ID SMK2B_MOUSE Reviewed; 484 AA.
AC Q9QYZ3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Sperm motility kinase 2B {ECO:0000312|MGI:MGI:3037705};
DE EC=2.7.11.1 {ECO:0000269|PubMed:10647005};
GN Name=Smok2b {ECO:0000312|MGI:MGI:3037705}; Synonyms=Gm1847;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv; 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 Evidence={ECO:0000269|PubMed:10647005};
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; Evidence={ECO:0000269|PubMed:10647005};
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; AJ245456; CAB61344.1; -; Genomic_DNA.
DR CCDS; CCDS49952.1; -.
DR RefSeq; NP_001161385.1; NM_001167913.2.
DR AlphaFoldDB; Q9QYZ3; -.
DR SMR; Q9QYZ3; -.
DR STRING; 10090.ENSMUSP00000124967; -.
DR GlyGen; Q9QYZ3; 1 site, 1 O-linked glycan (1 site).
DR PaxDb; 10090-ENSMUSP00000124967; -.
DR DNASU; 236574; -.
DR Ensembl; ENSMUST00000059824.7; ENSMUSP00000061516.7; ENSMUSG00000073457.5.
DR Ensembl; ENSMUST00000162940.3; ENSMUSP00000124967.2; ENSMUSG00000073457.5.
DR GeneID; 236574; -.
DR KEGG; mmu:236574; -.
DR UCSC; uc012akm.2; mouse.
DR AGR; MGI:3037705; -.
DR CTD; 236574; -.
DR MGI; MGI:3037705; Smok2b.
DR VEuPathDB; HostDB:ENSMUSG00000073457; -.
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000160886; -.
DR HOGENOM; CLU_000288_157_7_1; -.
DR InParanoid; Q9QYZ3; -.
DR OMA; ARRIFWQ; -.
DR OrthoDB; 1090327at2759; -.
DR PhylomeDB; Q9QYZ3; -.
DR TreeFam; TF338820; -.
DR BioGRID-ORCS; 236574; 1 hit in 77 CRISPR screens.
DR PRO; PR:Q9QYZ3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QYZ3; Protein.
DR Bgee; ENSMUSG00000073457; Expressed in testis and 7 other cell types or tissues.
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: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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR008271; Ser/Thr_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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..484
FT /note="Sperm motility kinase 2B"
FT /id="PRO_0000307868"
FT DOMAIN 8..256
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 272..314
FT /note="UBA"
FT REGION 356..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..450
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:PRU10027"
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; 54698 MW; C53B0ABEEB97364C CRC64;
MENFHAQYVM LETIGHGGCS KVMLARHRLT GSHVAVKMIR KSECWCNPVM SEVELLMMAD
HPNIISLLQV IETKKKVYLI MELCEGKSLY QHIRNAGYLQ EDEARALFKQ LLSAMNYCHN
QGIVHRDLKP DNIMVEKDGK VKIIDFGLGT QVKPGQKLNL FCGTYPFSAP EVLLSRPYDG
PKIDVWTLGV VLYFMVTGKV PFDAASIQKL VRQILAGKYF VPSRLSVELR DLISLLMTAN
PKLRPTVAEV MVHPWVTEGS GVFPDPCEEQ MPLKPNPAIV KAMGYIGFQA QDIEDSLRQR
KFNETMASYC LLKKQILKEC DRPIRAQPMN PSVTPFPSLV DTSTFHLGLR RRETEPTSLR
LSANRQMSVC GRSTSKKRDR RFSWPSVSGR PLHTTHTMDH THTRTRSVPC IYSMFCTIQP
NSSDDSTEGH TSASAEDKPV RSRGWPRGIK GWTRKIGNVM RKLCCCIPSK ETSHVGHSRV
SPKK
//
