NRK2_MOUSE
ID NRK2_MOUSE Reviewed; 195 AA.
AC Q9D7C9; Q0VEG2; Q3UV96;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nicotinamide riboside kinase 2;
DE Short=NRK 2;
DE Short=NmR-K 2;
DE EC=2.7.1.22 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Integrin beta-1-binding protein 3;
DE AltName: Full=Muscle integrin-binding protein;
DE Short=MIBP;
DE AltName: Full=Nicotinic acid riboside kinase 2;
DE EC=2.7.1.173 {ECO:0000250|UniProtKB:Q9NWW6};
DE AltName: Full=Ribosylnicotinamide kinase 2;
DE Short=RNK 2;
DE AltName: Full=Ribosylnicotinic acid kinase 2;
GN Name=Nmrk2; Synonyms=Itgb1bp3, Nrk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
RA Li J., Mayne R., Wu C.;
RT "A novel muscle-specific beta 1 integrin binding protein (MIBP) that
RT modulates myogenic differentiation.";
RL J. Cell Biol. 147:1391-1398(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR)
CC and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide
CC (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix
CC deposition and cell adhesion to laminin, but not to fibronectin.
CC Involved in the regulation of PXN at the protein level and of PXN
CC tyrosine phosphorylation. May play a role in the regulation of terminal
CC myogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:10613898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide
CC D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q9NWW6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta-
CC D-ribonucleotide; Xref=Rhea:RHEA:25568, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57502, ChEBI:CHEBI:58527,
CC ChEBI:CHEBI:456216; EC=2.7.1.173;
CC Evidence={ECO:0000250|UniProtKB:Q9NWW6};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC {ECO:0000250|UniProtKB:Q9NWW6}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ITGB1 alone or when
CC associated with alpha-7, but not with alpha-5. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:10613898}.
CC -!- INDUCTION: Down-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:10613898}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK009352; BAB26235.1; -; mRNA.
DR EMBL; AK137483; BAE23375.1; -; mRNA.
DR EMBL; BC119244; AAI19245.1; -; mRNA.
DR EMBL; BC119246; AAI19247.1; -; mRNA.
DR CCDS; CCDS24046.1; -.
DR RefSeq; NP_081396.1; NM_027120.2.
DR AlphaFoldDB; Q9D7C9; -.
DR SMR; Q9D7C9; -.
DR BioGRID; 213534; 1.
DR STRING; 10090.ENSMUSP00000005069; -.
DR PhosphoSitePlus; Q9D7C9; -.
DR PaxDb; Q9D7C9; -.
DR PRIDE; Q9D7C9; -.
DR ProteomicsDB; 293734; -.
DR Antibodypedia; 23411; 107 antibodies from 20 providers.
DR DNASU; 69564; -.
DR Ensembl; ENSMUST00000005069; ENSMUSP00000005069; ENSMUSG00000004939.
DR GeneID; 69564; -.
DR KEGG; mmu:69564; -.
DR UCSC; uc007ggn.1; mouse.
DR CTD; 27231; -.
DR MGI; MGI:1916814; Nmrk2.
DR VEuPathDB; HostDB:ENSMUSG00000004939; -.
DR eggNOG; KOG3308; Eukaryota.
DR GeneTree; ENSGT00940000159842; -.
DR HOGENOM; CLU_058668_0_0_1; -.
DR InParanoid; Q9D7C9; -.
DR OMA; YQKYRRE; -.
DR OrthoDB; 1230625at2759; -.
DR PhylomeDB; Q9D7C9; -.
DR TreeFam; TF105395; -.
DR BRENDA; 2.7.1.22; 3474.
DR Reactome; R-MMU-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; -.
DR BioGRID-ORCS; 69564; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D7C9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D7C9; protein.
DR Bgee; ENSMUSG00000004939; Expressed in knee joint and 42 other tissues.
DR Genevisible; Q9D7C9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; ISO:MGI.
DR GO; GO:0061769; F:ribosylnicotinate kinase activity; ISO:MGI.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Nicotinamide riboside kinase 2"
FT /id="PRO_0000215895"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 35..38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 54..55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 134..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
FT BINDING 174..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NWW6"
SQ SEQUENCE 195 AA; 22375 MW; 83B0FB3F52738455 CRC64;
MKLIIGIGGV TNGGKTTLTN SLLKALPNCC VIHQDDFFKP QDQIAVGEDG FKQWDVLESL
DMETMLSTVQ AWVKDPHKFA RAHGVSLQSG ASDTHVLLLE GFLLYSYRPL VDLYSQRYFL
TVPYEECKRR RRSRTYMVPD PPGLFDGHVW PMYQKYRREM EQDGVEVVYL DGMKSPEGLF
HQVLEDIQNR LLNTS
