ID KGUA_PIG Reviewed; 198 AA. AC P31006; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 112. DE RecName: Full=Guanylate kinase; DE EC=2.7.4.8 {ECO:0000269|PubMed:29515371}; DE AltName: Full=GMP kinase; GN Name=GUK1; Synonyms=GUK; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP PROTEIN SEQUENCE OF 2-198, ACETYLATION AT GLY-2, AND SUBUNIT. RC TISSUE=Brain; RX PubMed=8097461; DOI=10.1111/j.1432-1033.1993.tb17757.x; RA Zschocke P.D., Schiltz E., Schulz G.E.; RT "Purification and sequence determination of guanylate kinase from pig RT brain."; RL Eur. J. Biochem. 213:263-269(1993). RN [2] RP FUNCTION, INTERACTION WITH RD3, CATALYTIC ACTIVITY, AND ACTIVITY RP 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). Involved in the CC cGMP metabolism in photoreceptors. {ECO:0000269|PubMed:29515371}. 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}; CC -!- ACTIVITY REGULATION: Up-regulated by RD3. CC {ECO:0000269|PubMed:29515371}. CC -!- SUBUNIT: Monomer (PubMed:8097461). Interacts with RD3 (By similarity). CC {ECO:0000250|UniProtKB:Q16774, ECO:0000269|PubMed:8097461}. 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 -!- SIMILARITY: Belongs to the guanylate kinase family. {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 PIR; S23776; KIPGGU. DR AlphaFoldDB; P31006; -. DR SMR; P31006; -. DR STRING; 9823.ENSSSCP00000035398; -. DR iPTMnet; P31006; -. DR PaxDb; 9823-ENSSSCP00000014875; -. DR PeptideAtlas; P31006; -. DR eggNOG; KOG0707; Eukaryota. DR InParanoid; P31006; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. 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; ISS:UniProtKB. DR GO; GO:0050145; F:nucleoside monophosphate kinase activity; EXP:Reactome. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006163; P:purine nucleotide metabolic process; ISS: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:0000269|PubMed:8097461" FT CHAIN 2..198 FT /note="Guanylate kinase" FT /id="PRO_0000170653" 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-acetylglycine" FT /evidence="ECO:0000269|PubMed:8097461" SQ SEQUENCE 198 AA; 21921 MW; 09E9CC7130CCE1A7 CRC64; MGSPRPVVLS GPSGAGKSTL LKKLLQEHSS IFGFSVSHTT RDPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKAAVRA VQAMNRICVL DVDLQGVRNI KKTDLQPIYI FVQPPSLDVL EQRLRQRNTE TEESLAKRLA AAKADMESSK EPGLFDLIII NDSLDKAYWA LKEALSEEIK KAQATGHS //