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Nicotinamide riboside kinase 2 (NRK 2) (NmR-K 2) (EC 2.7.1.22) (Integrin beta-1-binding protein 3) (Muscle integrin-binding protein) (MIBP) (Nicotinic acid riboside kinase 2) (EC 2.7.1.173) (Ribosylnicotinamide kinase 2) (RNK 2) (Ribosylnicotinic acid kinase 2)

 NRK2_MOUSE              Reviewed;         195 AA.
Q9D7C9; Q0VEG2; Q3UV96;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
07-JUN-2017, entry version 101.
RecName: Full=Nicotinamide riboside kinase 2;
Short=NRK 2;
Short=NmR-K 2;
EC=2.7.1.22 {ECO:0000250|UniProtKB:Q9NWW6};
AltName: Full=Integrin beta-1-binding protein 3;
AltName: Full=Muscle integrin-binding protein;
Short=MIBP;
AltName: Full=Nicotinic acid riboside kinase 2;
EC=2.7.1.173 {ECO:0000250|UniProtKB:Q9NWW6};
AltName: Full=Ribosylnicotinamide kinase 2;
Short=RNK 2;
AltName: Full=Ribosylnicotinic acid kinase 2;
Name=Nmrk2; Synonyms=Itgb1bp3, Nrk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
Li J., Mayne R., Wu C.;
"A novel muscle-specific beta 1 integrin binding protein (MIBP) that
modulates myogenic differentiation.";
J. Cell Biol. 147:1391-1398(1999).
-!- FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside
(NR) and nicotinic acid riboside (NaR) to form nicotinamide
mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN).
Reduces laminin matrix deposition and cell adhesion to laminin,
but not to fibronectin. Involved in the regulation of PXN at the
protein level and of PXN tyrosine phosphorylation. May play a role
in the regulation of terminal myogenesis (By similarity).
{ECO:0000250, ECO:0000269|PubMed:10613898}.
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
{ECO:0000250|UniProtKB:Q9NWW6}.
-!- CATALYTIC ACTIVITY: ATP + beta-D-ribosylnicotinate = ADP +
nicotinate beta-D-ribonucleotide. {ECO:0000250|UniProtKB:Q9NWW6}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
{ECO:0000250|UniProtKB:Q9NWW6}.
-!- SUBUNIT: Monomer (By similarity). Interacts with ITGB1 alone or
when associated with alpha-7, but not with alpha-5. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein
level). {ECO:0000269|PubMed:10613898}.
-!- INDUCTION: Down-regulated during myoblast differentiation.
{ECO:0000269|PubMed:10613898}.
-!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK009352; BAB26235.1; -; mRNA.
EMBL; AK137483; BAE23375.1; -; mRNA.
EMBL; BC119244; AAI19245.1; -; mRNA.
EMBL; BC119246; AAI19247.1; -; mRNA.
CCDS; CCDS24046.1; -.
RefSeq; NP_081396.1; NM_027120.2.
UniGene; Mm.437211; -.
ProteinModelPortal; Q9D7C9; -.
SMR; Q9D7C9; -.
BioGrid; 213534; 1.
STRING; 10090.ENSMUSP00000005069; -.
PhosphoSitePlus; Q9D7C9; -.
PaxDb; Q9D7C9; -.
PRIDE; Q9D7C9; -.
Ensembl; ENSMUST00000005069; ENSMUSP00000005069; ENSMUSG00000004939.
GeneID; 69564; -.
KEGG; mmu:69564; -.
UCSC; uc007ggn.1; mouse.
CTD; 27231; -.
MGI; MGI:1916814; Nmrk2.
eggNOG; ENOG410IR10; Eukaryota.
eggNOG; ENOG4111VGZ; LUCA.
GeneTree; ENSGT00510000046782; -.
HOGENOM; HOG000043899; -.
HOVERGEN; HBG052669; -.
InParanoid; Q9D7C9; -.
KO; K10524; -.
OMA; PQKFARA; -.
OrthoDB; EOG091G0JV5; -.
PhylomeDB; Q9D7C9; -.
TreeFam; TF105395; -.
Reactome; R-MMU-196807; Nicotinate metabolism.
UniPathway; UPA00253; -.
PRO; PR:Q9D7C9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000004939; -.
CleanEx; MM_ITGB1BP3; -.
Genevisible; Q9D7C9; MM.
GO; GO:0005622; C:intracellular; IPI:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050262; F:ribosylnicotinamide kinase activity; ISO:MGI.
GO; GO:0061769; F:ribosylnicotinate kinase activity; ISO:MGI.
GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:MGI.
InterPro; IPR027417; P-loop_NTPase.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Pyridine nucleotide biosynthesis;
Reference proteome; Transferase.
CHAIN 1 195 Nicotinamide riboside kinase 2.
/FTId=PRO_0000215895.
NP_BIND 9 17 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
NP_BIND 134 136 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
NP_BIND 174 176 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
REGION 35 38 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
REGION 54 55 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
REGION 136 137 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
ACT_SITE 35 35 Proton acceptor.
{ECO:0000250|UniProtKB:Q9NWW6}.
METAL 16 16 Magnesium.
{ECO:0000250|UniProtKB:Q9NWW6}.
METAL 35 35 Magnesium.
{ECO:0000250|UniProtKB:Q9NWW6}.
BINDING 130 130 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
BINDING 131 131 Substrate.
{ECO:0000250|UniProtKB:Q9NWW6}.
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


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