KAD2_RAT
ID KAD2_RAT Reviewed; 239 AA.
AC P29410; Q6P7C6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Adenylate kinase 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03168};
DE Short=AK 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP-AMP transphosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03168};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03168};
GN Name=Ak2;
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 [MRNA] (ISOFORM 1).
RX PubMed=8468325; DOI=10.1093/oxfordjournals.jbchem.a124026;
RA Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A.;
RT "Tissue-specific and developmentally regulated expression of the genes
RT encoding adenylate kinase isozymes.";
RL J. Biochem. 113:200-207(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
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: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. Adenylate kinase
CC activity is critical for regulation of the phosphate utilization and
CC the AMP de novo biosynthesis pathways. Plays a key role in
CC hematopoiesis. {ECO:0000255|HAMAP-Rule:MF_03168}.
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:0000255|HAMAP-Rule:MF_03168};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03168}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000255|HAMAP-Rule:MF_03168}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29410-2; Sequence=VSP_036505;
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03168}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03168}.
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DR EMBL; D13061; BAA02378.1; -; mRNA.
DR EMBL; BC061727; AAH61727.1; -; mRNA.
DR PIR; JQ1944; JQ1944.
DR RefSeq; NP_001029139.1; NM_001033967.2.
DR AlphaFoldDB; P29410; -.
DR SMR; P29410; -.
DR STRING; 10116.ENSRNOP00000000134; -.
DR BindingDB; P29410; -.
DR ChEMBL; CHEMBL2376; -.
DR DrugCentral; P29410; -.
DR iPTMnet; P29410; -.
DR PhosphoSitePlus; P29410; -.
DR SwissPalm; P29410; -.
DR jPOST; P29410; -.
DR PaxDb; P29410; -.
DR PRIDE; P29410; -.
DR GeneID; 24184; -.
DR KEGG; rno:24184; -.
DR CTD; 204; -.
DR RGD; 2077; Ak2.
DR eggNOG; KOG3078; Eukaryota.
DR InParanoid; P29410; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; P29410; -.
DR TreeFam; TF300896; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:P29410; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0097226; C:sperm mitochondrial sheath; ISO:RGD.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046083; P:adenine metabolic process; TAS:RGD.
DR GO; GO:0006172; P:ADP biosynthetic process; IDA:RGD.
DR GO; GO:0046033; P:AMP metabolic process; IDA:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0046060; P:dATP metabolic process; IDA:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0006119; P:oxidative phosphorylation; IEP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03168; Adenylate_kinase_AK2; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR028587; AK2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; ATP-binding; Disulfide bond; Kinase;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..239
FT /note="Adenylate kinase 2, mitochondrial"
FT /id="PRO_0000158920"
FT REGION 45..74
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT REGION 141..178
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 25..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 46
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 51
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 72..74
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 100..103
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 151..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 175
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 186
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 62
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTP6"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54819"
FT DISULFID 42..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03168"
FT VAR_SEQ 232..239
FT /note="CKDLVMFV -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036505"
FT CONFLICT 14
FT /note="E -> K (in Ref. 2; AAH61727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26379 MW; 075A4ACBD581DB8C CRC64;
MAPNALAPEP EHPEGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML RAMVASGSEL
GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG FPRTVKQAEM LDDLMDKRKE
KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EAMKDDITGE PLIRRSDDNE
KALKTRLEAY HTQTTPLVEY YRKRGIHCAI DASQTPDVVF ASILAAFSKA TCKDLVMFV
