NON_TER         1
FT   NON_TER         239
SQ   SEQUENCE   239 AA;  26743 MW;  16BD07206287716C CRC64;
     NPHYVDKDRD LDIACRRIAW GKFMNSGQTC VAPDYILCDP SIQSQVVEKL KKSLKEFYGE
     DAKKSRDYGR IINSRHFQRV MGLLEGQKVA YGGTGDATTR YIAPTILTDV DPESPVMQEE
     VFGPVLPIMC VRSLEEAIQF ITQREKPLAL YVFSPNDKVI KKMIAETSSG GVTANDVVVH
     ISVHSLPYGG VGDSGMGSYH GRKSFETFSH RRSCLVRPLL NEETLKARYP RARPICPDT
 
 
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