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   03-AUG-2022, entry version 105.
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}.
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DR   EMBL; AJ245455; CAB61343.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9QYZ4; -.
DR   SMR; Q9QYZ4; -.
DR   PRIDE; Q9QYZ4; -.
DR   MGI; MGI:1351488; Smok1.
DR   InParanoid; Q9QYZ4; -.
DR   PRO; PR:Q9QYZ4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9QYZ4; protein.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 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