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Creatine kinase B-type (EC 2.7.3.2) (B-CK) (Creatine kinase B chain) (Fragments)

 KCRB_SQUAC              Reviewed;          52 AA.
P26460;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 78.
RecName: Full=Creatine kinase B-type;
EC=2.7.3.2;
AltName: Full=B-CK;
AltName: Full=Creatine kinase B chain;
Flags: Fragments;
Squalus acanthias (Spiny dogfish).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Squalimorphii; Squaliformes; Squalidae; Squalus.
NCBI_TaxID=7797;
[1]
PROTEIN SEQUENCE.
TISSUE=Rectal gland;
PubMed=1310991;
Friedman D.L., Roberts R.;
"Purification and localization of brain-type creatine kinase in sodium
chloride transporting epithelia of the spiny dogfish, Squalus
acanthias.";
J. Biol. Chem. 267:4270-4276(1992).
-!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
ATP and various phosphogens (e.g. creatine phosphate). Creatine
kinase isoenzymes play a central role in energy transduction in
tissues with large, fluctuating energy demands, such as skeletal
muscle, heart, brain and spermatozoa.
-!- FUNCTION: The isoform-specific function of B creatine kinase may
be to provide a system for the rapid regeneration of metabolic
energy for sodium transport.
-!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
the major form in skeletal muscle and myocardium, MB existing in
myocardium, and BB existing in many tissues, especially brain.
-!- SUBCELLULAR LOCATION: Basal cell membrane. Note=Basal membrane of
the sodium chloride-secreting epithelia.
-!- TISSUE SPECIFICITY: Creatine kinase B is the major isoform present
in the rectal gland.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
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PIR; A42272; A42272.
PIR; B42272; B42272.
ProteinModelPortal; P26460; -.
GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 2.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Direct protein sequencing; Kinase;
Membrane; Nucleotide-binding; Polymorphism; Transferase.
CHAIN <1 >52 Creatine kinase B-type.
/FTId=PRO_0000211972.
DOMAIN 1 52 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
DOMAIN 1 52 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
BINDING 13 13 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 47 47 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
VARIANT 3 3 V -> I.
VARIANT 5 5 T -> S.
VARIANT 10 10 K -> S.
VARIANT 13 13 R -> K.
VARIANT 16 16 S -> Q.
UNSURE 38 38
NON_CONS 28 29 {ECO:0000305}.
NON_TER 1 1
NON_TER 52 52
SEQUENCE 52 AA; 5778 MW; 3BC2C989F21CFF30 CRC64;
AKVLTLDLYK KLRDKSTPSG FTLDDIIQNE HLGYVLTCPS NLGTXLRAXV HV


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