ID   KGUA_BOVIN              Reviewed;         198 AA.
AC   P46195; Q3ZCE9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Guanylate kinase;
DE            EC=2.7.4.8 {ECO:0000269|PubMed:29515371, ECO:0000269|PubMed:7911663, ECO:0000269|PubMed:8243671};
DE   AltName: Full=GMP kinase;
GN   Name=GUK1; Synonyms=GUK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=7911663;
RA   Gaidarov I.O., Suslov O.N., Ovchinnikova T.V., Abdulaev N.G.;
RT   "Guanylate kinase from bovine retina: isolation, primary structure, and
RT   expression in E. coli.";
RL   Bioorg. Khim. 20:367-381(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 10-17; 24-32; 35-82; 90-97; 121-126; 139-146; 149-154
RP   AND 178-182, AND CATALYTIC ACTIVITY.
RX   PubMed=8243671; DOI=10.1016/0014-5793(93)80444-y;
RA   Gaidarov I.O., Suslov O.N., Abdulaev N.G.;
RT   "Enzymes of the cyclic GMP metabolism in bovine retina. I. Cloning and
RT   expression of the gene for guanylate kinase.";
RL   FEBS Lett. 335:81-84(1993).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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).
CC   -!- FUNCTION: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme
CC       for recycling GMP and indirectly, cyclic GMP (cGMP) (PubMed:8243671,
CC       PubMed:29515371, PubMed:7911663). Involved in the cGMP metabolism in
CC       photoreceptors (PubMed:29515371, PubMed:8243671).
CC       {ECO:0000269|PubMed:29515371, ECO:0000269|PubMed:7911663,
CC       ECO:0000269|PubMed:8243671}.
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:29515371, ECO:0000269|PubMed:7911663,
CC         ECO:0000269|PubMed:8243671};
CC   -!- ACTIVITY REGULATION: Up-regulated by RD3.
CC       {ECO:0000269|PubMed:29515371}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with RD3 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P31006,
CC       ECO:0000250|UniProtKB:Q16774}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:Q64520}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q64520}. Note=Colocalizes with RD3 in
CC       photoreceptor inner segments and to a lesser extent in the outer
CC       plexiform layer. {ECO:0000250|UniProtKB:Q64520}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina. {ECO:0000269|PubMed:7911663}.
CC   -!- SIMILARITY: Belongs to the guanylate kinase family. {ECO:0000305}.
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DR   EMBL; X67029; CAA47423.1; -; mRNA.
DR   EMBL; BC102478; AAI02479.1; -; mRNA.
DR   PIR; S39447; S39447.
DR   RefSeq; NP_001152884.1; NM_001159412.1.
DR   RefSeq; NP_001152885.1; NM_001159413.1.
DR   RefSeq; NP_776503.1; NM_174078.3.
DR   RefSeq; XP_005208455.1; XM_005208398.3.
DR   AlphaFoldDB; P46195; -.
DR   SMR; P46195; -.
DR   STRING; 9913.ENSBTAP00000068771; -.
DR   PaxDb; 9913-ENSBTAP00000019656; -.
DR   Ensembl; ENSBTAT00000036545.2; ENSBTAP00000036402.1; ENSBTAG00000014775.6.
DR   Ensembl; ENSBTAT00000066343.2; ENSBTAP00000054864.1; ENSBTAG00000014775.6.
DR   GeneID; 281217; -.
DR   KEGG; bta:281217; -.
DR   CTD; 2987; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014775; -.
DR   VGNC; VGNC:29725; GUK1.
DR   eggNOG; KOG0707; Eukaryota.
DR   GeneTree; ENSGT00940000155815; -.
DR   HOGENOM; CLU_001715_0_2_1; -.
DR   InParanoid; P46195; -.
DR   OMA; HFFEHVK; -.
DR   OrthoDB; 324675at2759; -.
DR   Reactome; R-BTA-499943; Interconversion of nucleotide di- and triphosphates.
DR   Reactome; R-BTA-9748787; Azathioprine ADME.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000014775; Expressed in retina and 109 other cell types or tissues.
DR   ExpressionAtlas; P46195; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004385; F:guanylate kinase activity; IMP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IMP:UniProtKB.
DR   CDD; cd00071; GMPK; 1.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03263; guanyl_kin; 1.
DR   PANTHER; PTHR23117:SF13; GUANYLATE KINASE; 1.
DR   PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q16774"
FT   CHAIN           2..198
FT                   /note="Guanylate kinase"
FT                   /id="PRO_0000170650"
FT   DOMAIN          4..186
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         37..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   BINDING         171..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q64520"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16774"
SQ   SEQUENCE   198 AA;  21910 MW;  9A153A0924C1F3AB CRC64;
     MSGPRPVVLS GPSGAGKSTL LKKLLQEHGS IFGFSVSHTT RDPRPGEENG KDYYFVTREV
     MQRDIAAGDF IEHAEFSGNL YGTSKAAVRA VQAMNRICVL DVDLQGVRNI KKTDLRPIYI
     FVQPPSLDVL EQRLRQRNTE TEESLAKRLA AARADMESSK EPGLFDLIIV NDSLDKAYWA
     LKEALSEEIK KAQGTGQS
//