Tag | Content |
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CPLM ID | CPLM-018220 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Isoaspartyl peptidase/L-asparaginase |
Protein Synonyms/Alias | Asparaginase-like protein 1; Asparaginase-like sperm autoantigen; Beta-aspartyl-peptidase; Glial asparaginase; Isoaspartyl dipeptidase; L-asparagine amidohydrolase; Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain |
Gene Name | Asrgl1 |
Gene Synonyms/Alias | Alp; Gliap; Hiob |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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52 | LVSEGIAKAATEGYN | acetylation | [1] | 134 | LARLVMEKTPHCFLT | acetylation | [1] | 147 | LTGRGAEKFAADMGI | acetylation | [1] | 161 | IPQTPAEKLITERTK | acetylation | [1] | 173 | RTKKHLEKEKLEKGA | acetylation | [1] | 187 | AQKADCPKNSGTVGA | acetylation | [1] | 279 | TLALDYMKSKLKGLG | acetylation | [1] | 283 | DYMKSKLKGLGGLIL | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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. |
Sequence Annotation | REGION 219 222 Substrate binding (By similarity). REGION 242 245 Substrate binding (By similarity). ACT_SITE 191 191 Nucleophile (By similarity). |
Keyword | Autocatalytic cleavage; Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 333 AA |
Protein Sequence | MATARPSSCG RDSVPATPRA SIDVSLVVVV HGGGASNISP GRKELVSEGI AKAATEGYNI 60 LKAGGSAVDA VEGAVTMLEN DPEFNAGYGS VLNADGDIEM DASIMDGKDL SAGAVSAVRC 120 IANPVKLARL VMEKTPHCFL TGRGAEKFAA DMGIPQTPAE KLITERTKKH LEKEKLEKGA 180 QKADCPKNSG TVGAVALDCK GNLAYATSTG GIVNKMVGRV GDSPCIGAGG YADNNLGAVS 240 TTGHGESILK VNLARLALFH VEQGKTVDEA ATLALDYMKS KLKGLGGLIL INKTGDWVAK 300 WTSASMPWAA VKNGKLQAGI DLCETKTRNL PTC 333 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:MGI. GO:0015630; C:microtubule cytoskeleton; IEA:Compara. GO:0005634; C:nucleus; IEA:Compara. GO:0004067; F:asparaginase activity; IDA:MGI. GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB. GO:0033345; P:asparagine catabolic process via L-aspartate; IDA:UniProtKB. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
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PROSITE | |
PRINTS | |