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P29410 (KAD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylate kinase 2, mitochondrial
Short name=AK 2
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase 2
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene names
Name:Ak2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis By similarity. HAMAP-Rule MF_03168

Catalytic activity

ATP + AMP = 2 ADP. HAMAP-Rule MF_03168

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion intermembrane space By similarity HAMAP-Rule MF_03168.

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_03168

Sequence similarities

Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processADP biosynthetic process

Inferred from direct assay PubMed 5123889. Source: RGD

AMP metabolic process

Inferred from direct assay PubMed 5010295. Source: RGD

ATP metabolic process

Inferred from direct assay PubMed 5010295. Source: RGD

adenine metabolic process

Traceable author statement Ref.1. Source: RGD

brain development

Inferred from expression pattern PubMed 9920788. Source: RGD

dATP metabolic process

Inferred from direct assay PubMed 5010295. Source: RGD

liver development

Inferred from expression pattern PubMed 5123889. Source: RGD

oxidative phosphorylation

Inferred from expression pattern PubMed 18423391. Source: RGD

response to thyroid hormone stimulus

Inferred from expression pattern PubMed 21563808. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 9504419. Source: RGD

mitochondrial inner membrane

Inferred from electronic annotation. Source: Compara

mitochondrial intermembrane space

Inferred from direct assay PubMed 19139979. Source: RGD

sperm mitochondrial sheath

Inferred from electronic annotation. Source: Compara

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from direct assay PubMed 19049516. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29410-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P29410-2)

The sequence of this isoform differs from the canonical sequence as follows:
     232-239: CKDLVMFV → S
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 239238Adenylate kinase 2, mitochondrial HAMAP-Rule MF_03168
PRO_0000158920

Regions

Nucleotide binding25 – 306ATP By similarity
Nucleotide binding72 – 743AMP By similarity
Nucleotide binding100 – 1034AMP By similarity
Nucleotide binding151 – 1522ATP By similarity
Region45 – 7430NMPbind By similarity
Region141 – 17838LID By similarity

Sites

Binding site461AMP By similarity
Binding site511AMP By similarity
Binding site1071AMP By similarity
Binding site1421ATP By similarity
Binding site1751AMP By similarity
Binding site1861AMP By similarity
Binding site2141ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue931N6-acetyllysine By similarity
Disulfide bond42 ↔ 92 By similarity

Natural variations

Alternative sequence232 – 2398CKDLVMFV → S in isoform 2.
VSP_036505

Experimental info

Sequence conflict141E → K in AAH61727. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 075A4ACBD581DB8C

FASTA23926,379
        10         20         30         40         50         60 
MAPNALAPEP EHPEGIRAVL LGPPGAGKGT QAPKLAENFC VCHLATGDML RAMVASGSEL 

        70         80         90        100        110        120 
GKKLKATMDA GKLVSDEMVV ELIEKNLETP SCKNGFLLDG FPRTVKQAEM LDDLMDKRKE 

       130        140        150        160        170        180 
KLDSVIEFSI QDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EAMKDDITGE PLIRRSDDNE 

       190        200        210        220        230 
KALKTRLEAY HTQTTPLVEY YRKRGIHCAI DASQTPDVVF ASILAAFSKA TCKDLVMFV

« Hide

Isoform 2 [UniParc].

Checksum: 07537364EC6EEFA4
Show »

FASTA23225,530

References

« Hide 'large scale' references
[1]"Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes."
Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A.
J. Biochem. 113:200-207(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13061 mRNA. Translation: BAA02378.1.
BC061727 mRNA. Translation: AAH61727.1.
IPIIPI00230857.
IPI00923141.
PIRJQ1944.
RefSeqNP_001029139.1. NM_001033967.2.
UniGeneRn.3421.

3D structure databases

ProteinModelPortalP29410.
SMRP29410. Positions 15-232.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000000134.

PTM databases

PhosphoSiteP29410.

Proteomic databases

PaxDbP29410.
PRIDEP29410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000134; ENSRNOP00000000134; ENSRNOG00000000122.
GeneID24184.
KEGGrno:24184.

Organism-specific databases

CTD204.
RGD2077. Ak2.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00700000104498.
HOGENOMHOG000238772.
HOVERGENHBG000458.
InParanoidQ6P7C6.
KOK00939.
OrthoDBEOG483D5C.

Gene expression databases

GenevestigatorP29410.
GermOnlineENSRNOG00000000122. Rattus norvegicus.

Family and domain databases

HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP29410.
ChEMBLCHEMBL2376.
NextBio602539.

Entry information

Entry nameKAD2_RAT
AccessionPrimary (citable) accession number: P29410
Secondary accession number(s): Q6P7C6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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