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Protein

Nitrilase homolog 1

Gene

Nit1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in cell growth and apoptosis: loss of expression promotes cell growth, resistance to DNA damage stress and increased incidence to NMBA-induced tumors. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. Has apparently no omega-amidase activity such as NIT2.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821Proton acceptorPROSITE-ProRule annotation
Active sitei157 – 1571Proton donorPROSITE-ProRule annotation
Active sitei199 – 1991NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrilase homolog 1 (EC:3.5.-.-)
Gene namesi
Name:Nit1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1350916. Nit1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Mice are normal at birth as well as during growth. Mammary glands exhibit an increase in ductal and alveolar structures as well as more cyclin-D1 positive cells in mid-pregnancy. In the basal layer of epidermis, the number of cyclin-D1 positive cells is also higher. No lymphoid malignancy is observed. Kidney cells lacking Nit1 exhibit round and compact shapes, loss of lobular structure, higher cell density with increased S and G2/M cell populations. Cyclin D1 expression is increased, whereas differences in the other cell cycle-associated proteins appeared minimal. T-cells lacking NIT-1 display enhanced proliferation, elevated activation marker expression, accelerated cell cycle progression and aberrant expression of some cell cycle proteins.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Nitrilase homolog 1PRO_0000213252Add
BLAST

Proteomic databases

EPDiQ8VDK1.
MaxQBiQ8VDK1.
PaxDbiQ8VDK1.
PeptideAtlasiQ8VDK1.
PRIDEiQ8VDK1.

PTM databases

iPTMnetiQ8VDK1.
PhosphoSiteiQ8VDK1.

Expressioni

Tissue specificityi

Expressed in most tissues with higher expression in adult liver and kidney as well as in fetal adrenal gland and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ8VDK1.
CleanExiMM_NIT1.
ExpressionAtlasiQ8VDK1. baseline and differential.
GenevisibleiQ8VDK1. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8VDK1. 1 interaction.
MINTiMINT-4130913.
STRINGi10090.ENSMUSP00000106926.

Structurei

3D structure databases

ProteinModelPortaliQ8VDK1.
SMRiQ8VDK1. Positions 44-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 316274CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0807. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000075099.
HOGENOMiHOG000222700.
HOVERGENiHBG052628.
InParanoidiQ8VDK1.
OMAiMCESNST.
TreeFamiTF313080.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR001110. UPF0012_CS.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
PS01227. UPF0012. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VDK1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLGFITRPPH QLLCTGYRLL RTPVLCTQPR PRTMSSSTSW ELPLVAVCQV
60 70 80 90 100
TSTPNKQENF KTCAELVQEA ARLGACLAFL PEAFDFIARN PAETLLLSEP
110 120 130 140 150
LNGDLLGQYS QLARECGIWL SLGGFHERGQ DWEQNQKIYN CHVLLNSKGS
160 170 180 190 200
VVASYRKTHL CDVEIPGQGP MRESNYTKPG GTLEPPVKTP AGKVGLAICY
210 220 230 240 250
DMRFPELSLK LAQAGAEILT YPSAFGSVTG PAHWEVLLRA RAIESQCYVI
260 270 280 290 300
AAAQCGRHHE TRASYGHSMV VDPWGTVVAR CSEGPGLCLA RIDLHFLQQM
310 320
RQHLPVFQHR RPDLYGSLGH PLS
Length:323
Mass (Da):35,705
Last modified:July 27, 2011 - v2
Checksum:iF8CD7730713665EF
GO
Isoform 2 (identifier: Q8VDK1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Show »
Length:290
Mass (Da):31,886
Checksum:i34493DBFF2170C71
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221T → I in AAC40184 (PubMed:9671749).Curated
Sequence conflicti222 – 2221P → S in AAH21634 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2. CuratedVSP_011548Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069985 Genomic DNA. Translation: AAC40184.1.
AF069988 mRNA. Translation: AAC40185.1.
BC021634 mRNA. Translation: AAH21634.1.
CCDSiCCDS35775.1. [Q8VDK1-1]
CCDS56656.1. [Q8VDK1-2]
RefSeqiNP_001229509.1. NM_001242580.1. [Q8VDK1-2]
NP_036179.1. NM_012049.2. [Q8VDK1-1]
XP_006496929.1. XM_006496866.2. [Q8VDK1-2]
UniGeneiMm.12915.
Mm.270139.
Mm.440362.

Genome annotation databases

EnsembliENSMUST00000111289; ENSMUSP00000106920; ENSMUSG00000013997. [Q8VDK1-2]
ENSMUST00000111295; ENSMUSP00000106926; ENSMUSG00000013997. [Q8VDK1-1]
GeneIDi27045.
KEGGimmu:27045.
UCSCiuc007doa.2. mouse. [Q8VDK1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069985 Genomic DNA. Translation: AAC40184.1.
AF069988 mRNA. Translation: AAC40185.1.
BC021634 mRNA. Translation: AAH21634.1.
CCDSiCCDS35775.1. [Q8VDK1-1]
CCDS56656.1. [Q8VDK1-2]
RefSeqiNP_001229509.1. NM_001242580.1. [Q8VDK1-2]
NP_036179.1. NM_012049.2. [Q8VDK1-1]
XP_006496929.1. XM_006496866.2. [Q8VDK1-2]
UniGeneiMm.12915.
Mm.270139.
Mm.440362.

3D structure databases

ProteinModelPortaliQ8VDK1.
SMRiQ8VDK1. Positions 44-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VDK1. 1 interaction.
MINTiMINT-4130913.
STRINGi10090.ENSMUSP00000106926.

PTM databases

iPTMnetiQ8VDK1.
PhosphoSiteiQ8VDK1.

Proteomic databases

EPDiQ8VDK1.
MaxQBiQ8VDK1.
PaxDbiQ8VDK1.
PeptideAtlasiQ8VDK1.
PRIDEiQ8VDK1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111289; ENSMUSP00000106920; ENSMUSG00000013997. [Q8VDK1-2]
ENSMUST00000111295; ENSMUSP00000106926; ENSMUSG00000013997. [Q8VDK1-1]
GeneIDi27045.
KEGGimmu:27045.
UCSCiuc007doa.2. mouse. [Q8VDK1-1]

Organism-specific databases

CTDi4817.
MGIiMGI:1350916. Nit1.

Phylogenomic databases

eggNOGiKOG0807. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000075099.
HOGENOMiHOG000222700.
HOVERGENiHBG052628.
InParanoidiQ8VDK1.
OMAiMCESNST.
TreeFamiTF313080.

Miscellaneous databases

PROiQ8VDK1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VDK1.
CleanExiMM_NIT1.
ExpressionAtlasiQ8VDK1. baseline and differential.
GenevisibleiQ8VDK1. MM.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
IPR001110. UPF0012_CS.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
PS01227. UPF0012. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans."
    Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y., Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K., Buchberg A.M., Mazo A., Brenner C., Croce C.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  3. "Biological functions of mammalian Nit1, the counterpart of the invertebrate NitFhit Rosetta stone protein, a possible tumor suppressor."
    Semba S., Han S.-Y., Qin H.R., McCorkell K.A., Iliopoulos D., Pekarsky Y., Druck T., Trapasso F., Croce C.M., Huebner K.
    J. Biol. Chem. 281:28244-28253(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  4. "Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2."
    Jaisson S., Veiga-da-Cunha M., Van Schaftingen E.
    Biochimie 91:1066-1071(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination."
    Krasnikov B.F., Chien C.-H., Nostramo R., Pinto J.T., Nieves E., Callaway M., Sun J., Huebner K., Cooper A.J.L.
    Biochimie 91:1072-1080(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Mammalian nitrilase 1 homologue Nit1 is a negative regulator in T cells."
    Zhang H., Hou Y.-J., Han S.-Y., Zhang E.C., Huebner K., Zhang J.
    Int. Immunol. 21:691-703(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNIT1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDK1
Secondary accession number(s): O88526, Q9R1N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

According to Rosetta Stone theory, the existence of a fusion protein in one genome predicts that the separate polypeptides expressed in other organisms function in the same cellular or biochemical pathway. In Drosophila melanogaster and Caenorhabditis elegans, NitFhit is a fusion protein composed of a C-terminal Fhit domain and a domain related to plant and bacterial nitrilase.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.