KAD7_MOUSE
ID KAD7_MOUSE Reviewed; 614 AA.
AC Q9D2H2; Q8BVH3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Adenylate kinase 7;
DE Short=AK 7;
DE EC=2.7.4.3 {ECO:0000250|UniProtKB:Q96M32};
DE EC=2.7.4.6 {ECO:0000250|UniProtKB:Q96M32};
DE AltName: Full=ATP-AMP transphosphorylase 7;
GN Name=Ak7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18776131; DOI=10.1165/rcmb.2008-0102oc;
RA Fernandez-Gonzalez A., Kourembanas S., Wyatt T.A., Mitsialis S.A.;
RT "Mutation of murine adenylate kinase 7 underlies a primary ciliary
RT dyskinesia phenotype.";
RL Am. J. Respir. Cell Mol. Biol. 40:305-313(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=29365104; DOI=10.1093/hmg/ddy034;
RA Lores P., Coutton C., El Khouri E., Stouvenel L., Givelet M., Thomas L.,
RA Rode B., Schmitt A., Louis B., Sakheli Z., Chaudhry M.,
RA Fernandez-Gonzales A., Mitsialis A., Dacheux D., Wolf J.P., Papon J.F.,
RA Gacon G., Escudier E., Arnoult C., Bonhivers M., Savinov S.N., Amselem S.,
RA Ray P.F., Dulioust E., Toure A.;
RT "Homozygous missense mutation L673P in adenylate kinase 7 (AK7) leads to
RT primary male infertility and multiple morphological anomalies of the
RT flagella but not to primary ciliary dyskinesia.";
RL Hum. Mol. Genet. 27:1196-1211(2018).
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. Involved in maintaining ciliary
CC structure and function. {ECO:0000269|PubMed:18776131}.
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:Q96M32};
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:Q96M32};
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:Q96M32};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96M32}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q96M32}. Note=Detected along the full length of
CC sperm flagellum, where it colocalizes with alpha-tubulin.
CC {ECO:0000250|UniProtKB:Q96M32}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D2H2-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2H2-1; Sequence=VSP_008474, VSP_008475, VSP_008476;
CC -!- DISRUPTION PHENOTYPE: Mutant mice present pathological signs
CC characteristic of primary ciliary dyskinesia (PCD), including high
CC prevalence of microtubular defects, significantly decreased ciliary
CC beat frequency, hydrocephalus, abnormal spermatogenesis, mucus
CC accumulation in the paranasal passages, and exacerbated respiratory
CC responses upon allergen challenge. This phenotype arose serendipitously
CC in the process of generating transgenic mice harboring a heme oxygenase
CC 1 construct, due to the serendipitous disruption of Ak7 locus by the
CC transgene insertion event (PubMed:18776131). Mutant testes reveal the
CC absence of flagellum structures, compared with those from control
CC littermates. In mutant testes, nearly all sperm heads are attached to
CC cytoplasmic mass and not prolonged by flagellar structures, such as
CC mitochondrial sheath, fibrous sheath and axoneme. In mutant epididymes,
CC very few sperm structures are observed. The rare sperm flagellum
CC observed show an absence of the central pair of microtubules
CC (PubMed:29365104). {ECO:0000269|PubMed:18776131,
CC ECO:0000269|PubMed:29365104}.
CC -!- SIMILARITY: In the central section; belongs to the adenylate kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dpy-30 family.
CC {ECO:0000305}.
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DR EMBL; AK019664; BAB31828.1; -; mRNA.
DR EMBL; AK078221; BAC37180.1; -; mRNA.
DR RefSeq; NP_084463.1; NM_030187.1.
DR AlphaFoldDB; Q9D2H2; -.
DR SMR; Q9D2H2; -.
DR BioGRID; 219643; 2.
DR STRING; 10090.ENSMUSP00000043145; -.
DR iPTMnet; Q9D2H2; -.
DR PhosphoSitePlus; Q9D2H2; -.
DR MaxQB; Q9D2H2; -.
DR PaxDb; Q9D2H2; -.
DR PRIDE; Q9D2H2; -.
DR ProteomicsDB; 269240; -. [Q9D2H2-2]
DR ProteomicsDB; 269241; -. [Q9D2H2-1]
DR GeneID; 78801; -.
DR KEGG; mmu:78801; -.
DR UCSC; uc007oyu.1; mouse. [Q9D2H2-1]
DR CTD; 122481; -.
DR MGI; MGI:1926051; Ak7.
DR eggNOG; KOG3078; Eukaryota.
DR InParanoid; Q9D2H2; -.
DR OrthoDB; 572856at2759; -.
DR PhylomeDB; Q9D2H2; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 78801; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Ak7; mouse.
DR PRO; PR:Q9D2H2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D2H2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
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:0035082; P:axoneme assembly; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR026867; AK7.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PANTHER; PTHR23359:SF105; PTHR23359:SF105; 1.
DR Pfam; PF05186; Dpy-30; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Flagellum; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..614
FT /note="Adenylate kinase 7"
FT /id="PRO_0000158954"
FT REGION 258..503
FT /note="Adenylate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q96M32"
FT REGION 288..346
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..438
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 570..614
FT /note="DPY-30"
FT /evidence="ECO:0000250|UniProtKB:Q96M32"
FT COILED 376..568
FT /evidence="ECO:0000255"
FT COMPBIAS 311..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 323..346
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 373..376
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 380
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 446
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT VAR_SEQ 1..57
FT /note="MECDAVIYNITENVQQVEEALWAVSALNEEISHFEKRKVFILLSTVMTWARS
FT KPLDP -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008474"
FT VAR_SEQ 181..206
FT /note="KCISKNTGPGKIQKVPKENAFLTKDL -> KVCVLTPCRASLSSCTLWMLVT
FT DFLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008475"
FT VAR_SEQ 207..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008476"
SQ SEQUENCE 614 AA; 70675 MW; 0ABA0DC6C7CE5E8B CRC64;
MECDAVIYNI TENVQQVEEA LWAVSALNEE ISHFEKRKVF ILLSTVMTWA RSKPLDPDDN
EVPFTEEDYR RRKHHPNFLD HINAEKIVLK FGKNAKKFAT YVVASGLQYG AEGGILHTFF
KMAWLGEVPA LPVFGDGTNC IPAIHVVDLA GVIQNIIDHV PKLHYLVAVD EAVHTLEDLV
KCISKNTGPG KIQKVPKENA FLTKDLTQEY LDHLLVNLRM EALFVKENFN IRWVAQTGFV
ENINSILKEY KQSRGLLPIK ICILGPPAVG KSSISEELAK YYKLHHIKMK DVIAEAIAKL
EAIVAPKDSV EGEEEGEEEE EEENVDDAQE LLDGIKESME QNAGRLEDQY IIRFVKEKLK
SMPCRNQGFI LDGFPKTYDQ AKDLFNQEEE EEEEEIRGKI FPYDKLITPE FVCGLDASDE
FLKERVMNLP ESVVAGTHYS QDRFLRSLSH YRDINTDDET VFNYFDELEI HPIHIDVGKL
EDAQNRLAIK QLIKEIGKPR NYGLTDEEKA EEEKKAAEER LAKEAAQTAE LEHKEAMEMA
EKIARWEEWN KRLEEVKREE RELLEVQSVP LRNYLMTYVM PTLMQGLNEC CKVRPEDPVD
FLAEYLFKNN PEMQ
