Q9R0Y5 (KAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylate kinase isoenzyme 1
Short name=AK 1
EC=2.7.4.3

Alternative name(s):
ATP-AMP transphosphorylase 1
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Myokinase

Gene names

Name:

Ak1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 By similarity. May provide a mechanism to buffer the adenylate energy charge for sperm motility. Ref.2
Catalytic activity	ATP + AMP = 2 ADP. HAMAP-Rule MF_03171
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Developmental stage	Up-regulated during late spermiogenesis, when the flagellum is being assembled. Ref.2
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_03171
Sequence similarities	Belongs to the adenylate kinase family. AK1 subfamily.
Sequence caution	The sequence CAM16612.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP metabolic process Inferred from electronic annotation. Source: InterPro cell cycle arrest Inferred from direct assay Ref.1. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: MGI outer dense fiber Inferred from direct assay Ref.2. Source: MGI plasma membrane Inferred from direct assay Ref.1. Source: MGI sperm flagellum Inferred from direct assay Ref.2. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from direct assay PubMed 198184PubMed 7323947PubMed 7444718. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9R0Y5-1)

Also known as: Ak1a;

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: Q9R0Y5-2)

Also known as: Ak1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ME → MGCCVSSEPQEEGGRKTG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 194	194	Adenylate kinase isoenzyme 1 HAMAP-Rule MF_03171		PRO_0000158911
Regions
	Nucleotide binding	18 – 23	6	ATP By similarity
	Nucleotide binding	65 – 67	3	AMP By similarity
	Nucleotide binding	94 – 97	4	AMP By similarity
	Region	38 – 67	30	NMPbind By similarity
	Region	131 – 141	11	LID By similarity
Sites
	Binding site	39	1	AMP By similarity
	Binding site	44	1	AMP By similarity
	Binding site	101	1	AMP By similarity
	Binding site	132	1	ATP By similarity
	Binding site	138	1	AMP By similarity
	Binding site	149	1	AMP By similarity
	Binding site	177	1	ATP; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
Natural variations
	Alternative sequence	1 – 2	2	ME → MGCCVSSEPQEEGGRKTG in isoform 2.		VSP_024843

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Ak1a) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 88E7862522967D14	FASTA	194	21,540
	10 20 30 40 50 60 MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SERGKKLSAI 70 80 90 100 110 120 MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK QGEEFEQKIG QPTLLLYVDA 130 140 150 160 170 180 GAETMTQRLL KRGETSGRVD DNEETIKKRL ETYYNATEPV ISFYDKRGIV RKVNAEGTVD 190 TVFSEVCTYL DSLK
	Isoform 2 (Ak1b) [UniParc]. Checksum: 5295189A6E7CB6D8	FASTA	210	23,116
	10 20 30 40 50 60 MGCCVSSEPQ EEGGRKTGEK LKKAKIIFVV GGPGSGKGTQ CEKIVQKYGY THLSTGDLLR 70 80 90 100 110 120 AEVSSGSERG KKLSAIMEKG ELVPLDTVLD MLRDAMLAKV DSSNGFLIDG YPREVKQGEE 130 140 150 160 170 180 FEQKIGQPTL LLYVDAGAET MTQRLLKRGE TSGRVDDNEE TIKKRLETYY NATEPVISFY 190 200 210 DKRGIVRKVN AEGTVDTVFS EVCTYLDSLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"wt p53 dependent expression of a membrane-associated isoform of adenylate kinase." Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M., Schneider C. Oncogene 18:5879-5888(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Adenylate kinases 1 and 2 are part of the accessory structures in the mouse sperm flagellum." Cao W., Haig-Ladewig L., Gerton G.L., Moss S.B. Biol. Reprod. 75:492-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE. Strain: CD-1.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Adipose tissue.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6 and FVB/N. Tissue: Mammary tumor and Retina.
[6]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 32-44; 64-77; 84-97 AND 150-166, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ010108 mRNA. Translation: CAB52407.1. AJ010109 mRNA. Translation: CAB52408.1. DQ486026 mRNA. Translation: ABF46940.1. AK046613 mRNA. Translation: BAC32808.1. AK089270 mRNA. Translation: BAC40822.1. AL772271 Genomic DNA. Translation: CAM16612.1. Sequence problems. AL772271 Genomic DNA. Translation: CAM16613.1. AL772271 Genomic DNA. Translation: CAM16614.1. BC014802 mRNA. Translation: AAH14802.1. BC054366 mRNA. Translation: AAH54366.1.
IPI	IPI00128209. IPI00750256.
RefSeq	NP_001185719.1. NM_001198790.1. NP_001185720.1. NM_001198791.1. NP_001185721.1. NM_001198792.1. NP_067490.1. NM_021515.3.
UniGene	Mm.29189.
3D structure databases
ProteinModelPortal	Q9R0Y5.
SMR	Q9R0Y5. Positions 1-194.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R0Y5. 2 interactions.
PTM databases
PhosphoSite	Q9R0Y5.
2D gel databases
REPRODUCTION-2DPAGE	IPI00128209. Q9R0Y5.
Proteomic databases
PaxDb	Q9R0Y5.
PRIDE	Q9R0Y5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817. ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817. ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817. ENSMUST00000156578; ENSMUSP00000123534; ENSMUSG00000026817.
GeneID	11636.
KEGG	mmu:11636.
UCSC	uc008jgh.2. mouse. uc008jgj.2. mouse.
Organism-specific databases
CTD	203.
MGI	MGI:87977. Ak1.
Phylogenomic databases
eggNOG	COG0563.
GeneTree	ENSGT00390000016215.
HOGENOM	HOG000238771.
HOVERGEN	HBG108060.
KO	K00939.
OMA	NRMKVYL.
OrthoDB	EOG402WT6.
Enzyme and pathway databases
BRENDA	2.7.4.3. 3474.
Gene expression databases
Bgee	Q9R0Y5.
CleanEx	MM_AK1.
Genevestigator	Q9R0Y5.
GermOnline	ENSMUSG00000026817. Mus musculus.
Family and domain databases
HAMAP	MF_00235. Adenylate_kinase_Adk. MF_03171. Adenylate_kinase_AK1.
InterPro	IPR000850. Adenylate_kin. IPR006267. Adenylate_kin1. [Graphical view]
PANTHER	PTHR23359. PTHR23359. 1 hit.
Pfam	PF00406. ADK. 1 hit. [Graphical view]
PRINTS	PR00094. ADENYLTKNASE.
TIGRFAMs	TIGR01360. aden_kin_iso1. 1 hit.
PROSITE	PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279205.
SOURCE	Search...

Entry information

Entry name

KAD1_MOUSE

Accession

Primary (citable) accession number: Q9R0Y5
Secondary accession number(s): A2AK80, Q542C5, Q9R0Y4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 4, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program