MAK_RAT
ID MAK_RAT Reviewed; 622 AA.
AC P20793; G3V7Y4; Q6AYW0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 142.
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;
GN Name=Mak;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=2183027; DOI=10.1128/mcb.10.5.2261-2268.1990;
RA Matsushime H., Jinno A., Takagi N., Shibuya M.;
RT "A novel mammalian protein kinase gene (mak) is highly expressed in
RT testicular germ cells at and after meiosis.";
RL Mol. Cell. Biol. 10:2261-2268(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Brown Norway; TISSUE=Testis;
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).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION, AND ALTERNATIVE SPLICING.
RX PubMed=8321219; DOI=10.1128/mcb.13.7.4146-4156.1993;
RA Jinno A., Tanaka K., Matsushime H., Haneji T., Shibuya M.;
RT "Testis-specific mak protein kinase is expressed specifically in the
RT meiotic phase in spermatogenesis and is associated with a 210-kilodalton
RT cellular phosphoprotein.";
RL Mol. Cell. Biol. 13:4146-4156(1993).
CC -!- FUNCTION: Essential for the regulation of ciliary length and required
CC for the long-term survival of photoreceptors (By similarity). Could
CC play an important function in spermatogenesis. Phosphorylates FZR1 in a
CC cell cycle-dependent manner (By similarity). Plays a role in the
CC transcriptional coactivation of AR (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:2183027}.
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 RP1. Interacts with AR and CDK20. Found in a
CC complex containing MAK, AR and NCOA3. Interacts with FZR1 (via WD
CC repeats) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:8321219}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250}. Photoreceptor inner segment
CC {ECO:0000250}. Note=Localized in both the connecting cilia and the
CC outer segment axonemes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20793-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20793-2; Sequence=VSP_042475;
CC -!- TISSUE SPECIFICITY: Expressed mainly in testicular cells at and after
CC meiosis. {ECO:0000269|PubMed:2183027, ECO:0000269|PubMed:8321219}.
CC -!- DEVELOPMENTAL STAGE: Expression in testis is detected 16 days after
CC birth and increases gradually to reach a plateau about 4 weeks after
CC birth (at protein level). {ECO:0000269|PubMed:8321219}.
CC -!- PTM: Autophosphorylated (By similarity). Phosphorylated on serine and
CC threonine residues. {ECO:0000250, ECO:0000269|PubMed:8321219}.
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; M35862; AAA41562.1; -; mRNA.
DR EMBL; CH473977; EDL98222.1; -; Genomic_DNA.
DR EMBL; BC078887; AAH78887.1; -; mRNA.
DR PIR; A34711; A34711.
DR RefSeq; NP_037268.1; NM_013136.1. [P20793-1]
DR AlphaFoldDB; P20793; -.
DR SMR; P20793; -.
DR STRING; 10116.ENSRNOP00000020672; -.
DR PhosphoSitePlus; P20793; -.
DR jPOST; P20793; -.
DR PaxDb; P20793; -.
DR PRIDE; P20793; -.
DR Ensembl; ENSRNOT00000020672; ENSRNOP00000020672; ENSRNOG00000015101. [P20793-1]
DR Ensembl; ENSRNOT00000107200; ENSRNOP00000079083; ENSRNOG00000015101. [P20793-2]
DR GeneID; 25677; -.
DR KEGG; rno:25677; -.
DR UCSC; RGD:3036; rat. [P20793-1]
DR CTD; 4117; -.
DR RGD; 3036; Mak.
DR eggNOG; KOG0661; Eukaryota.
DR GeneTree; ENSGT00940000156581; -.
DR HOGENOM; CLU_000288_181_25_1; -.
DR InParanoid; P20793; -.
DR OMA; PMHQENI; -.
DR OrthoDB; 76933at2759; -.
DR BRENDA; 2.7.11.22; 5301.
DR PRO; PR:P20793; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000015101; Expressed in testis and 3 other tissues.
DR Genevisible; P20793; RN.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS: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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; Developmental protein; Differentiation; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Spermatogenesis;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..622
FT /note="Serine/threonine-protein kinase MAK"
FT /id="PRO_0000086286"
FT DOMAIN 4..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
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 531..571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042475"
FT CONFLICT 581
FT /note="Q -> R (in Ref. 1; AAA41562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69897 MW; 7C2056E1D116D3BF CRC64;
MNRYTTMRQL GDGTYGSVLM GKSNESGELV AIKRMKRKFY SWDECMNLRE VKSLKKLNHA
NVIKLKEVIR ENDHLYFIFE YMKENLYQLM KDRNKLFPES VIRNIMYQIL QGLAFIHKHG
FFHRDMKPEN LLCMGPELVK IADFGLAREL RSQPPYTDYV STRWYRAPEV LLRSSVYSSP
IDVWAVGSIM AELYTFRPLF PGTSEVDEIF KICQVLGTPK KSDWPEGYQL ASSMNFRFPQ
CIPINLKTLI PNASSEAIQL MTEMLNWDPK KRPTASQALK HPYFQVGQVL GPSAHHLDAK
QTLHKQLQPP EPKPSSSERD PKPLPNILDQ PAGQPQPKQG HQPLQAIQPP QNTVVQPPPK
QQGHHKQPQT MFPSIVKTIP TNPVSTVGHK GARRRWGQTV FKSGDSCDNI EDCDLGASHS
KKPSMDAFKE KKKKESPFRF PEAGLPVSNH LKGENRNLHA SLKSDTNLST ASTAKQYYLK
QSRYLPGVNP KNVSLVAGGK DINSHSWNNQ LFPKSLGSMG ADLAFKRSNA AGNLGSYSAY
SQTGCVPSFL KKEVGSAGQR IHLAPLGASA ADYTWSTKTG QGQFSGRTYN PTAKNLNIVN
RTQPVPSVHG RTDWVAKYGG HR
