DYRK4_MOUSE
ID DYRK4_MOUSE Reviewed; 632 AA.
AC Q8BI55; Q80WP9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 4;
DE EC=2.7.12.1 {ECO:0000250|UniProtKB:Q9NR20};
GN Name=Dyrk4 {ECO:0000312|MGI:MGI:1330292};
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] {ECO:0000305, ECO:0000312|EMBL:BAC36621.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36621.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC36621.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH52324.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH52324.1};
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 [3] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17292540; DOI=10.1016/j.mce.2006.12.041;
RA Sacher F., Moeller C., Bone W., Gottwald U., Fritsch M.;
RT "The expression of the testis-specific Dyrk4 kinase is highly restricted to
RT step 8 spermatids but is not required for male fertility in mice.";
RL Mol. Cell. Endocrinol. 267:80-88(2007).
CC -!- FUNCTION: Possible non-essential role in spermiogenesis.
CC {ECO:0000269|PubMed:17292540}.
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=2.7.12.1;
CC Evidence={ECO:0000250|UniProtKB:Q9NR20};
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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q9NR20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000250|UniProtKB:Q9NR20};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NR20};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NR20}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8BI55-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8BI55-2; Sequence=VSP_052456, VSP_052457;
CC -!- TISSUE SPECIFICITY: Highly expressed in testes.
CC {ECO:0000269|PubMed:17292540}.
CC -!- PTM: Autophosphorylation on Tyr-379 in the activation loop is required
CC for kinase activity. {ECO:0000250|UniProtKB:Q9NR20}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; AK077117; BAC36621.1; -; mRNA.
DR EMBL; BC052324; AAH52324.1; -; mRNA.
DR CCDS; CCDS20559.2; -. [Q8BI55-1]
DR RefSeq; NP_997093.2; NM_207210.2. [Q8BI55-1]
DR AlphaFoldDB; Q8BI55; -.
DR SMR; Q8BI55; -.
DR STRING; 10090.ENSMUSP00000077606; -.
DR iPTMnet; Q8BI55; -.
DR PhosphoSitePlus; Q8BI55; -.
DR PaxDb; Q8BI55; -.
DR PeptideAtlas; Q8BI55; -.
DR PRIDE; Q8BI55; -.
DR ProteomicsDB; 277621; -. [Q8BI55-1]
DR ProteomicsDB; 277622; -. [Q8BI55-2]
DR Antibodypedia; 22291; 294 antibodies from 28 providers.
DR DNASU; 101320; -.
DR Ensembl; ENSMUST00000078521; ENSMUSP00000077606; ENSMUSG00000030345. [Q8BI55-1]
DR GeneID; 101320; -.
DR KEGG; mmu:101320; -.
DR UCSC; uc009dvg.1; mouse. [Q8BI55-2]
DR UCSC; uc009dvh.1; mouse. [Q8BI55-1]
DR CTD; 8798; -.
DR MGI; MGI:1330292; Dyrk4.
DR VEuPathDB; HostDB:ENSMUSG00000030345; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000159401; -.
DR HOGENOM; CLU_000288_5_9_1; -.
DR InParanoid; Q8BI55; -.
DR OMA; KASEMPF; -.
DR OrthoDB; 870358at2759; -.
DR PhylomeDB; Q8BI55; -.
DR TreeFam; TF314624; -.
DR BRENDA; 2.7.12.1; 3474.
DR BioGRID-ORCS; 101320; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q8BI55; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BI55; protein.
DR Bgee; ENSMUSG00000030345; Expressed in testis and 17 other tissues.
DR ExpressionAtlas; Q8BI55; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR Gene3D; 3.30.10.30; -; 1.
DR InterPro; IPR042521; DYRK.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..632
FT /note="Dual specificity tyrosine-phosphorylation-regulated
FT kinase 4"
FT /id="PRO_0000291539"
FT DOMAIN 219..515
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 225..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NR20,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 298..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 379
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9NR20"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052456"
FT VAR_SEQ 36..44
FT /note="KKQSFTSVK -> MRTSKAQSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052457"
FT CONFLICT 495..497
FT /note="Missing (in Ref. 2; AAH52324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 72561 MW; 2F2F74C6695833DD CRC64;
MQLLRLPALT RTETSMDTNK ARKRSLTTFP ILKARKKQSF TSVKVESKPL GHLQKPSSKN
KKLRVNRCPQ KIPSNTAFPF VDTKGKRNTV NFPQIGNKVP SKGPMQYQEN QIHNQVLSSE
LKTSEIPFNI NTKAQDTKPH PELQKKHKVP LTVAEALKFF KNQLSPYEQS EILGYSELWF
LGLEAKKLNV VPEKFSKTSF DDEHGSYMKV LHDHIAYRYE VLEMIGKGSF GQVAKCLDHK
NNELVALKII RNKKRFHHQA LVELKILEAL RRKDKDNNHN VVHMKDFFYF RNHLCITFEL
LGINLYELMK NNSFHGFNLS IVRRFTFSIL KCLHMLYVEK IIHCDLKPEN IVLYQRGQVT
VKVIDFGSSC YEHQKVYTYI QSRFYRSPEV ILGHPYNMAI DMWSLGCIMA ELYTGYPLFP
GENEVEQLAC IMEVLGLPPA HFTQTASRRQ VFFDSKGLPK NINNNRGGKR YPDSKDLTMV
VKTYDSSFLD FLRRCLVWEP SLRMTPEQAL KHAWIHEPRK FKPRPKPQIL RKPGASISSE
ISTEKAEEQQ ASKGKKDEAT KETTDKLKDE AEKHLENSGK QQSSVEHTAD TIQLPHLTEA
SGKSETVAGS EMSAEQQSTS SPKSTNILPP IV
