ASGL1_RAT
ID ASGL1_RAT Reviewed; 333 AA.
AC Q8VI04; Q8CG44;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5 {ECO:0000269|PubMed:12753071};
DE EC=3.5.1.1 {ECO:0000269|PubMed:12753071};
DE AltName: Full=Asparaginase-like protein 1;
DE AltName: Full=Asparaginase-like sperm autoantigen;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Glial asparaginase;
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; Synonyms=Alp, Gliap, Hiob;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Lewis; TISSUE=Testis;
RX PubMed=11984834; DOI=10.1002/mrd.10092;
RA Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A.,
RA Flickinger C.J.;
RT "A novel asparaginase-like protein is a sperm autoantigen in rats.";
RL Mol. Reprod. Dev. 62:233-247(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=12753071; DOI=10.1046/j.1471-4159.2003.01766.x;
RA Dieterich D.C., Landwehr M., Reissner C., Smalla K.-H., Richter K.,
RA Wolf G., Boeckers T.M., Gundelfinger E.D., Kreutz M.R.;
RT "Gliap -- a novel untypical L-asparaginase localized to rat brain
RT astrocytes.";
RL J. Neurochem. 85:1117-1125(2003).
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC Is highly active with L-Asp beta-methyl ester. Besides, has catalytic
CC activity toward beta-aspartyl dipeptides and their methyl esters,
CC including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame),
CC beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have
CC aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn.
CC Likewise, has no activity toward glutamine (By similarity). May be
CC involved in the production of L-aspartate, which can act as an
CC excitatory neurotransmitter in some brain regions.
CC {ECO:0000250|UniProtKB:Q7L266, ECO:0000269|PubMed:12753071}.
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:0000269|PubMed:12753071};
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:0000269|PubMed:12753071};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for L-aspartic acid beta-(7-amido-4-methylcoumarin)
CC {ECO:0000269|PubMed:12753071};
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. This heterodimer may then dimerize in turn, giving rise
CC to a heterotetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11984834,
CC ECO:0000269|PubMed:12753071}. Note=Midpiece of sperm tail.
CC -!- TISSUE SPECIFICITY: Present in testis, brain, liver, kidney, heart and
CC skeletal muscle. In brain, specifically present in the astrocytic
CC lineage. Present in sperm (at protein level).
CC {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:12753071}.
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 -!- MISCELLANEOUS: In vasectomized rats, autoantibodies against Asrgl1 are
CC present.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AF329099; AAL41029.1; -; mRNA.
DR EMBL; AJ427914; CAD20833.1; -; mRNA.
DR EMBL; AJ427915; CAD20834.1; -; mRNA.
DR RefSeq; NP_659557.1; NM_145089.4.
DR AlphaFoldDB; Q8VI04; -.
DR SMR; Q8VI04; -.
DR BioGRID; 251586; 2.
DR IntAct; Q8VI04; 2.
DR STRING; 10116.ENSRNOP00000027459; -.
DR iPTMnet; Q8VI04; -.
DR PhosphoSitePlus; Q8VI04; -.
DR SwissPalm; Q8VI04; -.
DR jPOST; Q8VI04; -.
DR PaxDb; Q8VI04; -.
DR PRIDE; Q8VI04; -.
DR GeneID; 246307; -.
DR KEGG; rno:246307; -.
DR UCSC; RGD:708526; rat.
DR CTD; 80150; -.
DR RGD; 708526; Asrgl1.
DR VEuPathDB; HostDB:ENSRNOG00000020202; -.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q8VI04; -.
DR OMA; ERPLDCM; -.
DR OrthoDB; 797598at2759; -.
DR PhylomeDB; Q8VI04; -.
DR TreeFam; TF323960; -.
DR Reactome; R-RNO-8964208; Phenylalanine metabolism.
DR SABIO-RK; Q8VI04; -.
DR PRO; PR:Q8VI04; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020202; Expressed in testis and 19 other tissues.
DR Genevisible; Q8VI04; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; IDA:MGI.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; IDA: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 1: Evidence at protein level;
KW Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..190
FT /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT /id="PRO_0000420561"
FT CHAIN 191..333
FT /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT /id="PRO_0000420562"
FT ACT_SITE 191
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 219..222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242..245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 34410 MW; FD0BF38DAC6F905D CRC64;
MATARPSSCG RDSVPATPRA SIDVSLVVVV HGGGASNISP GRKELVSEGI AKAATEGYNI
LKAGGSAVDA VEGAVTMLEN DPEFNAGYGS VLNADGDIEM DASIMDGKDL SAGAVSAVRC
IANPVKLARL VMEKTPHCFL TGRGAEKFAA DMGIPQTPAE KLITERTKKH LEKEKLEKGA
QKADCPKNSG TVGAVALDCK GNLAYATSTG GIVNKMVGRV GDSPCIGAGG YADNNLGAVS
TTGHGESILK VNLARLALFH VEQGKTVDEA ATLALDYMKS KLKGLGGLIL INKTGDWVAK
WTSASMPWAA VKNGKLQAGI DLCETKTRNL PTC
