ID   NMRL1_RAT               Reviewed;         150 AA.
AC   P86172;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=NmrA-like family domain-containing protein 1 {ECO:0000250|UniProtKB:Q9HBL8};
DE   Flags: Fragments;
GN   Name=Nmral1 {ECO:0000250|UniProtKB:Q9HBL8};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=Wistar; TISSUE=Cerebellum;
RA   Maurya D.K., Bhargava P.;
RL   Submitted (DEC-2008) to UniProtKB.
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:0000255}.
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   AlphaFoldDB; P86172; -.
DR   SMR; P86172; -.
DR   jPOST; P86172; -.
DR   PRIDE; P86172; -.
DR   UCSC; RGD:1311451; rat.
DR   RGD; 1311451; Nmral1.
DR   InParanoid; P86172; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NADP; Nucleus; Reference proteome.
FT   CHAIN           <1..>150
FT                   /note="NmrA-like family domain-containing protein 1"
FT                   /id="PRO_0000365638"
FT   BINDING         7..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000305"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000305"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000305"
FT   NON_CONS        95..96
FT                   /evidence="ECO:0000305"
FT   NON_CONS        132..133
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         150
SQ   SEQUENCE   150 AA;  16901 MW;  2FA8F99233E2EF84 CRC64;
     KLVVVFGATG AQGGSVARTL LEDGTFRVRV VTRNPEQKLL ADLAKRLGLH YVVYSGLENI
     KKLAAGHFDG KGEVEEYFRK PEEYIGQNVG LSTCRTTPEE YEKLGFQGAQ DLANMFRFYA
     LKPDRNIDLT LRAQTLDQWL EQHKGDFAHL