KAD8_RAT
ID KAD8_RAT Reviewed; 479 AA.
AC Q68FP8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=Ak8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000250|UniProtKB:Q96MA6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000250|UniProtKB:Q96MA6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000250|UniProtKB:Q96MA6};
CC -!- SUBUNIT: Interacts with CFAP45 and CFAP52; CFAP45 and AK8 dimerization
CC may create a cavity at the interface of the dimer that can accommodate
CC AMP. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of
CC respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; BC079446; AAH79446.1; -; mRNA.
DR RefSeq; NP_001004266.1; NM_001004266.1.
DR AlphaFoldDB; Q68FP8; -.
DR SMR; Q68FP8; -.
DR IntAct; Q68FP8; 1.
DR STRING; 10116.ENSRNOP00000017029; -.
DR CarbonylDB; Q68FP8; -.
DR PaxDb; Q68FP8; -.
DR PRIDE; Q68FP8; -.
DR Ensembl; ENSRNOT00000017029; ENSRNOP00000017029; ENSRNOG00000012761.
DR GeneID; 311833; -.
DR KEGG; rno:311833; -.
DR UCSC; RGD:1303144; rat.
DR CTD; 158067; -.
DR RGD; 1303144; Ak8.
DR eggNOG; KOG3078; Eukaryota.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000161613; -.
DR HOGENOM; CLU_044905_0_0_1; -.
DR InParanoid; Q68FP8; -.
DR OMA; DCIRRGW; -.
DR OrthoDB; 961384at2759; -.
DR PhylomeDB; Q68FP8; -.
DR TreeFam; TF328560; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q68FP8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000012761; Expressed in testis and 4 other tissues.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; ISS:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; ISO:RGD.
DR CDD; cd01428; ADK; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57774; SSF57774; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Adenylate kinase 8"
FT /id="PRO_0000279386"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 87..113
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 177..206
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 269..471
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 298..327
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 391..424
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 140..143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 203
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 325..327
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 354..357
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 361
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 479 AA; 54966 MW; D2331D51EFC5A15A CRC64;
MDATSAPHRI PPEMPQYGED YHIFEMMQSM LEQLLIHQPE DPISFMISHL RRNNDNVPRV
VILGPPASGK TTIAMWLCKH LNSNLITKEN LLEREFSLLS LEAKKHYQVY KRVPNSTLVS
LVQERLNEDD CLRRGWILDG IPERREQALM IQTLGLAPKH VIVLSAPDSV LIERNVGKRI
DPVTGEIYHT TFDWPPELEI QNRLIQPEGI SEIDTAKKLL EYHRHIIRIL PSYPKILKTI
SSDQPCVDVF YQALTYVQSG HRCNAPFTPK VLLCGPMGCG KKLQAALLSQ KYGLVNISCG
QLLKEAMAAE SSLGDLIEPF FEKRMTVPDS IITRVLTERL KQQDCIQKGW VLHGFPRDLD
QARLLNSMGY SPNRVFFLNV PLDSILERLT LRRTDPVTGE RFHLMYKPPP TIEVQARLLQ
NPKDSEEYIK LQTDLFYRNS GDLEQYYDRA IIVNGDQDPY TVFEYIESGI INPLPRKVT
