ID   SPE8_CAEBR              Reviewed;         479 AA.
AC   A8WZ92;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 96.
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:CBG05099};
GN   Name=spe-8 {ECO:0000312|WormBase:CBG05099};
GN   ORFNames=CBG05099 {ECO:0000312|WormBase:CBG05099};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN   [1] {ECO:0000312|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP25702.2,
RC   ECO:0000312|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=25523309; DOI=10.1038/ncomms6888;
RA   Wei Q., Zhao Y., Guo Y., Stomel J., Stires R., Ellis R.E.;
RT   "Co-option of alternate sperm activation programs in the evolution of self-
RT   fertile nematodes.";
RL   Nat. Commun. 5:5888-5888(2014).
CC   -!- FUNCTION: Probable non-receptor tyrosine-protein kinase which plays a
CC       role in spermatid activation (spermiogenesis) in hermaphrodites.
CC       {ECO:0000269|PubMed:25523309}.
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; Peripheral membrane protein.
CC       Cytoplasm. Note=Localizes mainly in the cytoplasm in stage I
CC       spermatocytes and at the cell membrane in stage II spermatocytes and in
CC       spermatids. {ECO:0000250|UniProtKB:O01798}.
CC   -!- TISSUE SPECIFICITY: Expressed in hermaphrodite larvae but not in adult.
CC       Expressed in both male larvae and adult. {ECO:0000269|PubMed:25523309}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE600988; CAP25702.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8WZ92; -.
DR   SMR; A8WZ92; -.
DR   STRING; 6238.CBG05099; -.
DR   WormBase; CBG05099; CBP31785; WBGene00027634; Cbr-spe-8.
DR   eggNOG; KOG0194; Eukaryota.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; A8WZ92; -.
DR   OMA; KFYGVAT; -.
DR   OrthoDB; 685240at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
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: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:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript 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..479
FT                   /note="Spermatocyte protein spe-8"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433987"
FT   DOMAIN          119..208
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          209..450
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         146..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   479 AA;  54291 MW;  8372AB2DF846CCA2 CRC64;
     MSGVELQPES TQSEEKEEPK TAATTISSTE ETKTENPNVA LDNLAKTPIQ LILQPTPQTP
     AKTPETPRIQ KINNLKKSAS FDSKNQPEDS KTPKQRDQLI EVPSDEVGRV ENNIDNLPFY
     HGFMGRTECE SMLSNHGDFL IRMTEVGRRV AYVISVRWHY QNSHVLVKRT KTKKLYWTKK
     YAFKSICELI AYHKLNQIPF YDNMTLICGL ARHEWQLNNE QVTLNKKLGE GQFGEVHKGK
     LKPNVIKFYG VCTMKEPIMI VMEFCDGSSL EDVLLSKESK VSSEDKILYL FHAACGIDYL
     HGKHVIHRDI AARNCLLNSK KVLKISDFGL SVKGVAIKER KGGCLPVKYM APETLKKGFY
     STASDIYSYG ALVYEVYTDG KTPFESCGLR GNELRKAIIG KSVILTIDVE CPEFVKAIFE
     QSRLYDTEQR ISSKRIIEIF KEEAGMHELD ATGLFGRIGS FFSRVRRQKE AEPSVPILT