ID   TSSK5_MOUSE             Reviewed;         372 AA.
AC   Q8C1R0; Q1WWK7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Testis-specific serine/threonine-protein kinase 5;
DE            Short=TSK-5;
DE            Short=TSSK-5;
DE            Short=Testis-specific kinase 5;
DE            EC=2.7.11.1;
GN   Name=Tssk5 {ECO:0000312|MGI:MGI:1920792};
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:BAC25160.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC25160.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAC25160.1};
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:AAI14544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-255.
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).
CC   -!- FUNCTION: May be involved in a signaling pathway during male germ cell
CC       development or mature sperm function. {ECO:0000250|UniProtKB:Q61241}.
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:Q9BXA7};
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:Q9BXA7};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9BXA7};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-207,
CC       potentially by autophosphorylation. {ECO:0000250|UniProtKB:Q9BXA7}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXA7}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25160.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK007032; BAC25160.1; ALT_FRAME; mRNA.
DR   EMBL; BC114543; AAI14544.1; -; mRNA.
DR   CCDS; CCDS37122.1; -.
DR   RefSeq; NP_898922.2; NM_183099.2.
DR   AlphaFoldDB; Q8C1R0; -.
DR   SMR; Q8C1R0; -.
DR   BioGRID; 216092; 2.
DR   MINT; Q8C1R0; -.
DR   STRING; 10090.ENSMUSP00000071120; -.
DR   SwissPalm; Q8C1R0; -.
DR   PaxDb; 10090-ENSMUSP00000071120; -.
DR   ProteomicsDB; 300143; -.
DR   DNASU; 73542; -.
DR   Ensembl; ENSMUST00000071119.8; ENSMUSP00000071120.7; ENSMUSG00000060794.9.
DR   GeneID; 73542; -.
DR   KEGG; mmu:73542; -.
DR   UCSC; uc007wka.1; mouse.
DR   AGR; MGI:1920792; -.
DR   CTD; 73542; -.
DR   MGI; MGI:1920792; Tssk5.
DR   VEuPathDB; HostDB:ENSMUSG00000060794; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00940000163790; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q8C1R0; -.
DR   OMA; VRECRDN; -.
DR   OrthoDB; 5475498at2759; -.
DR   PhylomeDB; Q8C1R0; -.
DR   TreeFam; TF105333; -.
DR   BioGRID-ORCS; 73542; 1 hit in 77 CRISPR screens.
DR   PRO; PR:Q8C1R0; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8C1R0; Protein.
DR   Bgee; ENSMUSG00000060794; Expressed in spermatid and 3 other cell types or tissues.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF86; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q8C1R0; MM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Developmental protein; Differentiation; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Spermatogenesis; Transferase.
FT   CHAIN           1..372
FT                   /note="Testis-specific serine/threonine-protein kinase 5"
FT                   /id="PRO_0000281894"
FT   DOMAIN          27..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          314..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P28523,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         33..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P28523,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P28523,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   372 AA;  42234 MW;  9F43A6148147DD06 CRC64;
     MRSSSWRKSD QRVFIEQVRE CMNNGYLLSS KKIGSGAFSK VYLAYATRER MKHNPRLSSD
     LRGKRHTMVA IKIVSMAEAP AEYSRKFLPR EILSLNATYK HMNIVQLYET YQNSQRSYLV
     LELAARGDLL EHINAVSDLR CCPGLEEEEA RRLFWQLVSA VAHCHNVGIV HRDLKCENIL
     LDDQGFIKLT DFGFANWVGL KNSLLSTFCG SVAYTAPEIL MSKKYNGEQA DLWSLGIILH
     AMVSGKLPFK EHQPHRMLNL IRRGPIFRPG LSPECRDLIR GLLQLHPCER LDLQQVAAHC
     WMLPAEHMLS SALGAPREQD HSWSTVAPDN TEPDRDTRHA RSKGSSSSSG RTSPRRPSLA
     QLCNTWKPAP EQ
//