ID   KCRB_CANFA              Reviewed;         381 AA.
AC   P05124;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   04-NOV-2008, entry version 63.
DE   RecName: Full=Creatine kinase B-type;
DE            EC=2.7.3.2;
DE   AltName: Full=Creatine kinase B chain;
DE   AltName: Full=B-CK;
GN   Name=CKB;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=86295699; PubMed=3755597; DOI=10.1016/0006-291X(86)90294-9;
RA   Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W.;
RT   "The complete nucleotide sequence of canine brain B creatine kinase
RT   mRNA: homology in the coding and 3' noncoding regions among species.";
RL   Biochem. Biophys. Res. Commun. 138:392-398(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208;
RP   224-236; 247-261; 268-287; 321-357 AND 364-381.
RC   TISSUE=Brain;
RX   MEDLINE=86094232; PubMed=3866230;
RA   Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B.,
RA   Strauss A.W.;
RT   "Complete nucleotide sequence of dog heart creatine kinase mRNA:
RT   conservation of amino acid sequence within and among species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC       the major form in skeletal muscle and myocardium, MB existing in
CC       myocardium, and BB existing in many tissues, especially brain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
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DR   EMBL; M13453; AAA30837.1; -; mRNA.
DR   PIR; A24227; B24686.
DR   HSSP; P05122; 1QH4.
DR   SMR; P05124; 2-381.
DR   Ensembl; ENSCAFG00000018277; Canis familiaris.
DR   HOVERGEN; P05124; -.
DR   GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR   GO; GO:0005515; F:protein binding; ISS:AgBase.
DR   GO; GO:0007420; P:brain development; ISS:AgBase.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; ISS:AgBase.
DR   InterPro; IPR000749; ATP-gua_Ptrans.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   PROSITE; PS00112; GUANIDO_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       Creatine kinase B-type.
FT                                /FTId=PRO_0000211965.
FT   NP_BIND     128    132       ATP (By similarity).
FT   NP_BIND     320    325       ATP (By similarity).
FT   BINDING     191    191       ATP (By similarity).
FT   BINDING     236    236       ATP (By similarity).
FT   BINDING     292    292       ATP (By similarity).
FT   BINDING     335    335       ATP (By similarity).
FT   MOD_RES      39     39       Phosphotyrosine (By similarity).
FT   MOD_RES     125    125       Phosphotyrosine (By similarity).
FT   MOD_RES     164    164       Phosphoserine (By similarity).
SQ   SEQUENCE   381 AA;  42701 MW;  2C2F925C78F16364 CRC64;
     MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG
     VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY KPSDEHKTDL 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 QAIDDLVPAQ K
//