TSSK5_MOUSE
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 03-AUG-2022, entry version 149.
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; Q8C1R0; -.
DR PRIDE; Q8C1R0; -.
DR ProteomicsDB; 300143; -.
DR DNASU; 73542; -.
DR Ensembl; ENSMUST00000071119; ENSMUSP00000071120; ENSMUSG00000060794.
DR GeneID; 73542; -.
DR KEGG; mmu:73542; -.
DR UCSC; uc007wka.1; mouse.
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; WMLPAAH; -.
DR OrthoDB; 1319999at2759; -.
DR PhylomeDB; Q8C1R0; -.
DR TreeFam; TF105333; -.
DR BioGRID-ORCS; 73542; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8C1R0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C1R0; protein.
DR Bgee; ENSMUSG00000060794; Expressed in spermatid and 3 other tissues.
DR Genevisible; Q8C1R0; MM.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
