ID KCRB_RAT Reviewed; 381 AA. AC P07335; A0JPK7; Q499P7; Q5PPJ5; Q6IRE0; Q6P139; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 04-NOV-2008, entry version 77. 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; Synonyms=Ckbb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86137395; PubMed=3005113; DOI=10.1016/0378-1119(85)90321-X; RA Benfield P.A., Henderson L., Pearson M.L.; RT "Expression of a rat brain creatine kinase-beta-galactosidase fusion RT protein in Escherichia coli and derivation of the complete amino acid RT sequence of rat brain creatine kinase."; RL Gene 39:263-267(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88255869; PubMed=2838389; DOI=10.1016/0378-1119(88)90527-6; RA Benfield P.A., Graf D., Korolkoff P.N., Hobson G., Pearson M.L.; RT "Isolation of four rat creatine kinase genes and identification of RT multiple potential promoter sequences within the rat brain creatine RT kinase promoter region."; RL Gene 63:227-243(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Uterus; RX MEDLINE=91133434; PubMed=2284002; RA Pentecost B.T., Mattheiss L., Dickerman H.W., Kumar S.A.; RT "Estrogen regulation of creatine kinase-B in the rat uterus."; RL Mol. Endocrinol. 4:1000-1010(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Embryonic brain, Heart, and Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 138-148; 157-172; 224-236; RP 253-265 AND 320-341, AND MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Diao W., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP PHOSPHORYLATION. RX MEDLINE=84307406; PubMed=6477506; RA Mahadevan L.C., Whatley S.A., Leung T.K.C., Lim L.; RT "The brain isoform of a key ATP-regulating enzyme, creatine kinase, is RT a phosphoprotein."; RL Biochem. J. 222:139-144(1984). RN [7] RP TISSUE SPECIFICITY. RX MEDLINE=92042182; PubMed=1939264; RA Friedman D.L., Perryman M.B.; RT "Compartmentation of multiple forms of creatine kinase in the distal RT nephron of the rat kidney."; RL J. Biol. Chem. 266:22404-22410(1991). 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 -!- TISSUE SPECIFICITY: In the kidney localized primarily in the outer CC medulla in the thick ascending limb and distal convoluted tubule. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14400; AAA40930.1; -; mRNA. DR EMBL; M18668; AAA40932.1; -; Genomic_DNA. DR EMBL; M57664; AAA40933.1; -; mRNA. DR EMBL; M57665; AAA40931.1; -; Genomic_DNA. DR EMBL; BC065307; AAH65307.2; -; mRNA. DR EMBL; BC070955; AAH70955.2; -; mRNA. DR EMBL; BC087656; AAH87656.1; ALT_INIT; mRNA. DR EMBL; BC099814; AAH99814.2; -; mRNA. DR EMBL; BC127477; AAI27478.2; -; mRNA. DR PIR; A23980; KIRTCB. DR RefSeq; NP_036661.2; -. DR UniGene; Rn.1472; -. DR HSSP; P05122; 1QH4. DR SMR; P07335; 2-381. DR PhosphoSite; P07335; -. DR Ensembl; ENSRNOG00000010872; Rattus norvegicus. DR GeneID; 24264; -. DR KEGG; rno:24264; -. DR RGD; 2357; Ckb. DR HOVERGEN; P07335; -. DR NextBio; 602815; -. DR ArrayExpress; P07335; -. DR GermOnline; ENSRNOG00000010872; Rattus norvegicus. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; IEA:EC. 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_0000211970. 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). FT CONFLICT 18 18 D -> A (in Ref. 3; AAA40931/AAA40933). FT CONFLICT 183 184 EQ -> DE (in Ref. 1; AAA40930 and 2; FT AAA40932). FT CONFLICT 206 206 G -> A (in Ref. 2; AAA40932). SQ SEQUENCE 381 AA; 42725 MW; A8C8A09F6FF1A4D1 CRC64; MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEDRHGGY QPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLS GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QPIDDLMPAQ K //