SMKTR_MOUSE
ID SMKTR_MOUSE Reviewed; 484 AA.
AC A2KF29;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Sperm motility kinase Tcr mutant form;
DE Short=SmokTcr;
DE Short=Tcr;
DE EC=2.7.11.1;
DE AltName: Full=Dominant negative form of Smok;
DE AltName: Full=Responder protein Smok-Tcr;
GN Name=Smoktcr;
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: While the main function of Smoks is to control sperm
CC motility, the role of Smok-Tcr, with reduced kinase activity, is to
CC counterbalance a signaling impairment caused by the distorter/sterility
CC loci, giving t-sperm an advantage in reaching the oocytes. Transmission
CC ratio distortion also called segregation distortion is the name given
CC to the phenomenon above-mentioned. Being associated with the T-complex,
CC it allows males heterozygous for a complete t-haplotype to
CC preferentially transmit the t-haplotype chromosome.
CC {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). Expressed late in spermiogenesis, only in
CC Tcr-containing t-haplotypes. {ECO:0000269|PubMed:10647005}.
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 -!- MISCELLANEOUS: T6 allele.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Smok subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although it is derived from a rearrangement with the
CC neighboring RSK3 gene, it plays a crucial role in t-haplotype cells.
CC {ECO:0000305}.
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DR EMBL; AJ245452; CAB61340.1; -; mRNA.
DR AlphaFoldDB; A2KF29; -.
DR SMR; A2KF29; -.
DR PRIDE; A2KF29; -.
DR InParanoid; A2KF29; -.
DR PRO; PR:A2KF29; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A2KF29; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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 Tcr mutant form"
FT /id="PRO_0000307873"
FT DOMAIN 8..256
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 355..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..446
FT /note="Disordered"
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; 54619 MW; A84F3BDCE420C973 CRC64;
MEKFHAQYEM LETIGQGGCA QVKLARHRLT GTHVAVKVIV KRECWFNPVM SEAELLMMTD
HPNIISLLQV IETKKKVYLI MELCEGKSLY QHIQNAGYLQ EDEARPLFKQ LLSAMNYCHN
QGIVHRDLTP DNIMVEKDGK VKIIDFGLGT QEKPGQNHNL FCEIYPFSTP EVLFNRPYDM
RKIDVWGLGV VLYFMVTGKI LFDTASVEKL RKQIVAEKCS VPCRLSVELQ DLIRLLMTDI
PELRPTVAEV MVHPWVTEGS GVLPDPCEEH IPLKPDPAIA KAMGFIGFQA QDIEDSLCQR
KFNETMASYC LLKKQILKEC DRPIRAQPMN PSVTPLSSLV DAPTFHLGLR RTETEPTGLR
LSDNKEVPVC GNSTSKKRER SFSGPGVLSR PINTTPTMDQ THTRTWSGPC IYSNVCTIHP
NSINESTEGH ISTSAEDKPV HSRGWPRGIK GWTRKIGNAM RKLCCCIPSK ETSHLGQRRV
CPKI
