ASGL1_MOUSE
ID ASGL1_MOUSE Reviewed; 326 AA.
AC Q8C0M9; Q91WC8; Q9CVX3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 6-13; 103-120 AND 129-155, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-326.
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 May be involved in the production of L-aspartate, which can act as an
CC excitatory neurotransmitter in some brain regions. Is highly active
CC with L-Asp beta-methyl ester. Besides, has catalytic activity toward
CC beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-
CC L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala,
CC 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.
CC {ECO:0000250|UniProtKB:Q7L266}.
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. This heterodimer may then dimerize in turn, giving rise
CC to a heterotetramer. {ECO:0000250|UniProtKB:Q7L266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L266}.
CC Note=Midpiece of sperm tail. In retina localizes in photoreceptor inner
CC segment (PubMed:27106100). {ECO:0000250|UniProtKB:Q7L266,
CC ECO:0000269|PubMed:27106100}.
CC -!- TISSUE SPECIFICITY: High expression in the heart and brain while low to
CC minimal expression in the other tissues. In ocular tissues, high levels
CC is observed in the optic nerve and retina while relatively low levels
CC of expression are detected in the iris-ciliary body, lens or retinal
CC pigment epithelium. {ECO:0000269|PubMed:27106100}.
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 -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB24431.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25294.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK006147; BAB24431.1; ALT_FRAME; mRNA.
DR EMBL; AK010381; BAC25294.1; ALT_FRAME; mRNA.
DR EMBL; AK030209; BAC26844.1; -; mRNA.
DR EMBL; BC016106; AAH16106.1; ALT_INIT; mRNA.
DR CCDS; CCDS29566.1; -.
DR RefSeq; NP_079886.2; NM_025610.3.
DR AlphaFoldDB; Q8C0M9; -.
DR SMR; Q8C0M9; -.
DR BioGRID; 211529; 2.
DR IntAct; Q8C0M9; 3.
DR MINT; Q8C0M9; -.
DR STRING; 10090.ENSMUSP00000051709; -.
DR iPTMnet; Q8C0M9; -.
DR PhosphoSitePlus; Q8C0M9; -.
DR SwissPalm; Q8C0M9; -.
DR REPRODUCTION-2DPAGE; IPI00223875; -.
DR EPD; Q8C0M9; -.
DR MaxQB; Q8C0M9; -.
DR PaxDb; Q8C0M9; -.
DR PeptideAtlas; Q8C0M9; -.
DR PRIDE; Q8C0M9; -.
DR ProteomicsDB; 277257; -.
DR Antibodypedia; 14797; 273 antibodies from 33 providers.
DR DNASU; 66514; -.
DR Ensembl; ENSMUST00000049948; ENSMUSP00000051709; ENSMUSG00000024654.
DR GeneID; 66514; -.
DR KEGG; mmu:66514; -.
DR UCSC; uc008gon.1; mouse.
DR CTD; 80150; -.
DR MGI; MGI:1913764; Asrgl1.
DR VEuPathDB; HostDB:ENSMUSG00000024654; -.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q8C0M9; -.
DR OMA; ERPLDCM; -.
DR OrthoDB; 797598at2759; -.
DR PhylomeDB; Q8C0M9; -.
DR TreeFam; TF323960; -.
DR Reactome; R-MMU-8964208; Phenylalanine metabolism.
DR BioGRID-ORCS; 66514; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Asrgl1; mouse.
DR PRO; PR:Q8C0M9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C0M9; protein.
DR Bgee; ENSMUSG00000024654; Expressed in seminiferous tubule of testis and 252 other tissues.
DR Genevisible; Q8C0M9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA: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 1: Evidence at protein level;
KW Autocatalytic cleavage; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome.
FT CHAIN 1..184
FT /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT /id="PRO_0000420559"
FT CHAIN 185..326
FT /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT /id="PRO_0000420560"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 33950 MW; B5AC25922D9A1338 CRC64;
MACARGTVAP PVRASIDVSL VVVVHGGGAS NISANRKELV REGIARAATE GYKILKAGGS
AVDAVEGAVT VLENDPEFNA GYGSVLNVNG DIEMDASIMD GKDLSAGAVS AVRCIANPVK
LARLVMEKTP HCFLTGHGAE KFAEDMGIPQ VPVEKLITER TKKHLEKEKL EKGAQNADCP
KNSGTVGAVA LDCRGNLAYA TSTGGIVNKM VGRVGDSPCI GAGGYADNNL GAVSTTGHGE
SILKVNLARL ALFHVEQGKT VEEAAQLALD YMKSKLKGLG GLILVNKTGD WVAKWTSASM
PWAAVKNGKL QAGIDLCETR TRDLPC
