NIT1_RAT
ID NIT1_RAT Reviewed; 327 AA.
AC Q7TQ94; Q5PQK6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Deaminated glutathione amidase;
DE Short=dGSH amidase;
DE EC=3.5.1.128 {ECO:0000250|UniProtKB:Q8VDK1};
DE AltName: Full=Nitrilase homolog 1;
DE Flags: Precursor;
GN Name=Nit1; ORFNames=rCG_20134;
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] (ISOFORM 2).
RC STRAIN=Sprague-Dawley;
RA Minto A.W. Jr., Quigg R.J. Jr.;
RT "Nirilase 1 expression in acute mesangio-proliferative
RT glomerulonephritis.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of the amide bond in N-(4-
CC oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite
CC repair reaction to dispose of the harmful deaminated glutathione. Plays
CC a role in cell growth and apoptosis: loss of expression promotes cell
CC growth, resistance to DNA damage stress and increased incidence to
CC NMBA-induced tumors. Has tumor suppressor properties that enhances the
CC apoptotic responsiveness in cancer cells; this effect is additive to
CC the tumor suppressor activity of FHIT. It is also a negative regulator
CC of primary T-cells. {ECO:0000250|UniProtKB:Q8VDK1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(4-oxoglutaryl)-L-cysteinylglycine = 2-oxoglutarate +
CC L-cysteinylglycine; Xref=Rhea:RHEA:54532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:61694, ChEBI:CHEBI:138256;
CC EC=3.5.1.128; Evidence={ECO:0000250|UniProtKB:Q8VDK1};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000250|UniProtKB:Q8VDK1}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q8VDK1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TQ94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TQ94-2; Sequence=VSP_059159;
CC -!- MISCELLANEOUS: According to Rosetta Stone theory, the existence of a
CC fusion protein in one genome predicts that the separate polypeptides
CC expressed in other organisms function in the same cellular or
CC biochemical pathway. In Drosophila melanogaster and Caenorhabditis
CC elegans, NitFhit is a fusion protein composed of a C-terminal Fhit
CC domain and a domain related to plant and bacterial nitrilase.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
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DR EMBL; AY300752; AAP76395.1; -; mRNA.
DR EMBL; CH473985; EDL94640.1; -; Genomic_DNA.
DR EMBL; BC087146; AAH87146.1; -; mRNA.
DR RefSeq; NP_001076049.1; NM_001082580.1. [Q7TQ94-2]
DR RefSeq; NP_001292575.1; NM_001305646.1.
DR RefSeq; NP_001292576.1; NM_001305647.1. [Q7TQ94-2]
DR RefSeq; NP_872609.2; NM_182668.2. [Q7TQ94-1]
DR AlphaFoldDB; Q7TQ94; -.
DR SMR; Q7TQ94; -.
DR STRING; 10116.ENSRNOP00000005194; -.
DR jPOST; Q7TQ94; -.
DR PaxDb; Q7TQ94; -.
DR PeptideAtlas; Q7TQ94; -.
DR PRIDE; Q7TQ94; -.
DR Ensembl; ENSRNOT00000117822; ENSRNOP00000096370; ENSRNOG00000003881. [Q7TQ94-2]
DR GeneID; 289222; -.
DR KEGG; rno:289222; -.
DR CTD; 4817; -.
DR RGD; 727821; Nit1.
DR VEuPathDB; HostDB:ENSRNOG00000003881; -.
DR eggNOG; KOG0807; Eukaryota.
DR GeneTree; ENSGT00550000075099; -.
DR InParanoid; Q7TQ94; -.
DR OMA; MTCYDVR; -.
DR OrthoDB; 1154369at2759; -.
DR TreeFam; TF313080; -.
DR PRO; PR:Q7TQ94; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000003881; Expressed in kidney and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0110050; F:deaminated glutathione amidase activity; ISO:RGD.
DR GO; GO:0043605; P:cellular amide catabolic process; ISO:RGD.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..327
FT /note="Deaminated glutathione amidase"
FT /id="PRO_0000213253"
FT DOMAIN 47..299
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 162
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /id="VSP_059159"
FT CONFLICT 323
FT /note="L -> LG (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36094 MW; D86F81FFB3A015C5 CRC64;
MLGFITRPPH QLLSLLCTGY RLPQISVLCT QPRPRAMAES SSTSWELPLV AVCQVTSTPN
KQENFKTCAE LVQEATRLGA CLAFLPEAFD FIARNPAETL LLSEPLDGDL LGQYSQLARE
CGIWLSLGGF HERGQDWEQT QKIYNCHVLL NSKGSVVASY RKTHLCDVEI PGQGPMRESN
YTMPGYALEP PVKTPAGKVG LAICYDMRFP ELSLKLAQAG AEILTYPSAF GSVTGPAHWE
VLLRARAIES QCYVIAAAQC GRHHETRASY GHSMVVDPWG TVVASCSEGP GLCLARIDLH
FLQQMRQHLP VFQHRRPDLY GSLLPLS
