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Protein

Lambda-crystallin

Gene

CRYL1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as crystallin in the rabbit eye lens. Has high L-gulonate 3-dehydrogenase activity.1 Publication

Catalytic activityi

L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH.

Enzyme regulationi

Inhibited by malonate and by inorganic phosphate.1 Publication

Kineticsi

  1. KM=0.011 mM for NAD1 Publication
  2. KM=0.0005 mM for NADH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361NAD1 Publication
    Binding sitei97 – 971NAD1 Publication
    Binding sitei102 – 1021NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 172NAD1 Publication

    GO - Molecular functioni

    • 3-hydroxyacyl-CoA dehydrogenase activity Source: InterPro
    • L-gulonate 3-dehydrogenase activity Source: UniProtKB
    • NAD+ binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • structural constituent of eye lens Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Eye lens protein, Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.1.1.45. 1749.
    SABIO-RKP14755.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lambda-crystallin (EC:1.1.1.45)
    Alternative name(s):
    L-gulonate 3-dehydrogenase
    Short name:
    Gul3DH
    Gene namesi
    Name:CRYL1
    Synonyms:GUL3DH
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    Proteomesi
    • UP000001811 Componenti: Unplaced

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361D → R: Reduces enzyme activity and alters specificity, so that NADP can be used as cosubstrate. 1 Publication
    Mutagenesisi124 – 1241S → A: Reduces enzyme activity 500-fold. 1 Publication
    Mutagenesisi145 – 1451H → Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi157 – 1571E → Q: No major effect on enzyme activity. 1 Publication
    Mutagenesisi196 – 1961N → D or Q: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved
    Chaini2 – 319318Lambda-crystallinPRO_0000109322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineCurated
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei111 – 1111PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Expressioni

    Tissue specificityi

    Detected in eye lens, kidney, liver, heart, lung, brain and testis.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000011580.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125Combined sources
    Helixi16 – 2712Combined sources
    Beta strandi32 – 354Combined sources
    Helixi39 – 5820Combined sources
    Beta strandi64 – 663Combined sources
    Helixi68 – 736Combined sources
    Beta strandi75 – 784Combined sources
    Helixi81 – 844Combined sources
    Turni85 – 873Combined sources
    Beta strandi88 – 936Combined sources
    Helixi99 – 11012Combined sources
    Beta strandi115 – 1217Combined sources
    Helixi128 – 1325Combined sources
    Helixi138 – 1403Combined sources
    Beta strandi141 – 1466Combined sources
    Turni150 – 1523Combined sources
    Beta strandi155 – 1606Combined sources
    Helixi166 – 17813Combined sources
    Beta strandi182 – 1854Combined sources
    Turni191 – 1944Combined sources
    Helixi195 – 21117Combined sources
    Helixi217 – 2259Combined sources
    Helixi228 – 2325Combined sources
    Helixi237 – 2437Combined sources
    Turni244 – 2463Combined sources
    Helixi248 – 26417Combined sources
    Helixi274 – 28714Combined sources
    Helixi292 – 31524Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ADOX-ray1.70A1-319[»]
    3ADPX-ray1.85A1-319[»]
    ProteinModelPortaliP14755.
    SMRiP14755. Positions 7-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14755.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG2305. Eukaryota.
    COG1250. LUCA.
    HOGENOMiHOG000141499.
    HOVERGENiHBG051126.
    InParanoidiP14755.
    KOiK13247.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14755-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASPAAGDVL IVGSGLVGRS WAMLFASGGF RVKLYDIEPR QITGALENIR
    60 70 80 90 100
    KEMKSLQQSG SLKGSLSAEE QLSLISSCTN LAEAVEGVVH IQECVPENLD
    110 120 130 140 150
    LKRKIFAQLD SIVDDRVVLS SSSSCLLPSK LFTGLAHVKQ CIVAHPVNPP
    160 170 180 190 200
    YYIPLVELVP HPETSPATVD RTHALMRKIG QSPVRVLKEI DGFVLNRLQY
    210 220 230 240 250
    AIISEAWRLV EEGIVSPSDL DLVMSDGLGM RYAFIGPLET MHLNAEGMLS
    260 270 280 290 300
    YCDRYSEGMK RVLKSFGSIP EFSGATVEKV NQAMCKKVPA DPEHLAARRE
    310
    WRDECLKRLA KLKRQMQPQ
    Length:319
    Mass (Da):35,202
    Last modified:September 22, 2009 - v3
    Checksum:iC6F66B558BA422F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti252 – 2521C → S in AAA31207 (PubMed:3170592).Curated
    Sequence conflicti288 – 2881V → G in AAA31207 (PubMed:3170592).Curated
    Sequence conflicti308 – 3081R → RE in AAA31207 (PubMed:3170592).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M22743 mRNA. Translation: AAA31207.1.
    AB359905 mRNA. Translation: BAF76380.1.
    PIRiA31992.
    RefSeqiNP_001075747.1. NM_001082278.1.
    UniGeneiOcu.1849.

    Genome annotation databases

    GeneIDi100009108.
    KEGGiocu:100009108.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M22743 mRNA. Translation: AAA31207.1.
    AB359905 mRNA. Translation: BAF76380.1.
    PIRiA31992.
    RefSeqiNP_001075747.1. NM_001082278.1.
    UniGeneiOcu.1849.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ADOX-ray1.70A1-319[»]
    3ADPX-ray1.85A1-319[»]
    ProteinModelPortaliP14755.
    SMRiP14755. Positions 7-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000011580.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi100009108.
    KEGGiocu:100009108.

    Organism-specific databases

    CTDi51084.

    Phylogenomic databases

    eggNOGiKOG2305. Eukaryota.
    COG1250. LUCA.
    HOGENOMiHOG000141499.
    HOVERGENiHBG051126.
    InParanoidiP14755.
    KOiK13247.

    Enzyme and pathway databases

    BRENDAi1.1.1.45. 1749.
    SABIO-RKP14755.

    Miscellaneous databases

    EvolutionaryTraceiP14755.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR022694. 3-OHacyl-CoA_DH.
    IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000105. HCDH. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases."
      Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H., de Jong W.W.
      J. Biol. Chem. 263:15462-15466(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Lens.
    2. "Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase."
      Ishikura S., Usami N., Araki M., Hara A.
      J. Biochem. 137:303-314(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-36; SER-124; HIS-145; GLU-157 AND ASN-196, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Liver.
    3. "Crystal structure of the rabbit L-gulonate 3-dehydrogenase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD.

    Entry informationi

    Entry nameiCRYL1_RABIT
    AccessioniPrimary (citable) accession number: P14755
    Secondary accession number(s): A7VMV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: September 22, 2009
    Last modified: December 9, 2015
    This is version 110 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.