KCRB_BOVIN
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 03-AUG-2022, entry version 119.
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.
CC {ECO:0000250|UniProtKB:P12277}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q04447}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q04447}. 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}.
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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; Q5EA61; -.
DR PeptideAtlas; Q5EA61; -.
DR PRIDE; Q5EA61; -.
DR Ensembl; ENSBTAT00000050490; ENSBTAP00000047181; ENSBTAG00000035998.
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; 825025at2759; -.
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 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; ISS:AgBase.
DR GO; GO:0030644; P:cellular 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 Gene3D; 1.10.135.10; -; 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; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 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; Cytoplasm; Kinase; Mitochondrion; Nitration;
KW Nucleotide-binding; Phosphoprotein; 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
