Tag | Content |
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CPLM ID | CPLM-004110 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutaminase kidney isoform, mitochondrial |
Protein Synonyms/Alias | GLS; K-glutaminase; L-glutamine amidohydrolase; Glutaminase kidney isoform 68 kDa chain; Glutaminase kidney isoform 65 kDa chain |
Gene Name | Gls |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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621 | CKVNPFPKDRWNNTP | 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 | Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. |
Sequence Annotation | REPEAT 590 619 ANK 1. REPEAT 624 653 ANK 2. BINDING 291 291 Substrate (By similarity). BINDING 340 340 Substrate (By similarity). BINDING 386 386 Substrate (By similarity). BINDING 393 393 Substrate (By similarity). BINDING 419 419 Substrate (By similarity). BINDING 471 471 Substrate (By similarity). BINDING 489 489 Substrate; via amide nitrogen (By MOD_RES 316 316 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Alternative splicing; ANK repeat; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Mitochondrion; Reference proteome; Repeat; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 674 AA |
Protein Sequence | MMRLRGSAML RELLLRPPAA VGGVLRRTQP LGTLCRRPRG GSRPAAGLVA AARLHPWWGG 60 GGRAKGPGSG GLSSSPSEIL QELGKGGTPP QQQQQQQQQP GASPPAAPGP KDSPGETDAF 120 GNSEGKEMVA AGDNKVKQGL LPSLEDLLFY TIAEGQEKIP VHKFITALKS TGLRTSDPRL 180 KECMDMLRLT LQTTSDGVML DKDLFKKCVQ SNIVLLTQAF RRKFVIPDFM SFTSHIDELY 240 ESAKKQSGGK VADYIPQLAK FSPDLWGVSV CTVDGQRHSI GDTKVPFCLQ SCVKPLKYAI 300 AVNDLGTEYV HRYVGKEPSG LRFNKLFLNE DDKPHNPMVN AGAIVVTSLI KQGVNNAEKF 360 DYVMQFLNKM AGNEYVGFSN ATFQSERESG DRNFAIGYYL KEKKCFPEGT DMVGILDFYF 420 QLCSIEVTCE SASVMAATLA NGGFCPITGE RVLSPEAVRN TLSLMHSCGM YDFSGQFAFH 480 VGLPAKSGVA GGILLVVPNV MGMMCWSPPL DKMGNSVKGI HFCHDLVSLC NFHNYDNLRH 540 FAKKLDPRRE GGDQRVKSVI NLLFAAYTGD VSALRRFALS AMDMEQRDYD SRTALHVAAA 600 EGHVEVVKFL LEACKVNPFP KDRWNNTPMD EALHFGHHDV FKILQEYQVQ YTPQGDSDDG 660 KENQTVHKNL DGLL 674 |
Gene Ontology | GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:RGD. GO:0004359; F:glutaminase activity; ISS:UniProtKB. GO:0006537; P:glutamate biosynthetic process; ISS:UniProtKB. GO:0006543; P:glutamine catabolic process; ISS:UniProtKB. GO:0051289; P:protein homotetramerization; ISS:UniProtKB. |
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Pfam | |
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PRINTS | |