SPE6_CAEEL
ID SPE6_CAEEL Reviewed; 379 AA.
AC Q95PZ9;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein kinase spe-6 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Defective spermatogenesis protein 6 {ECO:0000312|WormBase:Y66D12A.20};
GN Name=spe-6 {ECO:0000312|WormBase:Y66D12A.20};
GN ORFNames=Y66D12A.20 {ECO:0000312|WormBase:Y66D12A.20};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF SER-34; VAL-71;
RP GLY-90; CYS-98; ASP-106; SER-120; GLY-142; LEU-144; THR-194; SER-201;
RP ARG-211; SER-216; ARG-256; PRO-283 AND ALA-331.
RX PubMed=12019230; DOI=10.1093/genetics/161.1.143;
RA Muhlrad P.J., Ward S.;
RT "Spermiogenesis initiation in Caenorhabditis elegans involves a casein
RT kinase 1 encoded by the spe-6 gene.";
RL Genetics 161:143-155(2002).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF THR-194.
RX PubMed=8417991; DOI=10.1093/genetics/133.1.79;
RA Varkey J.P., Jansma P.L., Minniti A.N., Ward S.;
RT "The Caenorhabditis elegans spe-6 gene is required for major sperm protein
RT assembly and shows second site non-complementation with an unlinked
RT deficiency.";
RL Genetics 133:79-86(1993).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF VAL-71.
RX PubMed=29879108; DOI=10.1371/journal.pbio.2005069;
RA Zhao Y., Tan C.H., Krauchunas A., Scharf A., Dietrich N., Warnhoff K.,
RA Yuan Z., Druzhinina M., Gu S.G., Miao L., Singson A., Ellis R.E.,
RA Kornfeld K.;
RT "The zinc transporter ZIPT-7.1 regulates sperm activation in nematodes.";
RL PLoS Biol. 16:E2005069-E2005069(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase which is involved in
CC spermatogenesis (PubMed:12019230, PubMed:8417991, PubMed:29879108). In
CC spermatocytes, regulates meiosis and the localization and assembly of
CC major sperm protein (MSP) into fibrous bodies (PubMed:12019230,
CC PubMed:8417991). In addition, may suppress the initiation of
CC spermiogenesis downstream of spe-8, spe-12, spe-27 and spe-29
CC (PubMed:12019230). {ECO:0000269|PubMed:12019230,
CC ECO:0000269|PubMed:29879108, ECO:0000269|PubMed:8417991}.
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:0000305};
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:0000305};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BX284603; CAC70138.1; -; Genomic_DNA.
DR RefSeq; NP_499482.1; NM_067081.3.
DR AlphaFoldDB; Q95PZ9; -.
DR SMR; Q95PZ9; -.
DR STRING; 6239.Y66D12A.20; -.
DR EPD; Q95PZ9; -.
DR PaxDb; Q95PZ9; -.
DR EnsemblMetazoa; Y66D12A.20.1; Y66D12A.20.1; WBGene00004960.
DR GeneID; 176582; -.
DR KEGG; cel:CELE_Y66D12A.20; -.
DR CTD; 176582; -.
DR WormBase; Y66D12A.20; CE28799; WBGene00004960; spe-6.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_5_1; -.
DR InParanoid; Q95PZ9; -.
DR OMA; ANNFCIG; -.
DR OrthoDB; 810695at2759; -.
DR PhylomeDB; Q95PZ9; -.
DR PRO; PR:Q95PZ9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004960; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0051308; P:male meiosis chromosome separation; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048515; P:spermatid differentiation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Differentiation; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Spermatogenesis;
KW Transferase.
FT CHAIN 1..379
FT /note="Serine/threonine-protein kinase spe-6"
FT /id="PRO_0000432625"
FT DOMAIN 26..302
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 331..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..355
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 BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 34
FT /note="S->P: In hc167; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 71
FT /note="V->E: In hc163; low fertility affecting males more
FT severely. Mild defect in the initial formation of fibrous
FT bodies-membranous organelles structures in spermatocytes.
FT Precocious initiation of spermiogenesis but with few
FT spermatids maturing into spermatozoa. Restores fertility in
FT spe-8, spe-12, spe-27 or spe-29 mutants by rescuing
FT initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 71
FT /note="V->E: In hc163; premature spermatid activation in
FT spermathecae. Premature spermatid activation in
FT spermathecae is suppressed in a zipt-7.1 mutant (ok971)
FT background."
FT /evidence="ECO:0000269|PubMed:29879108"
FT MUTAGEN 90
FT /note="G->D: In hc174; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 98
FT /note="C->Y: In hc175; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 106
FT /note="D->N: In hc186; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 120
FT /note="S->F: In hc189; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 142
FT /note="G->E: In hc164, hc176 and hc187; restores fertility
FT in spe-27 mutants by rescuing initiation of
FT spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 144
FT /note="L->F: In hc168; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 194
FT /note="T->I: In hc92 and hc143; sterile. Failure to
FT assemble MSP into fibrous bodies and absence of spermatids
FT due to spermatocytes arresting at the diakinesis stage."
FT /evidence="ECO:0000269|PubMed:12019230,
FT ECO:0000269|PubMed:8417991"
FT MUTAGEN 201
FT /note="S->F: In hc173; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 211
FT /note="R->Q: In hc165; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 216
FT /note="S->N: In hc188; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 256
FT /note="R->Q: In hc166; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 283
FT /note="P->S: In hc169; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT MUTAGEN 331
FT /note="A->V: In hc172; restores fertility in spe-27 mutants
FT by rescuing initiation of spermiogenesis."
FT /evidence="ECO:0000269|PubMed:12019230"
FT CONFLICT 1..9
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42987 MW; 89545B584AA58E5D CRC64;
MSEQRDSRGM PQAGFIIEHQ SSDHKWKVLR NIYSGPFSDV YVVADTVTNE KYAMKCERQE
GNSRPVLKLD VMVLMATKGL RGFPNFVAAG RTDVYRYCIM QLVGPDLGRL RRTRPERKFS
LPTALQILGQ TLRRLEDLHN CGWLCRDVKA PNFCIGVGEN ESTVYILDFG FARKFVDKEG
KIIPPRTAAA LMGTFQYCAV SAHSHKDQCA RDDLESWFYM GIELLKGPLP WANIDGHKNH
KQIGEAKVAI RSEPLRSEFF EGVPKQFNEI LTILDQTSYF DRPNYKKLGD LLSQAATEHQ
VTLKEPLDWQ NNERMQQKAI FVGELGESHQ ASAKLDAKDN ANESMDIEFD DMPPKEGISK
SLSAEKSCTK NVETARTEK
