ID SMOK1_MOUSE Reviewed; 484 AA. AC Q9QYZ4; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=Sperm motility kinase 1; DE EC=2.7.11.1; GN Name=Smok1; 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 [GENOMIC DNA], TISSUE SPECIFICITY, AND FUNCTION. RC TISSUE=Testis; RX PubMed=10647005; DOI=10.1038/45970; RA Herrmann B.G., Koschorz B., Wertz K., McLaughlin K.J., Kispert A.; RT "A protein kinase encoded by the t complex responder gene causes non- RT Mendelian inheritance."; RL Nature 402:141-146(1999). CC -!- FUNCTION: May play a role in sperm motility, especially in the CC regulation of flagellar function. {ECO:0000269|PubMed:10647005}. 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 -!- TISSUE SPECIFICITY: Testis-specific. Expressed in the testis from 22 CC days postpartum (22 dpp). {ECO:0000269|PubMed:10647005}. CC -!- MISCELLANEOUS: Tw12 allele. CC -!- MISCELLANEOUS: Encoded on the T-complex, a region of 20-30 Mb on CC proximal third of mouse chromosome 17. Naturally occurring variant CC forms of the T-complex, known as complete t-haplotypes, are found in CC wild mouse populations. The t-haplotypes contain at least four CC nonoverlapping inversions that suppress recombination with the wild- CC type chromosome, and lock into strong linkage disequilibrium loci CC affecting normal transmission of the chromosome, male gametogenesis and CC embryonic development. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Smok subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; AJ245455; CAB61343.1; -; Genomic_DNA. DR AlphaFoldDB; Q9QYZ4; -. DR SMR; Q9QYZ4; -. DR AGR; MGI:1351488; -. DR MGI; MGI:1351488; Smok1. DR InParanoid; Q9QYZ4; -. DR PRO; PR:Q9QYZ4; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9QYZ4; Protein. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0004713; F:protein tyrosine kinase activity; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14003; STKc_AMPK-like; 1. DR CDD; cd14337; UBA_MARK_Par1; 1. 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; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF92; SPERM MOTILITY KINASE 3A; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. FT CHAIN 1..484 FT /note="Sperm motility kinase 1" FT /id="PRO_0000307870" FT DOMAIN 8..256 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 274..314 FT /note="UBA" FT REGION 423..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..444 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 127 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 14..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 37 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 484 AA; 54794 MW; 4244F91CF74D50AA CRC64; MEKFHAQYEM LETIGQGGCA KVKLARHRLT GTHVAVKMIP KREYWCKLLM FEAELLMMFN HPNIISLLQV IETKKKVYLI MELCEGKSLY QHIQNAGYLQ EDEARPLFKQ LLSAMNYCHN QGIVHRDLTP DNIMVEKDGR VKNIDFGLST HVKPGQKLNL FCGTYPFSAP EVLLSRPYGG PKIDVWTLGV VLYFMVIGKI PFDAASIEKL RKQIVAGKYS APCRLSVKLQ HLINLLMTDN PELRPTVAEV MVHPWITKGS GVFPDPCEEQ IPLKPDPAIV KPMGHIGFQA QDIEDSLRQR KFNETMASYC LLKKQILKEC DRPIRDQPMN PSVTPFPSLV DTPTFHLGLR RRETEPTGLR LSANRQVSVC GKSTSKKRDR SFIWPGVLSR PINTTPTMDQ THTRTRSVPC IYSNVCTIHP NSIDESTEGH TSASAEDKPV HSRGWPRGIK GWTRKIGNAM RKLCCCIPSK ETSHLGQSRV CPKK //