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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)DescriptionActionsGraphical viewLength
    Binding sitei36NAD1 Publication1
    Binding sitei97NAD1 Publication1
    Binding sitei102NAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi16 – 17NAD1 Publication2

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi36D → R: Reduces enzyme activity and alters specificity, so that NADP can be used as cosubstrate. 1 Publication1
    Mutagenesisi124S → A: Reduces enzyme activity 500-fold. 1 Publication1
    Mutagenesisi145H → Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi157E → Q: No major effect on enzyme activity. 1 Publication1
    Mutagenesisi196N → D or Q: Abolishes enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001093222 – 319Lambda-crystallinAdd BLAST318

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCurated1
    Modified residuei3PhosphoserineBy similarity1
    Modified residuei111PhosphoserineBy similarity1

    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

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 12Combined sources5
    Helixi16 – 27Combined sources12
    Beta strandi32 – 35Combined sources4
    Helixi39 – 58Combined sources20
    Beta strandi64 – 66Combined sources3
    Helixi68 – 73Combined sources6
    Beta strandi75 – 78Combined sources4
    Helixi81 – 84Combined sources4
    Turni85 – 87Combined sources3
    Beta strandi88 – 93Combined sources6
    Helixi99 – 110Combined sources12
    Beta strandi115 – 121Combined sources7
    Helixi128 – 132Combined sources5
    Helixi138 – 140Combined sources3
    Beta strandi141 – 146Combined sources6
    Turni150 – 152Combined sources3
    Beta strandi155 – 160Combined sources6
    Helixi166 – 178Combined sources13
    Beta strandi182 – 185Combined sources4
    Turni191 – 194Combined sources4
    Helixi195 – 211Combined sources17
    Helixi217 – 225Combined sources9
    Helixi228 – 232Combined sources5
    Helixi237 – 243Combined sources7
    Turni244 – 246Combined sources3
    Helixi248 – 264Combined sources17
    Helixi274 – 287Combined sources14
    Helixi292 – 315Combined sources24

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ADOX-ray1.70A1-319[»]
    3ADPX-ray1.85A1-319[»]
    ProteinModelPortaliP14755.
    SMRiP14755.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti252C → S in AAA31207 (PubMed:3170592).Curated1
    Sequence conflicti288V → G in AAA31207 (PubMed:3170592).Curated1
    Sequence conflicti308R → RE in AAA31207 (PubMed:3170592).Curated1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ADOX-ray1.70A1-319[»]
    3ADPX-ray1.85A1-319[»]
    ProteinModelPortaliP14755.
    SMRiP14755.
    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...

    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: November 2, 2016
    This is version 112 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.