TSSK3_MOUSE
ID TSSK3_MOUSE Reviewed; 268 AA.
AC Q9D2E1; Q9JL98;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Testis-specific serine/threonine-protein kinase 3;
DE Short=TSK-3;
DE Short=TSSK-3;
DE Short=Testis-specific kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase 22C;
GN Name=Tssk3; Synonyms=Stk22c, Stk22d;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Germ cell;
RX PubMed=11597141; DOI=10.1006/geno.2001.6628;
RA Visconti P.E., Hao Z., Purdon M.A., Stein P., Balsara B.R., Testa J.R.,
RA Herr J.C., Moss S.B., Kopf G.S.;
RT "Cloning and chromosomal localization of a gene encoding a novel
RT serine/threonine kinase belonging to the subfamily of testis-specific
RT kinases.";
RL Genomics 77:163-170(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10781952; DOI=10.1016/s0925-4773(00)00255-0;
RA Zuercher G., Rohrbach V., Andres A.-C., Ziemiecki A.;
RT "A novel member of the testis specific serine kinase family, tssk-3,
RT expressed in the Leydig cells of sexually mature mice.";
RL Mech. Dev. 93:175-177(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Testis;
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.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-168,
CC potentially by autophosphorylation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Developmentally expressed in testicular germ cells.
CC In adult testis, expression was detected in round and condensing
CC spermatids, but not in meiotic pachytene spermatocytes. Not expressed
CC in brain, ovary, kidney, liver or early embryonic cells.
CC {ECO:0000269|PubMed:10781952}.
CC -!- DEVELOPMENTAL STAGE: Expression begins 20-24 days after birth and is
CC maximal in the adult. The pattern of expression suggests that STK22D is
CC expressed postmeiotically.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: PubMed:10781952 has termed the gene 'STK22D' as it was then
CC thought that there were two different closely related genes.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF72581.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF298901; AAK97209.1; -; mRNA.
DR EMBL; AF201734; AAF72581.1; ALT_FRAME; mRNA.
DR EMBL; AK019840; BAB31876.1; -; mRNA.
DR EMBL; BC048470; AAH48470.1; -; mRNA.
DR CCDS; CCDS18693.1; -.
DR RefSeq; NP_536690.1; NM_080442.2.
DR AlphaFoldDB; Q9D2E1; -.
DR SMR; Q9D2E1; -.
DR BioGRID; 208450; 2.
DR STRING; 10090.ENSMUSP00000000421; -.
DR iPTMnet; Q9D2E1; -.
DR PhosphoSitePlus; Q9D2E1; -.
DR MaxQB; Q9D2E1; -.
DR PaxDb; Q9D2E1; -.
DR PeptideAtlas; Q9D2E1; -.
DR PRIDE; Q9D2E1; -.
DR ProteomicsDB; 298149; -.
DR Antibodypedia; 31305; 96 antibodies from 22 providers.
DR DNASU; 58864; -.
DR Ensembl; ENSMUST00000000421; ENSMUSP00000000421; ENSMUSG00000000411.
DR GeneID; 58864; -.
DR KEGG; mmu:58864; -.
DR UCSC; uc008uxc.1; mouse.
DR CTD; 81629; -.
DR MGI; MGI:1929914; Tssk3.
DR VEuPathDB; HostDB:ENSMUSG00000000411; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000161490; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q9D2E1; -.
DR OMA; KPGDAMK; -.
DR OrthoDB; 947464at2759; -.
DR PhylomeDB; Q9D2E1; -.
DR TreeFam; TF352374; -.
DR BioGRID-ORCS; 58864; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q9D2E1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D2E1; protein.
DR Bgee; ENSMUSG00000000411; Expressed in seminiferous tubule of testis and 10 other tissues.
DR Genevisible; Q9D2E1; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR CDD; cd14163; STKc_TSSK3-like; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR042709; TSSK3_STKc.
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.
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..268
FT /note="Testis-specific serine/threonine-protein kinase 3"
FT /id="PRO_0000086771"
FT DOMAIN 10..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 268 AA; 30209 MW; 4D4B8CE69BCA6705 CRC64;
MEDFLLSNGY QLGKTIGEGT YSKVKEAFSK KHQRKVAIKI IDKMGGPEEF IQRFLPRELQ
IVRTLDHKNI IQVYEMLESA DGKIYLVMEL AEGGDVFDCV LNGGPLPESR AKALFRQMVE
AIRYCHGCGV AHRDLKCENA LLQGFNLKLT DFGFAKVLPK SRRELSQTFC GSTAYAAPEV
LQGIPHDSKK GDVWSMGVVL YVMLCASLPF DDTDIPKMLW QQQKGVSFPT HLGISTECQD
LLKRLLEPDM ILRPSIEEVS WHPWLAST
