KCRB_CHICK
ID KCRB_CHICK Reviewed; 381 AA.
AC P05122; Q92061;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Creatine kinase B-type {ECO:0000303|PubMed:8525081};
DE EC=2.7.3.2 {ECO:0000269|PubMed:20026305, ECO:0000269|PubMed:8525081};
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 {ECO:0000303|PubMed:8525081};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BB-CK-1), AND TISSUE SPECIFICITY.
RX PubMed=3513124; DOI=10.1093/nar/14.3.1449;
RA Hossle J.P., Rosenberg U.B., Schaefer B.W., Eppenberger H.M.,
RA Perriard J.-C.;
RT "The primary structure of chicken B-creatine kinase and evidence for
RT heterogeneity of its mRNA.";
RL Nucleic Acids Res. 14:1449-1463(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BA-CK AND BB-CK-1).
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=2365692; DOI=10.1016/s0021-9258(19)38448-0;
RA Wirz T., Braendle U., Soldati T., Hossle J.P., Perriard J.-C.;
RT "A unique chicken B-creatine kinase gene gives rise to two B-creatine
RT kinase isoproteins with distinct N termini by alternative splicing.";
RL J. Biol. Chem. 265:11656-11666(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-381.
RC TISSUE=Brain;
RX PubMed=3840441; DOI=10.1016/0012-1606(85)90121-6;
RA Kwiatkowski R.W., Ehrismann R., Schweinfest C.W., Dottin R.P.;
RT "Accumulation of creatine kinase mRNA during myogenesis: molecular cloning
RT of a B-creatine kinase cDNA.";
RL Dev. Biol. 112:84-88(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-9; 12-20; 266-277 AND 320-329, AND PHOSPHORYLATION AT
RP THR-282; SER-285 AND THR-289.
RX PubMed=7669815; DOI=10.1016/0167-4838(95)00083-7;
RA Hemmer W., Furter-Graves E.M., Frank G., Wallimann T., Furter R.;
RT "Autophosphorylation of creatine kinase: characterization and
RT identification of a specifically phosphorylated peptide.";
RL Biochim. Biophys. Acta 1251:81-90(1995).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORMS BA-CK-2; BA-CK-3 AND BA-CK-4), AND
RP PHOSPHORYLATION.
RX PubMed=2307674; DOI=10.1016/s0021-9258(19)39591-2;
RA Soldati T., Schaefer B.W., Perriard J.-C.;
RT "Alternative ribosomal initiation gives rise to chicken brain-type creatine
RT kinase isoproteins with heterogeneous amino termini.";
RL J. Biol. Chem. 265:4498-4506(1990).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8525081; DOI=10.1016/0034-5288(95)90026-8;
RA Mitchell M.A., Sandercock D.A.;
RT "Creatine kinase isoenzyme profiles in the plasma of the domestic fowl
RT (Gallus domesticus): effects of acute heat stress.";
RL Res. Vet. Sci. 59:30-34(1995).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20026305; DOI=10.1016/j.bbrc.2009.12.083;
RA Sekrecka-Belniak A., Balcerzak M., Buchet R., Pikula S.;
RT "Active creatine kinase is present in matrix vesicles isolated from femurs
RT of chicken embryo: Implications for bone mineralization.";
RL Biochem. Biophys. Res. Commun. 391:1432-1436(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS).
RX PubMed=10595529; DOI=10.1110/ps.8.11.2258;
RA Eder M., Schlattner U., Becker A., Wallimann T., Kabsch W., Fritz-Wolf K.;
RT "Crystal structure of brain-type creatine kinase at 1.41-A resolution.";
RL Protein Sci. 8:2258-2269(1999).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate) (PubMed:8525081,
CC PubMed:20026305). Creatine kinase isoenzymes play a central role in
CC energy transduction in tissues with large, fluctuating energy demands,
CC such as skeletal muscle, heart, brain and spermatozoa (Probable).
CC {ECO:0000269|PubMed:20026305, ECO:0000269|PubMed:8525081, ECO:0000305}.
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:0000255|PROSITE-ProRule:PRU10029,
CC ECO:0000269|PubMed:20026305, ECO:0000269|PubMed:8525081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC Evidence={ECO:0000269|PubMed:20026305, ECO:0000269|PubMed:8525081};
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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Bb-CK-1 {ECO:0000303|PubMed:2365692, ECO:0000303|PubMed:3513124};
CC IsoId=P05122-1; Sequence=Displayed;
CC Name=Ba-CK {ECO:0000303|PubMed:2365692};
CC IsoId=P05122-2; Sequence=VSP_002814;
CC Name=Bb-CK-2 {ECO:0000303|PubMed:2307674};
CC IsoId=P05122-3; Sequence=VSP_010768;
CC Name=Bb-CK-3 {ECO:0000303|PubMed:2307674};
CC IsoId=P05122-4; Sequence=VSP_010769;
CC Name=Bb-CK-4 {ECO:0000303|PubMed:2307674};
CC IsoId=P05122-5; Sequence=VSP_010770;
CC -!- TISSUE SPECIFICITY: Expressed in almost all tissues and found enriched
CC in various region of the brain, retina, heart, gizzard, gut and sperm.
CC {ECO:0000269|PubMed:3513124}.
CC -!- PTM: Ba-CK and Bb-CK are phosphorylated. {ECO:0000269|PubMed:2307674}.
CC -!- PTM: The N-terminus of BA-CK is blocked. {ECO:0000269|PubMed:2365692}.
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; X03509; CAA27221.1; -; mRNA.
DR EMBL; M33714; AAA48613.1; -; Genomic_DNA.
DR EMBL; M33711; AAA48613.1; JOINED; Genomic_DNA.
DR EMBL; M33712; AAA48613.1; JOINED; Genomic_DNA.
DR EMBL; M33713; AAA48613.1; JOINED; Genomic_DNA.
DR EMBL; M33714; AAA48614.1; -; Genomic_DNA.
DR EMBL; M33711; AAA48614.1; JOINED; Genomic_DNA.
DR EMBL; M33712; AAA48614.1; JOINED; Genomic_DNA.
DR EMBL; M33713; AAA48614.1; JOINED; Genomic_DNA.
DR EMBL; M35381; AAA48687.1; -; Genomic_DNA.
DR PIR; A37059; A24793.
DR RefSeq; NP_990641.1; NM_205310.1. [P05122-1]
DR RefSeq; XP_015142790.1; XM_015287304.1. [P05122-2]
DR PDB; 1QH4; X-ray; 1.41 A; A/B/C/D=2-381.
DR PDBsum; 1QH4; -.
DR AlphaFoldDB; P05122; -.
DR SMR; P05122; -.
DR BioGRID; 676508; 1.
DR IntAct; P05122; 1.
DR STRING; 9031.ENSGALP00000018742; -.
DR iPTMnet; P05122; -.
DR PaxDb; P05122; -.
DR Ensembl; ENSGALT00000018765; ENSGALP00000018742; ENSGALG00000011511. [P05122-3]
DR Ensembl; ENSGALT00000053131; ENSGALP00000047068; ENSGALG00000011511. [P05122-2]
DR Ensembl; ENSGALT00000087830; ENSGALP00000062025; ENSGALG00000011511. [P05122-5]
DR GeneID; 396248; -.
DR KEGG; gga:396248; -.
DR CTD; 1152; -.
DR VEuPathDB; HostDB:geneid_396248; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR InParanoid; P05122; -.
DR OMA; ECINDAI; -.
DR PhylomeDB; P05122; -.
DR Reactome; R-GGA-71288; Creatine metabolism.
DR Reactome; R-GGA-9696264; RND3 GTPase cycle.
DR EvolutionaryTrace; P05122; -.
DR PRO; PR:P05122; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000011511; Expressed in testis and 13 other tissues.
DR ExpressionAtlas; P05122; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:AgBase.
DR GO; GO:0065010; C:extracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IDA:AgBase.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0006754; P:ATP biosynthetic process; IDA: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; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase B-type"
FT /id="PRO_0000211971"
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 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 282
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:7669815"
FT MOD_RES 285
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:7669815"
FT MOD_RES 289
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:7669815"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform Bb-CK-4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010770"
FT VAR_SEQ 1..65
FT /note="MPFSNSHNLLKMKYSVDDEYPDLSVHNNHMAKVLTLDLYKKLRDRQTSSGFT
FT LDDVIQTGVDNPG -> MAQLNNQRLPPEEEYPDLSTHNNHMAKVLTLDLYKKLRDRVT
FT PSGFTLDDVIQTGVDNPG (in isoform Ba-CK)"
FT /evidence="ECO:0000305"
FT /id="VSP_002814"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform Bb-CK-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_010769"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform Bb-CK-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010768"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1QH4"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1QH4"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1QH4"
FT TURN 204..214
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 223..244
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 246..266
FT /evidence="ECO:0007829|PDB:1QH4"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1QH4"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1QH4"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 346..368
FT /evidence="ECO:0007829|PDB:1QH4"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1QH4"
SQ SEQUENCE 381 AA; 42871 MW; 313BCCB46BCDD02B CRC64;
MPFSNSHNLL KMKYSVDDEY PDLSVHNNHM AKVLTLDLYK KLRDRQTSSG FTLDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PVIEDRHGGY KPTDEHKTDL NADNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLSVE ALGSLGGDLK GKYYALRNMT
DAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
NLGKHEKFGE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEKRLEKG QSIDDLMPAQ K
