ID TSSK4_MOUSE Reviewed; 328 AA. AC Q9D411; A3QQQ9; A3QQR0; A3QQR1; A9P6P7; A9P6P9; Q9DA58; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 10-FEB-2021, entry version 146. DE RecName: Full=Testis-specific serine/threonine-protein kinase 4 {ECO:0000303|PubMed:20729278}; DE Short=TSK-4 {ECO:0000305}; DE Short=TSSK-4 {ECO:0000303|PubMed:20729278}; DE Short=Testis-specific kinase 4 {ECO:0000305}; DE EC=2.7.11.1 {ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:23599433, ECO:0000269|PubMed:26940607}; GN Name=Tssk4 {ECO:0000312|MGI:MGI:1918349}; GN Synonyms=Tssk5 {ECO:0000303|PubMed:17927909}; 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:0000312|EMBL:ABO33082.1, ECO:0000312|EMBL:ABO33083.1, ECO:0000312|EMBL:ABO33084.1, ECO:0000312|EMBL:ABO33085.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, CATALYTIC RP ACTIVITY, COFACTOR, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=ICR {ECO:0000312|EMBL:ABO33082.1, ECO:0000312|EMBL:ABO33083.1, RC ECO:0000312|EMBL:ABO33084.1, ECO:0000312|EMBL:ABO33085.1}; RX PubMed=17927909; DOI=10.5483/bmbrep.2007.40.5.749; RA Wei Y., Fu G., Hu H., Lin G., Yang J., Guo J., Zhu Q., Yu L.; RT "Isolation and characterization of mouse testis specific serine/threonine RT kinase 5 possessing four alternatively spliced variants."; RL J. Biochem. Mol. Biol. 40:749-756(2007). RN [2] {ECO:0000312|EMBL:ABD59200.1, ECO:0000312|EMBL:ABD59201.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Testis {ECO:0000312|EMBL:ABD59200.1, ECO:0000312|EMBL:ABD59201.1}; RX PubMed=20729278; DOI=10.1093/molehr/gaq071; RA Li Y., Sosnik J., Brassard L., Reese M., Spiridonov N.A., Bates T.C., RA Johnson G.R., Anguita J., Visconti P.E., Salicioni A.M.; RT "Expression and localization of five members of the testis-specific serine RT kinase (Tssk) family in mouse and human sperm and testis."; RL Mol. Hum. Reprod. 17:42-56(2011). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589}; 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 [5] {ECO:0000312|EMBL:EDL36264.1, ECO:0000312|EMBL:EDL36265.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH HSP90, AND RP UBIQUITINATION. RX PubMed=23599433; DOI=10.1074/jbc.m112.400978; RA Jha K.N., Coleman A.R., Wong L., Salicioni A.M., Howcroft E., Johnson G.R.; RT "Heat shock protein 90 functions to stabilize and activate the testis- RT specific serine/threonine kinases, a family of kinases essential for male RT fertility."; RL J. Biol. Chem. 288:16308-16320(2013). RN [7] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND AUTOPHOSPHORYLATION RP AT THR-197. RX PubMed=23054012; DOI=10.1007/s11033-012-2078-x; RA Wei Y., Wang X., Fu G., Yu L.; RT "Testis specific serine/threonine kinase 4 (Tssk4) maintains its kinase RT activity by phosphorylating itself at Thr-197."; RL Mol. Biol. Rep. 40:439-447(2013). RN [8] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH ODF2, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP LYS-54 AND THR-197. RX PubMed=25361759; DOI=10.1093/molehr/gau097; RA Wang X., Wei Y., Fu G., Li H., Saiyin H., Lin G., Wang Z., Chen S., Yu L.; RT "Tssk4 is essential for maintaining the structural integrity of sperm RT flagellum."; RL Mol. Hum. Reprod. 21:136-145(2015). RN [9] {ECO:0000305} RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CREM, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, PHOSPHORYLATION AT THR-197, AND MUTAGENESIS OF LYS-54. RX PubMed=26940607; DOI=10.1080/09168451.2016.1146067; RA Fu G., Wei Y., Wang X., Yu L.; RT "Phosphorylated testis-specific serine/threonine kinase 4 may phosphorylate RT Crem at Ser-117."; RL Biosci. Biotechnol. Biochem. 80:1088-1094(2016). RN [10] {ECO:0000305} RP FUNCTION, SUBUNIT, AND INTERACTION WITH ODF2. RX PubMed=26961893; DOI=10.1038/srep22861; RA Wang X., Li H., Fu G., Wang Y., Du S., Yu L., Wei Y., Chen S.; RT "Testis-specific serine/threonine protein kinase 4 (Tssk4) phosphorylates RT Odf2 at Ser-76."; RL Sci. Rep. 6:22861-22861(2016). CC -!- FUNCTION: [Isoform 1]: Serine/threonine kinase which is involved in CC male germ cell development and in mature sperm function CC (PubMed:17927909, PubMed:23599433, PubMed:23054012, PubMed:25361759, CC PubMed:26940607). May be involved in the Cre/Creb signaling pathway CC (PubMed:26940607). Phosphorylates CREB1 on 'Ser-133' in vitro and can CC stimulate Cre/Creb pathway in cells (By similarity). Phosphorylates CC CREM on 'Ser-116' in vitro (PubMed:26940607). Phosphorylates ODF2 on CC 'Ser-95' (PubMed:26961893). {ECO:0000250|UniProtKB:Q6SA08, CC ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:23054012, CC ECO:0000269|PubMed:23599433, ECO:0000269|PubMed:25361759, CC ECO:0000269|PubMed:26940607, ECO:0000269|PubMed:26961893}. CC -!- FUNCTION: [Isoform 2]: Catalytically inactive. CC {ECO:0000269|PubMed:17927909}. CC -!- FUNCTION: [Isoform 3]: Catalytically inactive. CC {ECO:0000269|PubMed:17927909}. CC -!- FUNCTION: [Isoform 4]: Catalytically inactive. CC {ECO:0000269|PubMed:17927909}. 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:0000269|PubMed:17927909, ECO:0000269|PubMed:23054012, CC ECO:0000269|PubMed:23599433, ECO:0000269|PubMed:25361759, CC ECO:0000269|PubMed:26940607}; 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:0000269|PubMed:17927909, CC ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:23599433, CC ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17927909, ECO:0000269|PubMed:23599433}; CC Note=Mg(2+) and Mn(2+) were both present in the kinase buffer but CC Mg(2+) is likely to be the in vivo cofactor. CC {ECO:0000305|PubMed:23599433}; CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Thr-197. CC {ECO:0000269|PubMed:23054012}. CC -!- SUBUNIT: Homodimer (PubMed:17927909, PubMed:23054012). Interacts with CC HSP90; this interaction stabilizes and activates TSSK4 CC (PubMed:23599433). Interacts with ODF2 (via C-terminus); this CC interaction promotes ODF2 phosphorylation on 'Ser-95' (PubMed:25361759, CC PubMed:26961893). May interact with CREM (PubMed:26940607). Interacts CC with CREB1; this interaction facilitates CREB1 phosphorylation on 'Ser- CC 133' (By similarity). Interacts with QRICH2 (By similarity). CC {ECO:0000250|UniProtKB:Q6SA08, ECO:0000269|PubMed:17927909, CC ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:23599433, CC ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607, CC ECO:0000269|PubMed:26961893}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome CC {ECO:0000269|PubMed:20729278}. Cell projection, cilium, flagellum CC {ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:23054012, CC ECO:0000269|PubMed:25361759}. Note=In spermatozoa, present in the sperm CC head and in the flagellum. {ECO:0000269|PubMed:20729278}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Alpha {ECO:0000303|PubMed:17927909}; CC IsoId=Q9D411-1; Sequence=Displayed; CC Name=2; Synonyms=b {ECO:0000303|PubMed:20729278}, Beta CC {ECO:0000303|PubMed:17927909}; CC IsoId=Q9D411-2; Sequence=VSP_023561; CC Name=3; Synonyms=c {ECO:0000303|PubMed:20729278}, Gamma CC {ECO:0000303|PubMed:17927909}; CC IsoId=Q9D411-3; Sequence=VSP_023561, VSP_059881, VSP_059884; CC Name=4; Synonyms=Delta {ECO:0000303|PubMed:17927909}; CC IsoId=Q9D411-4; Sequence=VSP_023561, VSP_059882, VSP_059883; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in spermatocytes and mature CC sperm (at protein level) (PubMed:20729278, PubMed:23054012, CC PubMed:25361759, PubMed:26940607). Highly expressed in the spleen, CC heart and testis (PubMed:17927909, PubMed:20729278, PubMed:23054012). CC Isoform 2, isoform 3, and isoform 4: Expressed at highest level in CC testis and heart and at low levels in the liver, spleen, kidney, brain CC and thymus (PubMed:17927909). {ECO:0000269|PubMed:17927909, CC ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:23054012, CC ECO:0000269|PubMed:25361759, ECO:0000269|PubMed:26940607}. CC -!- DEVELOPMENTAL STAGE: Detected throughout spermiogenesis, in round CC spermatids, elongated spermatids, and mature spermatozoa CC (PubMed:23054012, PubMed:20729278, PubMed:26940607). Detected at low CC levels on postnatal day 14, with significantly increased expression on CC postnatal day 16. Expression levels are unchanged after postnatal day CC 16 (PubMed:17927909, PubMed:20729278). {ECO:0000269|PubMed:17927909, CC ECO:0000269|PubMed:20729278, ECO:0000269|PubMed:23054012, CC ECO:0000269|PubMed:26940607}. CC -!- PTM: Activated by autophosphorylation on Thr-197. ODF2 potentiates the CC autophosphorylation activity of TSSK4 at Thr-197. CC {ECO:0000269|PubMed:23054012, ECO:0000269|PubMed:26940607}. CC -!- PTM: Ubiquitinated; HSP90 activity negatively regulates ubiquitination CC and degradation. {ECO:0000269|PubMed:23599433}. CC -!- DISRUPTION PHENOTYPE: Male mice are subfertile due to reduced sperm CC motility. The reduced motility is due to morphological defects in the CC sperm flagellum at the midpiece-principal piece junction caused by the CC disordered arrangement of doublet microtubules and outer dense fibers. CC {ECO:0000269|PubMed:25361759}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB24429.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY461664; AAS17972.1; -; mRNA. DR EMBL; EF127819; ABO33082.1; -; mRNA. DR EMBL; EF127820; ABO33083.1; -; mRNA. DR EMBL; EF127821; ABO33084.1; -; mRNA. DR EMBL; EF127822; ABO33085.1; -; mRNA. DR EMBL; DQ397204; ABD59200.1; -; mRNA. DR EMBL; DQ397205; ABD59201.1; -; mRNA. DR EMBL; DQ397206; ABD59202.1; -; mRNA. DR EMBL; AK006144; BAB24429.1; ALT_SEQ; mRNA. DR EMBL; AK016890; BAB30483.1; -; mRNA. DR EMBL; AC174678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466535; EDL36265.1; -; Genomic_DNA. DR EMBL; CH466535; EDL36264.1; -; Genomic_DNA. DR CCDS; CCDS56959.1; -. [Q9D411-3] DR CCDS; CCDS88669.1; -. [Q9D411-2] DR CCDS; CCDS88670.1; -. [Q9D411-1] DR RefSeq; NP_001240817.1; NM_001253888.1. [Q9D411-2] DR RefSeq; NP_001240818.1; NM_001253889.1. [Q9D411-3] DR RefSeq; NP_081949.1; NM_027673.3. [Q9D411-1] DR SMR; Q9D411; -. DR BioGRID; 214476; 1. DR STRING; 10090.ENSMUSP00000007735; -. DR iPTMnet; Q9D411; -. DR PhosphoSitePlus; Q9D411; -. DR PaxDb; Q9D411; -. DR PRIDE; Q9D411; -. DR Antibodypedia; 22738; 135 antibodies. DR Ensembl; ENSMUST00000007735; ENSMUSP00000007735; ENSMUSG00000007591. [Q9D411-3] DR Ensembl; ENSMUST00000164809; ENSMUSP00000127728; ENSMUSG00000007591. [Q9D411-4] DR Ensembl; ENSMUST00000226591; ENSMUSP00000153752; ENSMUSG00000007591. [Q9D411-1] DR Ensembl; ENSMUST00000228395; ENSMUSP00000154783; ENSMUSG00000007591. [Q9D411-2] DR GeneID; 71099; -. DR KEGG; mmu:71099; -. DR UCSC; uc007tzx.3; mouse. DR UCSC; uc007tzy.2; mouse. [Q9D411-1] DR UCSC; uc011zlm.2; mouse. DR CTD; 283629; -. DR MGI; MGI:1918349; Tssk4. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00940000161286; -. DR HOGENOM; CLU_000288_63_0_1; -. DR InParanoid; Q9D411; -. DR OMA; KWENVKI; -. DR OrthoDB; 947464at2759; -. DR PhylomeDB; Q9D411; -. DR TreeFam; TF105333; -. DR BRENDA; 2.7.11.1; 3474. DR BioGRID-ORCS; 71099; 2 hits in 17 CRISPR screens. DR PRO; PR:Q9D411; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; Q9D411; protein. DR Bgee; ENSMUSG00000007591; Expressed in spermatid and 88 other tissues. DR ExpressionAtlas; Q9D411; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; TAS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0036126; C:sperm flagellum; IMP:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IMP:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB. DR GO; GO:0009566; P:fertilization; IMP:UniProtKB. DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:1990443; P:peptidyl-threonine autophosphorylation; IMP:UniProtKB. DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007286; P:spermatid development; IDA: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; KW Cytoplasmic vesicle; Developmental protein; Differentiation; Flagellum; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Spermatogenesis; KW Transferase; Ubl conjugation. FT CHAIN 1..328 FT /note="Testis-specific serine/threonine-protein kinase 4" FT /id="PRO_0000086773" FT DOMAIN 25..293 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 31..39 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 148 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 54 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000305|PubMed:25361759, ECO:0000305|PubMed:26940607" FT MOD_RES 197 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:23054012, FT ECO:0000269|PubMed:26940607" FT VAR_SEQ 147 FT /note="R -> RLTPSLSAAGR (in isoform 2, isoform 3 and FT isoform 4)" FT /id="VSP_023561" FT VAR_SEQ 269..282 FT /note="NLILQLLRQSTKRA -> GSSIKPGPQPLSPE (in isoform 3)" FT /id="VSP_059881" FT VAR_SEQ 269..278 FT /note="NLILQLLRQS -> VLAPPGGLRP (in isoform 4)" FT /id="VSP_059882" FT VAR_SEQ 279..328 FT /note="Missing (in isoform 4)" FT /id="VSP_059883" FT VAR_SEQ 283..328 FT /note="Missing (in isoform 3)" FT /id="VSP_059884" FT MUTAGEN 54 FT /note="K->M: Loss of kinase activity and no phosphorylation FT of ODF2. No effect on interaction with ODF2." FT /evidence="ECO:0000269|PubMed:25361759, FT ECO:0000269|PubMed:26940607" FT MUTAGEN 197 FT /note="T->A: Loss of kinase activity and no phosphorylation FT of ODF2. No effect on interaction with ODF2." FT /evidence="ECO:0000269|PubMed:25361759" FT CONFLICT 8 FT /note="E -> G (in Ref. 3; BAB24429)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="P -> H (in Ref. 2; ABD59201)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="S -> C (in Ref. 2; ABD59201)" FT /evidence="ECO:0000305" SQ SEQUENCE 328 AA; 37377 MW; 64C66FAC6A1762B1 CRC64; MGKGDTSETA SATPAYRSVM EEYGYEVGKI IGHGSYGTVY EAYYTKQKVM VAVKIISKKK ASEDYLNKFL PREIQVMKVL RHKYLINFYQ AIETTSRVYI ILELAQGGDV LEWIQRYGAC AETLAGKWFS QMALGIAYLH SKGIVHRDLK LENLLLDKRE NVKISDFGFA KMVPSSQPVH SSPSYRQMNS LSHLSQTYCG SFAYACPEIL LGLPYNPFLS DTWSMGVILY TLVVARLPFD DTNLKKLLRE TQKEVTFPAN LTISQECKNL ILQLLRQSTK RATILDVLRD PWMLKFQPEQ PSNEIRLLEA MYQPTSSAKR HQSLEITT //