ID   KCRT_ONCMY              Reviewed;         383 AA.
AC   P24722;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Creatine kinase, testis isozyme;
DE            EC=2.7.3.2;
GN   Name=tck1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=2223887; DOI=10.1016/0167-4781(90)90215-n;
RA   Garber A.T., Winkfein R.J., Dixon G.H.;
RT   "A novel creatine kinase cDNA whose transcript shows enhanced testicular
RT   expression.";
RL   Biochim. Biophys. Acta 1087:256-258(1990).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC       and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC       isoenzymes play a central role in energy transduction in tissues with
CC       large, fluctuating energy demands, such as skeletal muscle, heart,
CC       brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=creatine + ATP = N-phosphocreatine + ADP + H(+);
CC         Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10029};
CC   -!- TISSUE SPECIFICITY: Exists in many tissues, but preferentially in
CC       testis. {ECO:0000269|PubMed:2223887}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
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DR   EMBL; X53859; CAA37852.1; -; mRNA.
DR   PIR; S13164; S13164.
DR   RefSeq; NP_001118187.1; NM_001124715.2.
DR   AlphaFoldDB; P24722; -.
DR   SMR; P24722; -.
DR   GeneID; 100136767; -.
DR   KEGG; omy:100136767; -.
DR   OrthoDB; 430219at2759; -.
DR   Proteomes; UP000694395; Unplaced.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR   CDD; cd00716; creatine_kinase_like; 1.
DR   FunFam; 3.30.590.10:FF:000026; Creatine kinase B-type; 1.
DR   FunFam; 1.10.135.10:FF:000001; Creatine kinase M-type; 1.
DR   Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF23; CREATINE KINASE B-TYPE; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..383
FT                   /note="Creatine kinase, testis isozyme"
FT                   /id="PRO_0000211984"
FT   DOMAIN          14..100
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          127..369
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         322..327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   383 AA;  43004 MW;  608BAAA115C7D1EA CRC64;
     MEKINDKMAK LTIKRLSPEE EFPDLSQHNN HMAKVLTQDM YTKLRDRATP NGFTIDGVIQ
     TGIDNPGHPF IMTVGCVAGD EETYEVFKEL LDPIIEDRHG GYKPTDKHKT DLNPDNLKGG
     DDLDPNYVIS SRVRTGRSIR GFCLPPHCSR GERRGVEKMS VEALDSLSGD LKGKYYALKN
     MTDAEQQQLI DDHFLFDKPV SPLLLASGMA RDWPDGRGIW HNDTKTFLVW VNEEDHLRVI
     SMQKGGNMKE VFNRFCTGLT KIETLFKDKG TSFMWNEHLG YVLTCPSNLG TGLRAGVHVK
     IPNISKHAKF EEVLKRLRLQ KRGTGGVDTA AVGGTFDISN ADRLGFSEVE LVQMVVDGVK
     LLVEMEKKLE KGQSIDDLMP AQK
//