KGUA_BOVIN
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 03-AUG-2022, entry version 132.
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.ENSBTAP00000019656; -.
DR PaxDb; P46195; -.
DR Ensembl; ENSBTAT00000036545; ENSBTAP00000036402; ENSBTAG00000014775.
DR Ensembl; ENSBTAT00000066343; ENSBTAP00000054864; ENSBTAG00000014775.
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; NFITHEV; -.
DR OrthoDB; 1522834at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014775; Expressed in retina and 109 other 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 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 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
