NMRL1_BOVIN
ID NMRL1_BOVIN Reviewed; 299 AA.
AC Q0VCN1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=NmrA-like family domain-containing protein 1;
GN Name=NMRAL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Redox sensor protein. Undergoes restructuring and subcellular
CC redistribution in response to changes in intracellular NADPH/NADP(+)
CC levels. At low NADPH concentrations the protein is found mainly as a
CC monomer, and binds argininosuccinate synthase (ASS1), the enzyme
CC involved in nitric oxide synthesis. Association with ASS1 impairs its
CC activity and reduces the production of nitric oxide, which subsecuently
CC prevents apoptosis. Under normal NADPH concentrations, the protein is
CC found as a dimer and hides the binding site for ASS1. The homodimer
CC binds one molecule of NADPH. Has higher affinity for NADPH than for
CC NADP(+). Binding to NADPH is necessary to form a stable dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with ASS1. Interaction is enhanced by low
CC NADPH/NADP(+) ratios, which results in inhibition of ASS1 activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Nucleus. Note=Under normal redox growth conditions localizes in the
CC cytoplasm and perinuclear region. Nuclear localization is promoted by
CC increased intracellular nitric oxide and reduced NADPH/NADP(+) ratios
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Tyr residue in the active site triad of
CC Ser-Tyr-Lys necessary for dehydrogenase activity, suggesting that it
CC has no oxidoreductase activity. {ECO:0000305}.
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DR EMBL; BC120089; AAI20090.1; -; mRNA.
DR RefSeq; NP_001069500.1; NM_001076032.2.
DR RefSeq; XP_005224578.3; XM_005224521.3.
DR AlphaFoldDB; Q0VCN1; -.
DR SMR; Q0VCN1; -.
DR STRING; 9913.ENSBTAP00000013208; -.
DR PaxDb; Q0VCN1; -.
DR PeptideAtlas; Q0VCN1; -.
DR PRIDE; Q0VCN1; -.
DR Ensembl; ENSBTAT00000013208; ENSBTAP00000013208; ENSBTAG00000010015.
DR Ensembl; ENSBTAT00000069988; ENSBTAP00000065595; ENSBTAG00000010015.
DR GeneID; 534628; -.
DR KEGG; bta:534628; -.
DR CTD; 57407; -.
DR VEuPathDB; HostDB:ENSBTAG00000010015; -.
DR VGNC; VGNC:32134; NMRAL1.
DR eggNOG; ENOG502RG69; Eukaryota.
DR GeneTree; ENSGT00940000160872; -.
DR HOGENOM; CLU_007383_8_2_1; -.
DR InParanoid; Q0VCN1; -.
DR OMA; TPMDGMA; -.
DR OrthoDB; 707551at2759; -.
DR TreeFam; TF335532; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000010015; Expressed in digestive system secreted substance and 104 other tissues.
DR ExpressionAtlas; Q0VCN1; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NADP; Nucleus; Reference proteome.
FT CHAIN 1..299
FT /note="NmrA-like family domain-containing protein 1"
FT /id="PRO_0000278203"
FT REGION 153..189
FT /note="Interaction with ASS1"
FT /evidence="ECO:0000250"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 37..41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 58..59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 79..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 155..158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 33154 MW; 6A0CDCFB3A5CE904 CRC64;
MADKKLVVVF GATGAQGGSV ARTLLEDGTF RVRVVTRDPG QRAAKQLRLQ GAEVVQGDQD
DEASMELALS GAHATFIVTN YWENCSQEQE VKQGKLLADL AKRLGLRYVV YSGLENIKKL
TAGRLTVGHF DGKGEVEEYF RDIGVPMTSV RLPCYFENLL SYFLPQKAPD GRSYLLSLPM
GDVPIDGMSV ADLGPVVLSL LKTPEEYVGR NIGLSTCRHT VEEYAALLTK HTGKAVRDAK
TSPEDYEKLG FPGAQDLANM FRFYALKPDR NIELTLKLNP KARRLDQWLE QHKEDFAGL
