ASGL1_DANRE
ID ASGL1_DANRE Reviewed; 310 AA.
AC Q5BKW9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5 {ECO:0000250|UniProtKB:Q7L266};
DE EC=3.5.1.1 {ECO:0000250|UniProtKB:Q7L266};
DE AltName: Full=Asparaginase-like protein 1;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Isoaspartyl dipeptidase;
DE AltName: Full=L-asparagine amidohydrolase;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase alpha chain;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase beta chain;
DE Flags: Precursor;
GN Name=asrgl1; ORFNames=zgc:103568;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=27106100; DOI=10.1093/hmg/ddw113;
RA Biswas P., Chavali V.R., Agnello G., Stone E., Chakarova C., Duncan J.L.,
RA Kannabiran C., Homsher M., Bhattacharya S.S., Naeem M.A., Kimchi A.,
RA Sharon D., Iwata T., Riazuddin S., Reddy G.B., Hejtmancik J.F.,
RA Georgiou G., Riazuddin S.A., Ayyagari R.;
RT "A missense mutation in ASRGL1 is involved in causing autosomal recessive
RT retinal degeneration.";
RL Hum. Mol. Genet. 25:2483-2497(2016).
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC Does not have aspartylglucosaminidase activity and is inactive toward
CC GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC {ECO:0000250|UniProtKB:Q7L266}.
CC -!- DISRUPTION PHENOTYPE: Abnormal and deformed fish at 6 dpf.
CC {ECO:0000269|PubMed:27106100}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; BC090901; AAH90901.1; -; mRNA.
DR RefSeq; NP_001013547.1; NM_001013529.1.
DR AlphaFoldDB; Q5BKW9; -.
DR SMR; Q5BKW9; -.
DR STRING; 7955.ENSDARP00000033788; -.
DR PaxDb; Q5BKW9; -.
DR Ensembl; ENSDART00000029521; ENSDARP00000033788; ENSDARG00000021681.
DR Ensembl; ENSDART00000159281; ENSDARP00000130414; ENSDARG00000021681.
DR GeneID; 541402; -.
DR KEGG; dre:541402; -.
DR CTD; 80150; -.
DR ZFIN; ZDB-GENE-050320-102; asrgl1.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q5BKW9; -.
DR OrthoDB; 797598at2759; -.
DR PhylomeDB; Q5BKW9; -.
DR TreeFam; TF323960; -.
DR Reactome; R-DRE-8964208; Phenylalanine metabolism.
DR PRO; PR:Q5BKW9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000021681; Expressed in intestine and 21 other tissues.
DR ExpressionAtlas; Q5BKW9; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; ISS:UniProtKB.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04702; ASRGL1_like; 1.
DR InterPro; IPR033844; ASRGL1_meta.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..166
FT /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT /id="PRO_0000420563"
FT CHAIN 167..310
FT /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT /id="PRO_0000420564"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 195..198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218..221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 32929 MW; 2CFE4C0E019CC3F9 CRC64;
MLPVVVVHGG AGHIPKERTE ESTIGVKEAA RTGYAILQRG GSAVDAVVEA VALMETNPRF
NAGRGSVLNI KGEVEMDALV MDGRTLDSGA VSAVRRIANP VQLARLVMEK TKHLCLTAEG
ASKFARSMGV PEVPEESLIT DYAKMRWKKN LEPDANPVEC QMGKMGTVGA VAVDMDGNIA
CATSTGGMIN KMEGRVGDTP CVGCGGYADN KIGAVSPTGH GEAIMKVTLS RLVLFHMEQG
KTPEEASDLA LAYMKERVDG LGGVVVVDHN GTWAARFSSL QMSWAAAQQG KLHFGLFHGD
HFTEPVEEHT
