ID KCRB_BOVIN Reviewed; 381 AA. AC Q5EA61; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=Creatine kinase B-type; DE EC=2.7.3.2; DE AltName: Full=B-CK; DE AltName: Full=Creatine kinase B chain; DE AltName: Full=Creatine phosphokinase M-type; DE Short=CPK-B; GN Name=CKB; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 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. Acts as a key regulator of adaptive CC thermogenesis as part of the futile creatine cycle: localizes to the CC mitochondria of thermogenic fat cells and acts by mediating CC phosphorylation of creatine to initiate a futile cycle of creatine CC phosphorylation and dephosphorylation. During the futile creatine CC cycle, creatine and N-phosphocreatine are in a futile cycle, which CC dissipates the high energy charge of N-phosphocreatine as heat without CC performing any mechanical or chemical work. CC {ECO:0000250|UniProtKB:Q04447}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; 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:0000250|UniProtKB:Q04447, ECO:0000255|PROSITE- CC ProRule:PRU10029}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158; CC Evidence={ECO:0000250|UniProtKB:Q04447}; CC -!- SUBUNIT: Dimer of identical or non-identical chains, which can be CC either B (brain type) or M (muscle type). With MM being the major form CC in skeletal muscle and myocardium, MB existing in myocardium, and BB CC existing in many tissues, especially brain (By similarity). Interacts CC with SLC12A6 (via C-terminus); the interaction may be required for CC SLC12A6 potassium-chloride cotransport activity (By similarity). CC {ECO:0000250|UniProtKB:P12277}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q04447}. Mitochondrion CC {ECO:0000250|UniProtKB:Q04447}. Cell membrane CC {ECO:0000250|UniProtKB:P12277}. Note=Localizes to the mitochondria of CC thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. CC {ECO:0000250|UniProtKB:Q04447}. CC -!- DOMAIN: The internal MTS-like signal (iMTS-L) mediates targeting to CC mitochondria thermogenic fat cells. {ECO:0000250|UniProtKB:Q04447}. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE- CC ProRule:PRU00843}. 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; BT020708; AAX08725.1; -; mRNA. DR EMBL; BC102333; AAI02334.1; -; mRNA. DR RefSeq; NP_001015613.1; NM_001015613.1. DR PDB; 4Q2R; X-ray; 1.65 A; A/B=1-381. DR PDBsum; 4Q2R; -. DR AlphaFoldDB; Q5EA61; -. DR SMR; Q5EA61; -. DR STRING; 9913.ENSBTAP00000047181; -. DR PaxDb; 9913-ENSBTAP00000047181; -. DR PeptideAtlas; Q5EA61; -. DR Ensembl; ENSBTAT00000050490.2; ENSBTAP00000047181.1; ENSBTAG00000035998.4. DR GeneID; 516210; -. DR KEGG; bta:516210; -. DR CTD; 1152; -. DR VEuPathDB; HostDB:ENSBTAG00000035998; -. DR VGNC; VGNC:27384; CKB. DR eggNOG; KOG3581; Eukaryota. DR GeneTree; ENSGT00950000182772; -. DR HOGENOM; CLU_019868_4_2_1; -. DR InParanoid; Q5EA61; -. DR OMA; NRGHEFM; -. DR OrthoDB; 35839at2759; -. DR TreeFam; TF314214; -. DR Reactome; R-BTA-71288; Creatine metabolism. DR Reactome; R-BTA-9696264; RND3 GTPase cycle. DR Proteomes; UP000009136; Chromosome 21. DR Bgee; ENSBTAG00000035998; Expressed in retina and 106 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; ISS:AgBase. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0007420; P:brain development; ISS:AgBase. DR GO; GO:0140651; P:futile creatine cycle; IEA:Ensembl. DR GO; GO:0030644; P:intracellular chloride ion homeostasis; ISS:AgBase. 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: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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane; KW Mitochondrion; Nitration; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1..381 FT /note="Creatine kinase B-type" FT /id="PRO_0000244732" FT DOMAIN 11..98 FT /note="Phosphagen kinase N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842" FT DOMAIN 125..367 FT /note="Phosphagen kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT REGION 96..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 130..138 FT /note="Internal MTS-like signal" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT COMPBIAS 96..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 72 FT /ligand="creatine" FT /ligand_id="ChEBI:CHEBI:57947" FT /evidence="ECO:0000250|UniProtKB:P12277" FT BINDING 128..132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 232 FT /ligand="creatine" FT /ligand_id="ChEBI:CHEBI:57947" FT /evidence="ECO:0000250|UniProtKB:P12277" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 285 FT /ligand="creatine" FT /ligand_id="ChEBI:CHEBI:57947" FT /evidence="ECO:0000250|UniProtKB:P12277" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 320..325 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT BINDING 335 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P12277" FT MOD_RES 35 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P12277" FT MOD_RES 125 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P12277" FT MOD_RES 269 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT MOD_RES 322 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 29..33 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 36..42 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 126..135 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 204..214 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 223..244 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 246..266 FT /evidence="ECO:0007829|PDB:4Q2R" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 308..314 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 317..320 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 333..338 FT /evidence="ECO:0007829|PDB:4Q2R" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 346..368 FT /evidence="ECO:0007829|PDB:4Q2R" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:4Q2R" SQ SEQUENCE 381 AA; 42719 MW; ECBA70EF44052A22 CRC64; MPFSNSHNTL KLRFPAEDEF PDLSGHNNHM AKVLTPELYA ELRAKSTPSG FTVDDVIQTG VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY KPTDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K //