ID   Q7ZUN7_DANRE            Unreviewed;       417 AA.
AC   Q7ZUN7; A0A2R8PZ48; B2GSL6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Creatine kinase U-type, mitochondrial {ECO:0000256|ARBA:ARBA00039465};
DE            EC=2.7.3.2 {ECO:0000256|ARBA:ARBA00012231};
DE   AltName: Full=Acidic-type mitochondrial creatine kinase {ECO:0000256|ARBA:ARBA00041417};
DE   AltName: Full=Ubiquitous mitochondrial creatine kinase {ECO:0000256|ARBA:ARBA00041802};
GN   Name=ckmt1 {ECO:0000313|EMBL:AAI65565.1,
GN   ECO:0000313|Ensembl:ENSDARP00000011271,
GN   ECO:0000313|RefSeq:NP_942096.1, ECO:0000313|RefSeq:XP_021326125.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-611};
GN   Synonyms=fb37h03 {ECO:0000313|RefSeq:NP_942096.1,
GN   ECO:0000313|RefSeq:XP_021326125.1}, fb69a12
GN   {ECO:0000313|RefSeq:NP_942096.1, ECO:0000313|RefSeq:XP_021326125.1},
GN   wu:fb69a12 {ECO:0000313|RefSeq:NP_942096.1,
GN   ECO:0000313|RefSeq:XP_021326125.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI65565.1};
RN   [1] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=18046332; DOI=10.1038/nature06349;
RA   Hart D.O., Raha T., Lawson N.D., Green M.R.;
RT   "Initiation of zebrafish haematopoiesis by the TATA-box-binding protein-
RT   related factor Trf3.";
RL   Nature 450:1082-1085(2007).
RN   [2] {ECO:0000313|EMBL:AAI65565.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB {ECO:0000313|EMBL:AAH48050.1};
RC   TISSUE=PCR rescue {ECO:0000313|EMBL:AAI65565.1}, and Whole body
RC   {ECO:0000313|EMBL:AAH48050.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=20528263;
RA   Singh S.K., Sundaram C.S., Shanbhag S., Idris M.M.;
RT   "Proteomic profile of zebrafish brain based on two-dimensional gel
RT   electrophoresis matrix-assisted laser desorption/ionization MS/MS
RT   analysis.";
RL   Zebrafish 7:169-177(2010).
RN   [4] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=21756345;
RA   Hensley M.R., Emran F., Bonilla S., Zhang L., Zhong W., Grosu P.,
RA   Dowling J.E., Leung Y.F.;
RT   "Cellular expression of Smarca4 (Brg1)-regulated genes in zebrafish
RT   retinas.";
RL   BMC Dev. Biol. 11:45-45(2011).
RN   [5] {ECO:0000313|Ensembl:ENSDARP00000011271}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000011271};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [6] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=23557786;
RA   Zhang Y., Bonilla S., Chong L., Leung Y.F.;
RT   "Irx7, a Smarca4-regulated gene for retinal differentiation, regulates
RT   other genes controlled by Smarca4 in zebrafish retinas.";
RL   Gene Expr. Patterns 13:177-182(2013).
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000011271, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000011271};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [8] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [9] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=27031468;
RA   Ebrahimie E., Moussavi Nik S.H., Newman M., Van Der Hoek M., Lardelli M.;
RT   "The Zebrafish Equivalent of Alzheimer's Disease-Associated PRESENILIN
RT   Isoform PS2V Regulates Inflammatory and Other Responses to Hypoxic
RT   Stress.";
RL   J. Alzheimers Dis. 52:581-608(2016).
RN   [10] {ECO:0000313|RefSeq:NP_942096.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1};
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [11] {ECO:0000313|Ensembl:ENSDARP00000146491}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000146491};
RG   Ensembl;
RL   Submitted (APR-2018) to UniProtKB.
RN   [12] {ECO:0000313|RefSeq:NP_942096.1, ECO:0000313|RefSeq:XP_021326125.1}
RP   IDENTIFICATION.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_942096.1}, and Tuebingen
RC   {ECO:0000313|RefSeq:XP_021326125.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037274}.
CC   -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC       {ECO:0000256|ARBA:ARBA00038753}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC       {ECO:0000256|ARBA:ARBA00004137}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842,
CC       ECO:0000256|RuleBase:RU000505}.
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DR   EMBL; CR450696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR788324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC048050; AAH48050.1; -; mRNA.
DR   EMBL; BC165565; AAI65565.1; -; mRNA.
DR   RefSeq; NP_942096.1; NM_198801.1.
DR   RefSeq; XP_021326125.1; XM_021470450.1.
DR   STRING; 7955.ENSDARP00000011271; -.
DR   PaxDb; 7955-ENSDARP00000011271; -.
DR   Ensembl; ENSDART00000027393.8; ENSDARP00000011271.6; ENSDARG00000016598.8.
DR   Ensembl; ENSDART00000187606.1; ENSDARP00000154305.1; ENSDARG00000016598.8.
DR   Ensembl; ENSDART00000192731.1; ENSDARP00000146491.1; ENSDARG00000113143.1.
DR   GeneID; 321892; -.
DR   KEGG; dre:321892; -.
DR   AGR; ZFIN:ZDB-GENE-030131-611; -.
DR   CTD; 12716; -.
DR   ZFIN; ZDB-GENE-030131-611; ckmt1.
DR   eggNOG; KOG3581; Eukaryota.
DR   HOGENOM; CLU_019868_4_2_1; -.
DR   OMA; CTMKHHT; -.
DR   OrthoDB; 35839at2759; -.
DR   TreeFam; TF314214; -.
DR   Reactome; R-DRE-71288; Creatine metabolism.
DR   Proteomes; UP000000437; Alternate scaffold 25.
DR   Proteomes; UP000000437; Chromosome 25.
DR   Bgee; ENSDARG00000016598; Expressed in intestine and 22 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00716; creatine_kinase_like; 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:SF24; CREATINE KINASE U-TYPE, MITOCHONDRIAL; 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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00843};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00843};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00843};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q7ZUN7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00843}.
FT   DOMAIN          45..132
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51509"
FT   DOMAIN          159..401
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51510"
FT   BINDING         162..166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         326..330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
FT   BINDING         354..359
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00843"
SQ   SEQUENCE   417 AA;  46706 MW;  804420E5AE3CE4D5 CRC64;
     MASSFARILS GNRKVGILSL VGAGSLTVGF FLNREQHVSA GSSVRRIYPP SAEYPDLRKH
     NNCMASHLTP AVYAKLCDKS TPNGYTLDEA IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
     DIFNPVIKER HNGYDPCNMK HPTDLDSSKI RGGMFDEKYV LSSRVRTGRS IRGLSLPPAC
     TRAERREVER VVVDALAGLK GDLTGKYYSL TVMTEQEQQQ LIDDHFLFDK PVSPLLTCAG
     MARDWPDARG IWHNNEKTFL VWINEEDHTR VISMEKGGNM RRVFERFCKG LQEVERLIQE
     KGWEFMWNER LGYILTCPSN LGTGLRAGVH VNLPRLSKDP RFSKILDNLR LQKRGTGGVD
     TAAVGSTFDI SNLDRLGQSE VQLVQTVIDG VNYLIECERK LEKGQDIKIP APISQFK
//