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Protein

NmrA-like family domain-containing protein 1

Gene

Nmral1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP+ levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP+. Binding to NADPH is necessary to form a stable dimer (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei102 – 1021NADP; shared with dimeric partnerBy similarity
Binding sitei143 – 1431NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 166NADPBy similarity
Nucleotide bindingi37 – 415NADPBy similarity
Nucleotide bindingi58 – 592NADPBy similarity
Nucleotide bindingi79 – 813NADPBy similarity
Nucleotide bindingi165 – 1684NADPBy similarity

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NmrA-like family domain-containing protein 1
Gene namesi
Name:Nmral1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1915074. Nmral1.

Subcellular locationi

  • Cytoplasm
  • Cytoplasmperinuclear region
  • Nucleus

  • Note: Under normal redox growth conditions localizes in the cytoplasm and perinuclear region. Nuclear localization is promoted by increased intracellular nitric oxide and reduced NADPH/NADP+ ratios (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309NmrA-like family domain-containing protein 1PRO_0000278205Add
BLAST

Proteomic databases

EPDiQ8K2T1.
MaxQBiQ8K2T1.
PaxDbiQ8K2T1.
PRIDEiQ8K2T1.

2D gel databases

REPRODUCTION-2DPAGEIPI00169979.
Q8K2T1.
UCD-2DPAGEQ8K2T1.

PTM databases

iPTMnetiQ8K2T1.
PhosphoSiteiQ8K2T1.

Expressioni

Gene expression databases

BgeeiQ8K2T1.
CleanExiMM_NMRAL1.
ExpressionAtlasiQ8K2T1. baseline and differential.
GenevisibleiQ8K2T1. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with ASS1. Interaction is enhanced by low NADPH/NADP+ ratios, which results in inhibition of ASS1 activity (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8K2T1. 1 interaction.
STRINGi10090.ENSMUSP00000078132.

Structurei

3D structure databases

ProteinModelPortaliQ8K2T1.
SMRiQ8K2T1. Positions 3-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 19937Interaction with ASS1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the NmrA-type oxidoreductase family.Curated

Phylogenomic databases

eggNOGiENOG410IVQ5. Eukaryota.
COG0702. LUCA.
GeneTreeiENSGT00390000016395.
HOGENOMiHOG000035269.
HOVERGENiHBG082032.
InParanoidiQ8K2T1.
OMAiAVFSVQM.
PhylomeDBiQ8K2T1.
TreeFamiTF335532.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K2T1-1) [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
MADRKLVVVF GATGAQGGSV ARALLEDGTF RIRVVTRNPE QRAAKELKQQ
60 70 80 90 100
GAEVVRGDQD DAASMELALA GAHATFIVTN YWETCSQDRE VQQPHQWDQV
110 120 130 140 150
FKQGKLLADL AKRLGLHYVV YSGLENIRKL TAGKLAAGHF DGKGEVEEYF
160 170 180 190 200
RDIGVPMTSV RLPCYFENLL SYFLPQKAAD GKSFLLDLPM GDVPMDGMSV
210 220 230 240 250
SDLGPVVLSL LKKPEEYVGQ NIGLSTCRHT AEEYAALLSK HTGKAVHHAK
260 270 280 290 300
TTPEDYEKLG FQGAQDLANM FRFYTLKPDR NIHLTLRLNP KAQTLDQWLE

QHKGDFAQL
Length:309
Mass (Da):34,376
Last modified:October 1, 2002 - v1
Checksum:i0DA109085DF25142
GO
Isoform 2 (identifier: Q8K2T1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-102: Missing.
     251-253: TTP → PVH
     254-309: Missing.

Show »
Length:243
Mass (Da):26,469
Checksum:i57E42C3BC587BC2F
GO
Isoform 3 (identifier: Q8K2T1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-102: Missing.
     188-192: LPMGD → RLAHG
     193-309: Missing.

Show »
Length:182
Mass (Da):19,960
Checksum:iE70622DF9C0B2FAA
GO

Sequence cautioni

The sequence BAB28172.1 differs from that shown. Reason: Frameshift at position 178. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881L → M in BAB28172 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 10210Missing in isoform 2 and isoform 3. 1 PublicationVSP_023151
Alternative sequencei188 – 1925LPMGD → RLAHG in isoform 3. 1 PublicationVSP_027873
Alternative sequencei193 – 309117Missing in isoform 3. 1 PublicationVSP_027874Add
BLAST
Alternative sequencei251 – 2533TTP → PVH in isoform 2. 1 PublicationVSP_023153
Alternative sequencei254 – 30956Missing in isoform 2. 1 PublicationVSP_023154Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012340 mRNA. Translation: BAB28172.1. Frameshift.
AK078389 mRNA. Translation: BAC37249.1.
BC030039 mRNA. Translation: AAH30039.1.
CCDSiCCDS27923.1. [Q8K2T1-1]
CCDS70680.1. [Q8K2T1-2]
RefSeqiNP_001277690.1. NM_001290761.1.
NP_001277691.1. NM_001290762.1.
NP_001277692.1. NM_001290763.1. [Q8K2T1-2]
NP_080669.1. NM_026393.2. [Q8K2T1-1]
UniGeneiMm.28451.
Mm.372705.

Genome annotation databases

EnsembliENSMUST00000074970; ENSMUSP00000074500; ENSMUSG00000063445. [Q8K2T1-2]
ENSMUST00000079130; ENSMUSP00000078132; ENSMUSG00000063445. [Q8K2T1-1]
GeneIDi67824.
KEGGimmu:67824.
UCSCiuc007yae.2. mouse. [Q8K2T1-1]
uc056zav.1. mouse. [Q8K2T1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012340 mRNA. Translation: BAB28172.1. Frameshift.
AK078389 mRNA. Translation: BAC37249.1.
BC030039 mRNA. Translation: AAH30039.1.
CCDSiCCDS27923.1. [Q8K2T1-1]
CCDS70680.1. [Q8K2T1-2]
RefSeqiNP_001277690.1. NM_001290761.1.
NP_001277691.1. NM_001290762.1.
NP_001277692.1. NM_001290763.1. [Q8K2T1-2]
NP_080669.1. NM_026393.2. [Q8K2T1-1]
UniGeneiMm.28451.
Mm.372705.

3D structure databases

ProteinModelPortaliQ8K2T1.
SMRiQ8K2T1. Positions 3-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K2T1. 1 interaction.
STRINGi10090.ENSMUSP00000078132.

PTM databases

iPTMnetiQ8K2T1.
PhosphoSiteiQ8K2T1.

2D gel databases

REPRODUCTION-2DPAGEIPI00169979.
Q8K2T1.
UCD-2DPAGEQ8K2T1.

Proteomic databases

EPDiQ8K2T1.
MaxQBiQ8K2T1.
PaxDbiQ8K2T1.
PRIDEiQ8K2T1.

Protocols and materials databases

DNASUi67824.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074970; ENSMUSP00000074500; ENSMUSG00000063445. [Q8K2T1-2]
ENSMUST00000079130; ENSMUSP00000078132; ENSMUSG00000063445. [Q8K2T1-1]
GeneIDi67824.
KEGGimmu:67824.
UCSCiuc007yae.2. mouse. [Q8K2T1-1]
uc056zav.1. mouse. [Q8K2T1-2]

Organism-specific databases

CTDi57407.
MGIiMGI:1915074. Nmral1.

Phylogenomic databases

eggNOGiENOG410IVQ5. Eukaryota.
COG0702. LUCA.
GeneTreeiENSGT00390000016395.
HOGENOMiHOG000035269.
HOVERGENiHBG082032.
InParanoidiQ8K2T1.
OMAiAVFSVQM.
PhylomeDBiQ8K2T1.
TreeFamiTF335532.

Miscellaneous databases

ChiTaRSiNmral1. mouse.
NextBioi325637.
PROiQ8K2T1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2T1.
CleanExiMM_NMRAL1.
ExpressionAtlasiQ8K2T1. baseline and differential.
GenevisibleiQ8K2T1. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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).
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-22 AND 114-128, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNMRL1_MOUSE
AccessioniPrimary (citable) accession number: Q8K2T1
Secondary accession number(s): Q8BVF0, Q9CZP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 1, 2002
Last modified: March 16, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Lacks the conserved Tyr residue in the active site triad of Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it has no oxidoreductase activity.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.