ID Q7ZX84_XENLA Unreviewed; 418 AA.
AC Q7ZX84;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=ckmt1b.S {ECO:0000313|RefSeq:NP_001080463.1,
GN ECO:0000313|RefSeq:XP_018109560.1,
GN ECO:0000313|Xenbase:XB-GENE-6254065};
GN Synonyms=ckmt {ECO:0000313|RefSeq:XP_018109560.1}, ckmt1
GN {ECO:0000313|RefSeq:XP_018109560.1}, ckmt1b
GN {ECO:0000313|Xenbase:XB-GENE-6254065}, ckmt1b-a
GN {ECO:0000313|RefSeq:XP_018109560.1}, ckmt1b-b
GN {ECO:0000313|RefSeq:NP_001080463.1,
GN ECO:0000313|RefSeq:XP_018109560.1}, ckmt1b.L
GN {ECO:0000313|RefSeq:NP_001080463.1,
GN ECO:0000313|RefSeq:XP_018109560.1}, umtck
GN {ECO:0000313|RefSeq:XP_018109560.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH45123.1};
RN [1] {ECO:0000313|RefSeq:NP_001080463.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH45123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH45123.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001080463.1, ECO:0000313|RefSeq:XP_018109560.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018109560.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018109560.1};
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; BC045123; AAH45123.1; -; mRNA.
DR RefSeq; NP_001080463.1; NM_001086994.1.
DR RefSeq; XP_018109560.1; XM_018254071.2.
DR DNASU; 380155; -.
DR GeneID; 380155; -.
DR KEGG; xla:380155; -.
DR AGR; Xenbase:XB-GENE-6254065; -.
DR CTD; 380155; -.
DR Xenbase; XB-GENE-6254065; ckmt1b.S.
DR OrthoDB; 35839at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 380155; Expressed in camera-type eye and 15 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
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 2: Evidence at transcript 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}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
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 418 AA; 46857 MW; 6BDB8930C6E278ED CRC64;
MASTFSRILS SRKSAGLLAM VGAGSVATGY LMTRDAISAD TSHKRRMYPA SAEYPDLRKH
NNCMASSLTP AIYTKLCDKT TPAGFTLDEC IQTGVDNPGH PFIKTVGMVA GDEECYEVFG
DLFDPVIKER HNGYDPHTMK HPTDLDASKI KGGFFDERYV LSSRVRTGRS IRGLSLPPAC
TRAERREVEK VSVDALSGLK GDLSGQYYSL TQMTDKEQQQ LIDDHFLFDK PVSPLLTAAG
MARDWPDARG IWHNNEKTFL IWINEEDHTR IISMEKGGNM KRVFERFCRG LKEVEKLIQE
KGWEFMWNER LGYILTCPSN LGTGLRAGVH VNLPLLSKDA RFSKILENLR LQKRGTGGVD
TAAVGSTFDI SNLDRLGKSE VELVQMVIDG VNYLIDCEKR LERKQDIRVP APLSQFKH
//
