SMK2A_MOUSE
ID SMK2A_MOUSE Reviewed; 504 AA.
AC Q9QYZ6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sperm motility kinase 2A;
DE EC=2.7.11.1;
GN Name=Smok2a;
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 STRAIN=BALB/cJ; 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: 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. CAMK Ser/Thr
CC protein kinase family. Smok subfamily. {ECO:0000305}.
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DR EMBL; AJ245453; CAB61341.1; -; mRNA.
DR CCDS; CCDS49951.1; -.
DR AlphaFoldDB; Q9QYZ6; -.
DR SMR; Q9QYZ6; -.
DR STRING; 10090.ENSMUSP00000094432; -.
DR iPTMnet; Q9QYZ6; -.
DR PhosphoSitePlus; Q9QYZ6; -.
DR PaxDb; Q9QYZ6; -.
DR PRIDE; Q9QYZ6; -.
DR ProteomicsDB; 261440; -.
DR MGI; MGI:1351487; Smok2a.
DR eggNOG; KOG0586; Eukaryota.
DR InParanoid; Q9QYZ6; -.
DR PhylomeDB; Q9QYZ6; -.
DR ChiTaRS; Smok2a; mouse.
DR PRO; PR:Q9QYZ6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QYZ6; 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: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; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..504
FT /note="Sperm motility kinase 2A"
FT /id="PRO_0000307869"
FT DOMAIN 28..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 294..334
FT /note="UBA"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 504 AA; 56787 MW; 596F27F4804902C8 CRC64;
MGSGSQQKSE KLRSKPPFSE MENFHAQYEM LGTIGHGGST KVKLARHRLT GTHVAVKMIP
KREYWCKPLM SEAELLMMAD HPNIISLLQV IETKKKVYLI MELCEGKSLY QHIRNAGYLQ
EDEARALFKQ LLSAINYCRN QGIVHRDLKP DNIMVEKDGR VKIIDFGLGI QVKPGQKLNL
FCGTYPFSAP EVLLSRPYDG PKIDVWTLGV VLYFMVTGKI PFDAASIEKL RKQIVAGKYS
VPCRLSVKLH HLITLLMTDN PELRPTVAEV MMHPWVTKGS GVFPDPCEEQ IPLKPDPAIV
KAMGHIGFQA QDIEDSLRQR KFNETMASYC LLKKQLLKEC DRPIRAQPMN PSVTPFPSLV
DTPTFHLGLR RRETEPTSLR LSANRQMSVC GRSTSKKRDR SFSWPGVLSR PINITPTMDQ
THTCTRSVPC INSNFCIIHP NSSDESTEGH TSASAEDKPV RSRGWPRGIK GWTSKIGNAM
RKLCCCIPSN ETSHLGQRRV SPKK
