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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

ASRGL1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. 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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-BTA-71182. Phenylalanine and tyrosine catabolism.

Protein family/group databases

MEROPSiT02.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5By similarity, EC:3.5.1.1By similarity)
Alternative name(s):
Asparaginase-like protein 1
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase
L-asparagine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:ASRGL1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 29

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Midpiece of sperm tail.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Isoaspartyl peptidase/L-asparaginase alpha chainPRO_0000420554Add
BLAST
Chaini168 – 308141Isoaspartyl peptidase/L-asparaginase beta chainPRO_0000420555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

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

Acetylation, Autocatalytic cleavage

Proteomic databases

PaxDbiQ32LE5.
PRIDEiQ32LE5.

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009073.

Structurei

3D structure databases

ProteinModelPortaliQ32LE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 1994Substrate bindingBy similarity
Regioni219 – 2224Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174613.
HOVERGENiHBG101662.
InParanoidiQ32LE5.
KOiK13051.
OMAiDVCARMA.
OrthoDBiEOG7TBC2N.
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.

Q32LE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPVVVVHGG GASNISKDRK ERVRQGILRA ATVGYNILKQ GGSAVDAVEG
60 70 80 90 100
AVTVLEDDPD FNAGCGSVLN ENGEVEMDAS IMNGKDLSAG AVSAVRCIAN
110 120 130 140 150
PIKLARLVMD KTPHCFLTDQ GAARFAAANG IPTIPGQQLV TERSRKRLEK
160 170 180 190 200
EKLEKDAQKP DCQKNLGTVG AVALDCQGNL AYATSTGGIV NKMPGRVGDT
210 220 230 240 250
PCVGSGGYAD NDIGAVSTTG HGESILKVNL ARLALFHVEQ GKSLEEAANA
260 270 280 290 300
SLGHMKSKVK GVGGIIMVNK AGEWAVKWTS TSMPWAAAKD GKLHSGIDFG

DTSIIDLS
Length:308
Mass (Da):32,050
Last modified:December 6, 2005 - v1
Checksum:iF17066092C340EE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109621 mRNA. Translation: AAI09622.1.
RefSeqiNP_001070503.1. NM_001077035.2.
UniGeneiBt.685.

Genome annotation databases

EnsembliENSBTAT00000009073; ENSBTAP00000009073; ENSBTAG00000006910.
GeneIDi767970.
KEGGibta:767970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109621 mRNA. Translation: AAI09622.1.
RefSeqiNP_001070503.1. NM_001077035.2.
UniGeneiBt.685.

3D structure databases

ProteinModelPortaliQ32LE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009073.

Protein family/group databases

MEROPSiT02.002.

Proteomic databases

PaxDbiQ32LE5.
PRIDEiQ32LE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009073; ENSBTAP00000009073; ENSBTAG00000006910.
GeneIDi767970.
KEGGibta:767970.

Organism-specific databases

CTDi80150.

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174613.
HOVERGENiHBG101662.
InParanoidiQ32LE5.
KOiK13051.
OMAiDVCARMA.
OrthoDBiEOG7TBC2N.
TreeFamiTF323960.

Enzyme and pathway databases

ReactomeiR-BTA-71182. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

NextBioi20918325.

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.

Entry informationi

Entry nameiASGL1_BOVIN
AccessioniPrimary (citable) accession number: Q32LE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 71 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

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.