ID   KAPL_APLCA              Reviewed;         351 AA.
AC   P21901;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Spermatozoon-associated protein kinase;
DE            Short=SAK;
DE            EC=2.7.11.1;
DE   AltName: Full=C-APL-B;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1701024; DOI=10.1128/mcb.10.12.6775-6780.1990;
RA   Beushausen S., Bayley H.;
RT   "A relative of the catalytic subunit of cyclic AMP-dependent protein kinase
RT   in Aplysia spermatozoa.";
RL   Mol. Cell. Biol. 10:6775-6780(1990).
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   -!- TISSUE SPECIFICITY: Ovotestis.
CC   -!- DEVELOPMENTAL STAGE: Concentrated in meiotic and postmeiotic
CC       spermatogenic cells.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP 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; M59380; AAA27745.1; -; mRNA.
DR   PIR; A36371; OKGASA.
DR   RefSeq; NP_001191474.1; NM_001204545.1.
DR   AlphaFoldDB; P21901; -.
DR   SMR; P21901; -.
DR   GeneID; 100533231; -.
DR   CTD; 100533231; -.
DR   OrthoDB; 963519at2759; -.
DR   BRENDA; 2.7.11.1; 390.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProt.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd14209; STKc_PKA; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
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; IPR044109; STKc_PKA.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..351
FT                   /note="Spermatozoon-associated protein kinase"
FT                   /id="PRO_0000086072"
FT   DOMAIN          42..298
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          299..351
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         48..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         198
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  40994 MW;  625719EA850006DB CRC64;
     MAHNQVFPES QKWLKEYLES SLEQFENLFN KNVISTESIR NYTLIRTLGS GSFGRVMLSQ
     HGGDNPQKCY AIKILNKEKV VKMKQVEHTM NEKRILLSIG SPFVVRCLNA FKDTTNLYMV
     MEFVNGGELF HLLRKKGRLP EYWCTFYAAQ VTMALQYLHN CSLLYRDLKP ENILLDHLGY
     LKVTDFGFDR RVQGHTWTLC GTPQYLAPEM ILNRSYASQW TTGGLGILIY ELNAGFVPFD
     HKVPLKLYEL IVECRLTFPS FFKPTLRDLL TNIIQVDVTR RFGNLRNGAL DIINHPWFKD
     TDFRKILMKA EKAPWVPNLK GQWIHQTFDK WTEESISISK HDKYPDEFSN F