TSSK4_MOUSE
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 03-AUG-2022, entry version 152.
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};
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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 AlphaFoldDB; Q9D411; -.
DR SMR; Q9D411; -.
DR BioGRID; 214476; 1.
DR STRING; 10090.ENSMUSP00000007735; -.
DR iPTMnet; Q9D411; -.
DR PhosphoSitePlus; Q9D411; -.
DR PaxDb; Q9D411; -.
DR PRIDE; Q9D411; -.
DR ProteomicsDB; 298150; -. [Q9D411-1]
DR ProteomicsDB; 298151; -. [Q9D411-2]
DR ProteomicsDB; 336937; -.
DR ProteomicsDB; 341458; -.
DR Antibodypedia; 22738; 141 antibodies from 22 providers.
DR DNASU; 71099; -.
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 VEuPathDB; HostDB:ENSMUSG00000007591; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000161286; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9D411; -.
DR OMA; YMILELA; -.
DR OrthoDB; 947464at2759; -.
DR PhylomeDB; Q9D411; -.
DR TreeFam; TF105333; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 71099; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q9D411; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D411; protein.
DR Bgee; ENSMUSG00000007591; Expressed in spermatid and 45 other tissues.
DR ExpressionAtlas; Q9D411; baseline and differential.
DR GO; GO:0001669; C:acrosomal vesicle; TAS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
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:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
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: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 ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
