MAK_MOUSE
ID MAK_MOUSE Reviewed; 622 AA.
AC Q04859; E9Q4B2; E9QAU5; E9QKR3; Q8CDL5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Serine/threonine-protein kinase MAK;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P20794};
DE AltName: Full=Male germ cell-associated kinase;
DE AltName: Full=Protein kinase RCK;
GN Name=Mak; Synonyms=Rck;
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 [MRNA] (ISOFORM 1).
RX PubMed=8359591; DOI=10.1111/j.1432-0436.1993.tb00651.x;
RA Bladt F., Birchmeier C.;
RT "Characterization and expression analysis of the murine rck gene: a protein
RT kinase with a potential function in sensory cells.";
RL Differentiation 53:115-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=1473268; DOI=10.1002/cbf.290100411;
RA Koji T., Jinno A., Matsushime H., Shibuya M., Nakane P.K.;
RT "In situ localization of male germ cell-associated kinase (mak) mRNA in
RT adult mouse testis: specific expression in germ cells at stages around
RT meiotic cell division.";
RL Cell Biochem. Funct. 10:273-279(1992).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=11971961; DOI=10.1128/mcb.22.10.3276-3280.2002;
RA Shinkai Y., Satoh H., Takeda N., Fukuda M., Chiba E., Kato T.,
RA Kuramochi T., Araki Y.;
RT "A testicular germ cell-associated serine-threonine kinase, MAK, is
RT dispensable for sperm formation.";
RL Mol. Cell. Biol. 22:3276-3280(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RP1, AND TISSUE
RP SPECIFICITY.
RX PubMed=21148103; DOI=10.1073/pnas.1009437108;
RA Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S.,
RA Koyasu T., Kondo M., Furukawa T.;
RT "Negative regulation of ciliary length by ciliary male germ cell-associated
RT kinase (Mak) is required for retinal photoreceptor survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010).
CC -!- FUNCTION: Essential for the regulation of ciliary length and required
CC for the long-term survival of photoreceptors. Could have an important
CC function in sensory cells and in spermatogenesis. May participate in
CC signaling pathways used in visual and olfactory sensory transduction.
CC Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in
CC the transcriptional coactivation of AR (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:21148103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P20794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P20794};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P20794};
CC -!- SUBUNIT: Interacts with AR and CDK20. Found in a complex containing
CC MAK, AR and NCOA3. Interacts with FZR1 (via WD repeats) (By
CC similarity). Interacts with RP1. {ECO:0000250,
CC ECO:0000269|PubMed:21148103}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:21148103}. Photoreceptor inner segment
CC {ECO:0000250}. Note=Localizes in both the connecting cilia and the
CC outer segment axonemes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q04859-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04859-2; Sequence=VSP_042474;
CC Name=3;
CC IsoId=Q04859-3; Sequence=VSP_042472, VSP_042473;
CC -!- TISSUE SPECIFICITY: In pre- and postmeiotic male germ cells in testis.
CC In photoreceptor cells of the retina and in the olfactory receptors,
CC and in certain epithelia of the respiratory tract and choroid plexus
CC (brain). {ECO:0000269|PubMed:21148103}.
CC -!- DEVELOPMENTAL STAGE: On day 14 or 17 of embryonic development.
CC Expression is observed in germ cells at the stages of late pachytene
CC spermatocytes through to early round spermatids.
CC {ECO:0000269|PubMed:1473268}.
CC -!- PTM: Autophosphorylated. Phosphorylated on serine and threonine
CC residues (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are mostly fertile, develop normally, and
CC exhibit no gross abnormalities and spermatogenesis is intact. However,
CC both sperm motility and litter size is reduced.
CC {ECO:0000269|PubMed:11971961}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; X66983; CAA47392.1; -; mRNA.
DR EMBL; AK029894; BAC26662.1; -; mRNA.
DR EMBL; AC133496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26471.1; -. [Q04859-1]
DR CCDS; CCDS49244.1; -. [Q04859-3]
DR CCDS; CCDS49245.1; -. [Q04859-2]
DR PIR; I48733; I48733.
DR RefSeq; NP_001139274.1; NM_001145802.1. [Q04859-3]
DR RefSeq; NP_001139275.1; NM_001145803.1. [Q04859-2]
DR RefSeq; NP_032573.2; NM_008547.2. [Q04859-1]
DR RefSeq; XP_006516934.1; XM_006516871.2. [Q04859-1]
DR AlphaFoldDB; Q04859; -.
DR SMR; Q04859; -.
DR DIP; DIP-59494N; -.
DR IntAct; Q04859; 1.
DR STRING; 10090.ENSMUSP00000129615; -.
DR ChEMBL; CHEMBL2176784; -.
DR iPTMnet; Q04859; -.
DR PhosphoSitePlus; Q04859; -.
DR jPOST; Q04859; -.
DR MaxQB; Q04859; -.
DR PaxDb; Q04859; -.
DR PRIDE; Q04859; -.
DR ProteomicsDB; 292163; -. [Q04859-1]
DR ProteomicsDB; 292164; -. [Q04859-2]
DR ProteomicsDB; 292165; -. [Q04859-3]
DR Antibodypedia; 24855; 448 antibodies from 30 providers.
DR DNASU; 17152; -.
DR Ensembl; ENSMUST00000021792; ENSMUSP00000021792; ENSMUSG00000021363. [Q04859-1]
DR Ensembl; ENSMUST00000070193; ENSMUSP00000064750; ENSMUSG00000021363. [Q04859-3]
DR Ensembl; ENSMUST00000165087; ENSMUSP00000129615; ENSMUSG00000021363. [Q04859-2]
DR Ensembl; ENSMUST00000225084; ENSMUSP00000152946; ENSMUSG00000021363. [Q04859-2]
DR GeneID; 17152; -.
DR KEGG; mmu:17152; -.
DR UCSC; uc007qev.2; mouse. [Q04859-1]
DR UCSC; uc007qew.2; mouse. [Q04859-2]
DR UCSC; uc007qex.2; mouse. [Q04859-3]
DR CTD; 4117; -.
DR MGI; MGI:96913; Mak.
DR VEuPathDB; HostDB:ENSMUSG00000021363; -.
DR eggNOG; KOG0661; Eukaryota.
DR GeneTree; ENSGT00940000156581; -.
DR HOGENOM; CLU_000288_181_25_1; -.
DR InParanoid; Q04859; -.
DR OMA; INPYTWS; -.
DR OrthoDB; 76933at2759; -.
DR TreeFam; TF328769; -.
DR BRENDA; 2.7.11.22; 3474.
DR BioGRID-ORCS; 17152; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Ddx6; mouse.
DR PRO; PR:Q04859; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q04859; protein.
DR Bgee; ENSMUSG00000021363; Expressed in retinal neural layer and 71 other tissues.
DR ExpressionAtlas; Q04859; baseline and differential.
DR Genevisible; Q04859; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:1902856; P:negative regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..622
FT /note="Serine/threonine-protein kinase MAK"
FT /id="PRO_0000086285"
FT DOMAIN 4..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 157
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P20794"
FT MOD_RES 159
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P20794"
FT VAR_SEQ 94..124
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042472"
FT VAR_SEQ 531..571
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042473"
FT VAR_SEQ 531
FT /note="A -> EDSIIKPIENLSCTGKSAEQLEDPQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042474"
FT CONFLICT 128
FT /note="P -> H (in Ref. 2; BAC26662)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="N -> D (in Ref. 2; BAC26662)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="T -> A (in Ref. 1; CAA47392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70080 MW; DB7E3B758F8FEA69 CRC64;
MNRYTTMKQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA
NVIKLKEVIR ENDHLYFVFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG
FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP
IDVWAVGSIM AELYTFRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ
CIPINLKTLI PNASSEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GSSAHHLDTK
QTLHKQLQPL EPKPSSSERD PKPLPNILDQ PAGQPQPKQG HQPLQTIQPP QNTVTHPPPK
QQGHQKPPQT MFPSIIKTIP VNSVSTLGHK GARRRWGQTV FKSGDSCDDI EDDLGASHSK
KPSMEACKEK KKESPFRFPD SGLPVSNHFK GENRNLHASV SLKSDPNLST ASTAKQYYLK
QSRYLPGVNP KNVSLVAGGK DINSHSWNNQ LFPKSLGSMG ADLSFKRSNA AGNLGSYTTY
NQTGYMPSFL KKEVGSAGQR IQLAPLGASA SDYTWSTKTG RGQFSGRTYN PTAKNLNIVN
RTQPVPSVHG RTDWVAKYGG HR
