SPE8_CAEEL
ID SPE8_CAEEL Reviewed; 512 AA.
AC O01798;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Spermatocyte protein spe-8 {ECO:0000305};
DE EC=2.7.10.2;
DE AltName: Full=Defective spermatogenesis protein spe-8 {ECO:0000312|WormBase:F53G12.6};
GN Name=spe-8 {ECO:0000312|WormBase:F53G12.6};
GN ORFNames=F53G12.6 {ECO:0000312|WormBase:F53G12.6};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=25022984; DOI=10.1186/1471-2156-15-83;
RA Muhlrad P.J., Clark J.N., Nasri U., Sullivan N.G., LaMunyon C.W.;
RT "SPE-8, a protein-tyrosine kinase, localizes to the spermatid cell membrane
RT through interaction with other members of the SPE-8 group spermatid
RT activation signaling pathway in C. elegans.";
RL BMC Genet. 15:83-83(2014).
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 SER-150; GLY-229; VAL-231; GLY-405 AND
RP ARG-465.
RX PubMed=3197956; DOI=10.1093/genetics/120.2.435;
RA L'Hernault S.W., Shakes D.C., Ward S.;
RT "Developmental genetics of chromosome I spermatogenesis-defective mutants
RT in the nematode Caenorhabditis elegans.";
RL Genetics 120:435-452(1988).
CC -!- FUNCTION: Probable non-receptor tyrosine-protein kinase which plays a
CC role in spermatid activation (spermiogenesis) in hermaphrodites.
CC {ECO:0000269|PubMed:25022984, ECO:0000269|PubMed:3197956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25022984};
CC Peripheral membrane protein {ECO:0000269|PubMed:25022984}. Cytoplasm
CC {ECO:0000269|PubMed:25022984}. Note=Localizes mainly in the cytoplasm
CC of stage I spermatocytes and at the cell membrane of stage II
CC spermatocytes and spermatids. {ECO:0000269|PubMed:25022984}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to male germline.
CC {ECO:0000269|PubMed:25022984}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000305}.
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DR EMBL; BX284601; CCD71705.1; -; Genomic_DNA.
DR PIR; T29030; T29030.
DR RefSeq; NP_490680.1; NM_058279.1.
DR AlphaFoldDB; O01798; -.
DR SMR; O01798; -.
DR STRING; 6239.F53G12.6; -.
DR PaxDb; O01798; -.
DR EnsemblMetazoa; F53G12.6.1; F53G12.6.1; WBGene00004962.
DR GeneID; 171606; -.
DR KEGG; cel:CELE_F53G12.6; -.
DR UCSC; F53G12.6; c. elegans.
DR CTD; 171606; -.
DR WormBase; F53G12.6; CE29331; WBGene00004962; spe-8.
DR eggNOG; KOG0194; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; O01798; -.
DR OMA; KFYGVAT; -.
DR OrthoDB; 685240at2759; -.
DR PhylomeDB; O01798; -.
DR PRO; PR:O01798; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004962; Expressed in material anatomical entity and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:WormBase.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cytoplasm; Differentiation; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; SH2 domain; Spermatogenesis;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..512
FT /note="Spermatocyte protein spe-8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433988"
FT DOMAIN 114..205
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 217..485
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 223..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 150
FT /note="S->N: In hc134ts; temperature-sensitive self-
FT sterility in hermaphrodites but normal male fertility."
FT /evidence="ECO:0000269|PubMed:3197956"
FT MUTAGEN 229
FT /note="G->R: In hc79; self-sterility in hermaphrodites but
FT normal male fertility."
FT /evidence="ECO:0000269|PubMed:3197956"
FT MUTAGEN 231
FT /note="V->M: In hc53; self-sterility in hermaphrodites but
FT normal male fertility."
FT /evidence="ECO:0000269|PubMed:3197956"
FT MUTAGEN 405
FT /note="G->D: In hc108; self-sterility in hermaphrodites but
FT normal male fertility."
FT /evidence="ECO:0000269|PubMed:3197956"
FT MUTAGEN 465
FT /note="R->H: In hc40; self-sterility in hermaphrodites but
FT normal male fertility."
FT /evidence="ECO:0000269|PubMed:3197956"
SQ SEQUENCE 512 AA; 57802 MW; E6B44EB28C1D7EB1 CRC64;
MRSKSSEGDL QPEDTQSRED KETTATYSED TKPETQKERN AALDNLAKTP IQLVVQPTPL
TPAITPCEAP PPPPPPKPSS DNNNSKRLKV KDQLIEVPSD EVGRVENNID NFPFYHGFMG
RNECEAMLSN HGDFLIRMTE IGKRVAYVIS IKWKYQNIHV LVKRTKTKKL YWTKKYAFKS
ICELIAYHKR NHKPIYEGMT LICGLARHGW QLNNEQVTLN KKLGEGQFGE VHKGSLKTSV
FAAPVTVAVK TLHQNHLSAN EKILFLREAN VMLTLSHPNV IKFYGVCTMK EPIMIVMEFC
DGKSLEDALL SKEEKVSAED KILYLFHAAC GIDYLHGKQV IHRDIAARNC LLNSKKILKI
SDFGLSVKGV AIKERKGGCL PVKYMAPETL KKGLYSTASD IYSYGALMYE VYTDGKTPFE
TCGLRGNELR KAIIGKRISL AVEVELPVFI ANIFEQSRQY ETEDRISSKQ IIQIFKEEVG
FHEIETSGIL HKLVNSLPRI HNKERKPAAV AV
