SMKY_MOUSE
ID SMKY_MOUSE Reviewed; 508 AA.
AC A0AUV4; Q3B7Y1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sperm motility kinase Y;
DE EC=2.7.11.1;
GN Name=Gm7168;
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 [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role in sperm motility, especially in the
CC regulation of flagellar function. {ECO:0000250}.
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 -!- 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; BC107382; AAI07383.1; -; mRNA.
DR EMBL; BC125014; AAI25015.1; -; mRNA.
DR EMBL; BC125267; AAI25268.1; -; mRNA.
DR CCDS; CCDS49956.1; -.
DR RefSeq; NP_001116449.1; NM_001122977.1.
DR AlphaFoldDB; A0AUV4; -.
DR SMR; A0AUV4; -.
DR STRING; 10090.ENSMUSP00000094997; -.
DR PaxDb; A0AUV4; -.
DR PRIDE; A0AUV4; -.
DR DNASU; 635895; -.
DR GeneID; 635895; -.
DR KEGG; mmu:635895; -.
DR UCSC; uc008amu.1; mouse.
DR MGI; MGI:3643198; Gm7168.
DR eggNOG; KOG0586; Eukaryota.
DR InParanoid; A0AUV4; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; A0AUV4; -.
DR TreeFam; TF338820; -.
DR BioGRID-ORCS; 635895; 1 hit in 67 CRISPR screens.
DR ChiTaRS; Gm7168; mouse.
DR PRO; PR:A0AUV4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A0AUV4; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..508
FT /note="Sperm motility kinase Y"
FT /id="PRO_0000307876"
FT DOMAIN 28..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 294..334
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro 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"
FT CONFLICT 414
FT /note="A -> P (in Ref. 1; AAI07383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 57058 MW; 82E035C7F5BBF12C CRC64;
MPAHIEEELP PPSPQPSNPE DGELYSQYKV VRTLGHGTYA KVLLAKHWLT GTPVAVKVLL
KNKPCFQPAM KEANIMKKIK HPNIVSLLQV FETKTRGYLI MELVEGQELY EYIKSSGHIE
EDEARQIFLQ ILSAVSYCHG LGIVHRDLKP DNIMIDDKGS IKIIDFGLST QVKPGDLLDE
HCGAYAFGAP ELFLWKSYDG TKSDLWALGV ILYYMVVGKV PFDSYIIPEL QRQILAGVYP
APCGVSNELK DLLSLLMTVN PKYRPTVTEV MKHPWLRGHC KGLTNIHEEP VPVRPDPDIV
DAMQYIGFQA KDIRESLTKE KFNEMSAAYY LLEEQALQRE VRSTQAPTVS QVKAPFPSMD
AGEASCLKIK RSGSASILGR SVWPPSIDQE PAYVQKVRQR AGRRSSGHGL LFEANQMTPT
QDQHHIRAMS VPCMLSTSSI SEESVSEKRE ENLSHIALAE DKPIRSRGWC RGIMRWTRRV
GNAIRTLCCC IPSRKTPQLG QSRVSPQK
