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Q28399

- ALDH1_ELEED

UniProt

Q28399 - ALDH1_ELEED

Protein

Aldehyde dehydrogenase, cytosolic 1

Gene

ALDH1

Organism
Elephantulus edwardii (Cape long-eared elephant shrew)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.1 Publication

    Catalytic activityi

    An aldehyde + NAD+ + H2O = a carboxylate + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei170 – 1701Transition state stabilizer
    Active sitei269 – 2691Proton acceptor
    Active sitei303 – 3031Nucleophile

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 2516NAD1 Publication

    GO - Molecular functioni

    1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC

    GO - Biological processi

    1. ethanol catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.2.1.36. 7360.
    UniPathwayiUPA00780; UER00768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde dehydrogenase, cytosolic 1 (EC:1.2.1.3)
    Alternative name(s):
    ALDH class 1
    ETA-crystallin
    Gene namesi
    Name:ALDH1
    OrganismiElephantulus edwardii (Cape long-eared elephant shrew)
    Taxonomic identifieri28737 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaAfrotheriaMacroscelideaMacroscelididaeElephantulus

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 501501Aldehyde dehydrogenase, cytosolic 1PRO_0000056427Add
    BLAST

    Proteomic databases

    PRIDEiQ28399.

    Expressioni

    Tissue specificityi

    Eye specific, with very high expression in the lens.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 254
    Beta strandi28 – 303
    Beta strandi37 – 415
    Turni43 – 453
    Beta strandi48 – 536
    Helixi57 – 7115
    Helixi76 – 794
    Helixi82 – 9817
    Helixi100 – 11112
    Helixi115 – 1206
    Helixi122 – 13615
    Helixi137 – 1393
    Beta strandi142 – 1454
    Beta strandi148 – 15912
    Beta strandi162 – 1665
    Helixi172 – 18514
    Beta strandi189 – 1935
    Helixi200 – 21213
    Beta strandi218 – 2214
    Turni226 – 2283
    Helixi229 – 2346
    Beta strandi241 – 2466
    Helixi248 – 26013
    Beta strandi265 – 2695
    Beta strandi274 – 2785
    Helixi284 – 29613
    Helixi297 – 3004
    Beta strandi306 – 3127
    Helixi313 – 32614
    Helixi348 – 36417
    Beta strandi367 – 3704
    Beta strandi373 – 3797
    Beta strandi385 – 3906
    Helixi395 – 3984
    Beta strandi403 – 4119
    Helixi414 – 4229
    Beta strandi423 – 4253
    Beta strandi428 – 4336
    Helixi437 – 44610
    Beta strandi449 – 4557
    Helixi470 – 4723
    Beta strandi473 – 4753
    Helixi479 – 4835
    Helixi484 – 4863
    Beta strandi487 – 4959

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O9JX-ray2.40A/B/C/D1-501[»]
    1PEJmodel-A1-501[»]
    ProteinModelPortaliQ28399.
    SMRiQ28399. Positions 8-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ28399.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    HOVERGENiHBG000097.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q28399-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC    50
    EVEEADKEDV DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR 100
    LLLATLESIN AGKVFASAYL MDLDYCIKAL RYCAGWADKI QGRTIPVDGE 150
    FFSYTRHEPI GVCGLIFPWN APMILLACKI GPALCCGNTV IVKPAEQTPL 200
    TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTEV 250
    GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG 300
    QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ 350
    HNKIMELIES GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE 400
    IFGPVQQIMK FKSLDEVIKR ANNTYYGLVA GVFTKDLDKA VTVSSALQAG 450
    TVWVNCYLAA SAQSPAGGFK MSGHGREMGE YGIHEYTEVK TVTMKISEKN 500
    S 501
    Length:501
    Mass (Da):54,538
    Last modified:November 1, 1996 - v1
    Checksum:i9E3D5BBE083ACAD7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02483 mRNA. Translation: AAB60268.1.
    RefSeqiNP_001277088.1. NM_001290159.1.

    Genome annotation databases

    GeneIDi102867337.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02483 mRNA. Translation: AAB60268.1 .
    RefSeqi NP_001277088.1. NM_001290159.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O9J X-ray 2.40 A/B/C/D 1-501 [» ]
    1PEJ model - A 1-501 [» ]
    ProteinModelPortali Q28399.
    SMRi Q28399. Positions 8-501.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q28399.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102867337.

    Organism-specific databases

    CTDi 102867337.

    Phylogenomic databases

    HOVERGENi HBG000097.

    Enzyme and pathway databases

    UniPathwayi UPA00780 ; UER00768 .
    BRENDAi 1.2.1.36. 7360.

    Miscellaneous databases

    EvolutionaryTracei Q28399.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin."
      Graham C., Hodin J., Wistow G.
      J. Biol. Chem. 271:15623-15628(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    2. "Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens."
      Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., Wistow G.
      Biochemistry 42:4349-4356(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, HOMOTETRAMERIZATION.

    Entry informationi

    Entry nameiALDH1_ELEED
    AccessioniPrimary (citable) accession number: Q28399
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3