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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

Asrgl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions.By similarity1 Publication

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.1 Publication
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.1 Publication

Kineticsi

  1. KM=2.4 mM for L-aspartic acid beta-(7-amido-4-methylcoumarin)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei191 – 1911NucleophileBy similarity

    GO - Molecular functioni

    • asparaginase activity Source: MGI
    • beta-aspartyl-peptidase activity Source: UniProtKB

    GO - Biological processi

    • asparagine catabolic process via L-aspartate Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    ReactomeiR-RNO-71182. Phenylalanine and tyrosine catabolism.
    SABIO-RKQ8VI04.

    Protein family/group databases

    MEROPSiT02.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.51 Publication, EC:3.5.1.11 Publication)
    Alternative name(s):
    Asparaginase-like protein 1
    Asparaginase-like sperm autoantigen
    Beta-aspartyl-peptidase
    Glial asparaginase
    Isoaspartyl dipeptidase
    L-asparagine amidohydrolase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Asrgl1
    Synonyms:Alp, Gliap, Hiob
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 1

    Organism-specific databases

    RGDi708526. Asrgl1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: RGD
    • nucleus Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Isoaspartyl peptidase/L-asparaginase alpha chainPRO_0000420561Add
    BLAST
    Chaini191 – 333143Isoaspartyl peptidase/L-asparaginase beta chainPRO_0000420562Add
    BLAST

    Post-translational modificationi

    Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.By similarity

    Keywords - PTMi

    Autocatalytic cleavage

    Proteomic databases

    PaxDbiQ8VI04.
    PRIDEiQ8VI04.

    PTM databases

    iPTMnetiQ8VI04.

    Expressioni

    Tissue specificityi

    Present in testis, brain, liver, kidney, heart and skeletal muscle. In brain, specifically present in the astrocytic lineage. Present in sperm (at protein level).2 Publications

    Gene expression databases

    GenevisibleiQ8VI04. RN.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity).By similarity

    Protein-protein interaction databases

    IntActiQ8VI04. 1 interaction.
    STRINGi10116.ENSRNOP00000027459.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VI04.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 2224Substrate bindingBy similarity
    Regioni242 – 2454Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the Ntn-hydrolase family.Curated

    Phylogenomic databases

    eggNOGiKOG1592. Eukaryota.
    COG1446. LUCA.
    GeneTreeiENSGT00530000063034.
    HOGENOMiHOG000174613.
    HOVERGENiHBG101662.
    InParanoidiQ8VI04.
    KOiK13051.
    OMAiDGNIACA.
    OrthoDBiEOG7TBC2N.
    PhylomeDBiQ8VI04.
    TreeFamiTF323960.

    Family and domain databases

    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view]
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiPF01112. Asparaginase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q8VI04-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATARPSSCG RDSVPATPRA SIDVSLVVVV HGGGASNISP GRKELVSEGI
    60 70 80 90 100
    AKAATEGYNI LKAGGSAVDA VEGAVTMLEN DPEFNAGYGS VLNADGDIEM
    110 120 130 140 150
    DASIMDGKDL SAGAVSAVRC IANPVKLARL VMEKTPHCFL TGRGAEKFAA
    160 170 180 190 200
    DMGIPQTPAE KLITERTKKH LEKEKLEKGA QKADCPKNSG TVGAVALDCK
    210 220 230 240 250
    GNLAYATSTG GIVNKMVGRV GDSPCIGAGG YADNNLGAVS TTGHGESILK
    260 270 280 290 300
    VNLARLALFH VEQGKTVDEA ATLALDYMKS KLKGLGGLIL INKTGDWVAK
    310 320 330
    WTSASMPWAA VKNGKLQAGI DLCETKTRNL PTC
    Length:333
    Mass (Da):34,410
    Last modified:March 1, 2002 - v1
    Checksum:iFD0BF38DAC6F905D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF329099 mRNA. Translation: AAL41029.1.
    AJ427914 mRNA. Translation: CAD20833.1.
    AJ427915 mRNA. Translation: CAD20834.1.
    RefSeqiNP_659557.1. NM_145089.4.
    UniGeneiRn.22774.

    Genome annotation databases

    EnsembliENSRNOT00000027459; ENSRNOP00000027459; ENSRNOG00000020202.
    GeneIDi246307.
    KEGGirno:246307.
    UCSCiRGD:708526. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF329099 mRNA. Translation: AAL41029.1.
    AJ427914 mRNA. Translation: CAD20833.1.
    AJ427915 mRNA. Translation: CAD20834.1.
    RefSeqiNP_659557.1. NM_145089.4.
    UniGeneiRn.22774.

    3D structure databases

    ProteinModelPortaliQ8VI04.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8VI04. 1 interaction.
    STRINGi10116.ENSRNOP00000027459.

    Protein family/group databases

    MEROPSiT02.002.

    PTM databases

    iPTMnetiQ8VI04.

    Proteomic databases

    PaxDbiQ8VI04.
    PRIDEiQ8VI04.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000027459; ENSRNOP00000027459; ENSRNOG00000020202.
    GeneIDi246307.
    KEGGirno:246307.
    UCSCiRGD:708526. rat.

    Organism-specific databases

    CTDi80150.
    RGDi708526. Asrgl1.

    Phylogenomic databases

    eggNOGiKOG1592. Eukaryota.
    COG1446. LUCA.
    GeneTreeiENSGT00530000063034.
    HOGENOMiHOG000174613.
    HOVERGENiHBG101662.
    InParanoidiQ8VI04.
    KOiK13051.
    OMAiDGNIACA.
    OrthoDBiEOG7TBC2N.
    PhylomeDBiQ8VI04.
    TreeFamiTF323960.

    Enzyme and pathway databases

    ReactomeiR-RNO-71182. Phenylalanine and tyrosine catabolism.
    SABIO-RKQ8VI04.

    Miscellaneous databases

    NextBioi623728.
    PROiQ8VI04.

    Gene expression databases

    GenevisibleiQ8VI04. RN.

    Family and domain databases

    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view]
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiPF01112. Asparaginase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "A novel asparaginase-like protein is a sperm autoantigen in rats."
      Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A., Flickinger C.J.
      Mol. Reprod. Dev. 62:233-247(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: Lewis.
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: Wistar.
      Tissue: Brain.

    Entry informationi

    Entry nameiASGL1_RAT
    AccessioniPrimary (citable) accession number: Q8VI04
    Secondary accession number(s): Q8CG44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: March 1, 2002
    Last modified: January 20, 2016
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In vasectomized rats, autoantibodies against Asrgl1 are present.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 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.