KGUA_MOUSE
ID KGUA_MOUSE Reviewed; 198 AA.
AC Q64520; Q564F2; Q564G0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Guanylate kinase;
DE EC=2.7.4.8 {ECO:0000269|PubMed:8663313};
DE AltName: Full=GMP kinase {ECO:0000303|PubMed:12036965};
DE AltName: Full=Guanylate kinase 1;
GN Name=Guk1 {ECO:0000312|MGI:MGI:95871};
GN Synonyms=Gmk {ECO:0000303|PubMed:8663313};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RX PubMed=8663313; DOI=10.1074/jbc.271.28.16734;
RA Brady W.A., Kokoris M.S., Fitzgibbon M., Black M.E.;
RT "Cloning, characterization, and modeling of mouse and human guanylate
RT kinases.";
RL J. Biol. Chem. 271:16734-16740(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT Degeneration Protein 3.";
RL Front. Mol. Neurosci. 11:52-52(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP AND GMP ANALOG,
RP AND ACTIVE SITE.
RX PubMed=12036965; DOI=10.1074/jbc.m204668200;
RA Sekulic N., Shuvalova L., Spangenberg O., Konrad M., Lavie A.;
RT "Structural characterization of the closed conformation of mouse guanylate
RT kinase.";
RL J. Biol. Chem. 277:30236-30243(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme
CC for recycling GMP and indirectly, cyclic GMP (cGMP) (PubMed:8663313).
CC Involved in the cGMP metabolism in photoreceptors (By similarity).
CC {ECO:0000250|UniProtKB:P46195, ECO:0000269|PubMed:8663313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.8;
CC Evidence={ECO:0000269|PubMed:8663313};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with RD3 (By similarity).
CC {ECO:0000250|UniProtKB:P31006, ECO:0000250|UniProtKB:Q16774}.
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC {ECO:0000269|PubMed:29515371}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:29515371}. Note=Colocalizes with RD3 in
CC photoreceptor inner segments and to a lesser extent in the outer
CC plexiform layer. {ECO:0000269|PubMed:29515371}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64520-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64520-2; Sequence=VSP_060370;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:8663313). In retina is
CC expressed in inner segment, outer nuclear layer, outer plexiform layer,
CC inner plexiform layer, and ganglion cell layer (at protein level)
CC (PubMed:29515371). {ECO:0000269|PubMed:29515371,
CC ECO:0000269|PubMed:8663313}.
CC -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR EMBL; U53514; AAC52652.1; -; mRNA.
DR EMBL; AK013514; BAB28891.1; -; mRNA.
DR EMBL; AK004205; BAB23219.2; -; mRNA.
DR EMBL; AL645854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466628; EDL07674.1; -; Genomic_DNA.
DR EMBL; CH466628; EDL07676.1; -; Genomic_DNA.
DR EMBL; BC024625; AAH24625.1; -; mRNA.
DR CCDS; CCDS24762.2; -. [Q64520-2]
DR RefSeq; NP_001152882.1; NM_001159410.1.
DR RefSeq; NP_032219.2; NM_008193.3. [Q64520-2]
DR RefSeq; XP_006532308.1; XM_006532245.3. [Q64520-1]
DR RefSeq; XP_006532309.1; XM_006532246.2. [Q64520-1]
DR PDB; 1LVG; X-ray; 2.10 A; A=1-198.
DR PDBsum; 1LVG; -.
DR AlphaFoldDB; Q64520; -.
DR SMR; Q64520; -.
DR BioGRID; 200128; 6.
DR IntAct; Q64520; 1.
DR STRING; 10090.ENSMUSP00000127566; -.
DR iPTMnet; Q64520; -.
DR PhosphoSitePlus; Q64520; -.
DR EPD; Q64520; -.
DR MaxQB; Q64520; -.
DR PaxDb; Q64520; -.
DR PRIDE; Q64520; -.
DR ProteomicsDB; 263433; -. [Q64520-1]
DR ProteomicsDB; 334633; -.
DR Antibodypedia; 34661; 257 antibodies from 23 providers.
DR DNASU; 14923; -.
DR Ensembl; ENSMUST00000170202; ENSMUSP00000127566; ENSMUSG00000020444. [Q64520-2]
DR GeneID; 14923; -.
DR KEGG; mmu:14923; -.
DR UCSC; uc007jdg.2; mouse.
DR CTD; 2987; -.
DR MGI; MGI:95871; Guk1.
DR VEuPathDB; HostDB:ENSMUSG00000020444; -.
DR eggNOG; KOG0707; Eukaryota.
DR GeneTree; ENSGT00940000155815; -.
DR InParanoid; Q64520; -.
DR OMA; EWAVVHG; -.
DR OrthoDB; 1522834at2759; -.
DR TreeFam; TF314473; -.
DR BRENDA; 2.7.4.8; 3474.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR BioGRID-ORCS; 14923; 26 hits in 79 CRISPR screens.
DR ChiTaRS; Guk1; mouse.
DR EvolutionaryTrace; Q64520; -.
DR PRO; PR:Q64520; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64520; protein.
DR Bgee; ENSMUSG00000020444; Expressed in retinal neural layer and 273 other tissues.
DR ExpressionAtlas; Q64520; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004385; F:guanylate kinase activity; IDA:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0046060; P:dATP metabolic process; ISO:MGI.
DR GO; GO:0006185; P:dGDP biosynthetic process; ISO:MGI.
DR GO; GO:0046054; P:dGMP metabolic process; ISO:MGI.
DR GO; GO:0046711; P:GDP biosynthetic process; ISO:MGI.
DR GO; GO:0019673; P:GDP-mannose metabolic process; ISO:MGI.
DR GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
DR GO; GO:0046037; P:GMP metabolic process; ISO:MGI.
DR GO; GO:0046939; P:nucleotide phosphorylation; ISO:MGI.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR017665; Guanylate_kinase.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00625; Guanylate_kin; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03263; guanyl_kin; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..198
FT /note="Guanylate kinase"
FT /id="PRO_0000170652"
FT DOMAIN 4..186
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT ACT_SITE 44
FT /evidence="ECO:0000305|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT ACT_SITE 137
FT /evidence="ECO:0000305|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT ACT_SITE 148
FT /evidence="ECO:0000305|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT BINDING 37..51
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT BINDING 171..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12036965,
FT ECO:0007744|PDB:1LVG"
FT VAR_SEQ 1
FT /note="M -> MLRRPLVGLAVAALGRVPADGM (in isoform 2)"
FT /id="VSP_060370"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1LVG"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1LVG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:1LVG"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1LVG"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1LVG"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:1LVG"
SQ SEQUENCE 198 AA; 21918 MW; F584E4B6521C607B CRC64;
MAGPRPVVLS GPSGAGKSTL LKKLFQEHSS IFGFSVSHTT RNPRPGEEDG KDYYFVTREM
MQRDIAAGDF IEHAEFSGNL YGTSKEAVRA VQAMNRICVL DVDLQGVRSI KKTDLCPIYI
FVQPPSLDVL EQRLRLRNTE TEESLAKRLA AARTDMESSK EPGLFDLVII NDDLDKAYAT
LKQALSEEIK KAQGTGHA
