NmrA-like family domain-containing protein 1

Details

Name
NmrA-like family domain-containing protein 1
Synonyms
  • HSCARG
Gene Name
NMRAL1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0019564|NmrA-like family domain-containing protein 1
MVDKKLVVVFGGTGAQGGSVARTLLEDGTFKVRVVTRNPRKKAAKELRLQGAEVVQGDQD
DQVIMELALNGAYATFIVTNYWESCSQEQEVKQGKLLADLARRLGLHYVVYSGLENIKKL
TAGRLAAAHFDGKGEVEEYFRDIGVPMTSVRLPCYFENLLSHFLPQKAPDGKSYLLSLPT
GDVPMDGMSVSDLGPVVLSLLKMPEKYVGQNIGLSTCRHTAEEYAALLTKHTRKVVHDAK
MTPEDYEKLGFPGARDLANMFRFYALRPDRDIELTLRLNPKALTLDQWLEQHKGDFNLL
Number of residues
299
Molecular Weight
33344.14
Theoretical pI
7.63
GO Classification
Components
cytoplasm / nucleus / perinuclear region of cytoplasm
General Function
Not Available
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019565|NmrA-like family domain-containing protein 1 (NMRAL1)
ATGGTGGACAAGAAACTGGTGGTGGTTTTCGGAGGCACAGGTGCCCAGGGTGGCTCCGTG
GCCCGCACACTCCTGGAAGATGGGACATTCAAGGTTCGAGTGGTGACCCGAAACCCTAGG
AAGAAGGCAGCAAAGGAGCTGAGGCTGCAAGGTGCAGAAGTAGTGCAGGGAGACCAAGAT
GACCAGGTCATCATGGAGCTGGCCCTGAATGGGGCTTACGCCACCTTCATCGTGACCAAT
TACTGGGAGAGCTGCAGCCAGGAGCAGGAGGTCAAGCAGGGGAAGCTGCTCGCTGATCTG
GCCAGGCGCCTGGGCCTCCACTATGTGGTCTACAGCGGCCTGGAGAACATCAAGAAGCTG
ACGGCAGGGAGATTGGCCGCCGCGCACTTTGACGGCAAAGGGGAGGTGGAGGAATATTTC
CGGGACATTGGCGTTCCCATGACCAGTGTGCGGCTGCCCTGCTATTTTGAGAACCTCCTC
TCCCACTTCTTGCCCCAGAAAGCCCCAGACGGAAAGAGCTACTTGCTGAGCTTGCCCACA
GGTGACGTTCCCATGGATGGCATGTCCGTGTCTGACCTGGGTCCTGTGGTGCTCAGCCTT
TTGAAGATGCCAGAAAAATACGTCGGCCAGAACATCGGGCTGAGCACTTGCAGGCACACG
GCCGAGGAGTACGCTGCCCTGCTCACCAAGCACACCCGCAAGGTCGTGCACGATGCCAAG
ATGACTCCTGAGGACTACGAAAAGCTTGGCTTTCCCGGTGCCCGGGACCTGGCCAACATG
TTCCGTTTCTATGCCCTGAGACCCGACCGTGACATCGAGCTGACCCTGAGACTCAACCCC
AAGGCCCTGACGCTGGACCAGTGGCTGGAACAGCACAAAGGGGACTTCAACCTGCTGTGA
Chromosome Location
16
Locus
16p13.3
External Identifiers
ResourceLink
UniProtKB IDQ9HBL8
UniProtKB Entry NameNMRL1_HUMAN
GenBank Protein ID9963841
GenBank Gene IDAF225419
HGNC IDHGNC:24987
General References
  1. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [Article]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  3. Zhao Y, Zhang J, Li H, Li Y, Ren J, Luo M, Zheng X: An NADPH sensor protein (HSCARG) down-regulates nitric oxide synthesis by association with argininosuccinate synthetase and is essential for epithelial cell viability. J Biol Chem. 2008 Apr 18;283(16):11004-13. doi: 10.1074/jbc.M708697200. Epub 2008 Feb 8. [Article]
  4. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  5. Zheng X, Dai X, Zhao Y, Chen Q, Lu F, Yao D, Yu Q, Liu X, Zhang C, Gu X, Luo M: Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein. Proc Natl Acad Sci U S A. 2007 May 22;104(21):8809-14. Epub 2007 May 11. [Article]
  6. Dai X, Li Y, Meng G, Yao S, Zhao Y, Yu Q, Zhang J, Luo M, Zheng X: NADPH is an allosteric regulator of HSCARG. J Mol Biol. 2009 Apr 17;387(5):1277-85. doi: 10.1016/j.jmb.2009.02.049. Epub 2009 Feb 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB087842-(4-CHLORO-PHENYLAMINO)-NICOTINIC ACIDexperimentalunknownDetails