(data stored in ACNUC941 zone)

HOGENOM: RABIT11_2_PE8

ID   RABIT11_2_PE8                        STANDARD;      PRT;   419 AA.
AC   RABIT11_2_PE8; O77814;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Creatine kinase S-type, mitochondrial; EC=2.7.3 2;AltName:
DE   Full=Basic-type mitochondrial creatine kinase; Short=Mib-CK;AltName:
DE   Full=RSMTCK;AltName: Full=Sarcomeric mitochondrial creatine kinase;
DE   Short=S-MtCK;Flags: Precursor; (RABIT11_2.PE8).
GN   Name=CKMT2;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT11_2.PE8.
CC       Oryctolagus cuniculus chromosome 11 oryCun2 partial sequence
CC       1000001..2000000 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KCRS_RABIT
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side (By similarity).
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
CC   -!- GENE_FAMILY: HOG000232165 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000011211;ENSOCUT00000011210;ENSOCUP00000009646.
DR   EMBL; AJ011334; - ;
DR   UniProtKB/Swiss-Prot; O77814; -.
DR   EMBL; AJ011334; CAA09597.1; -; mRNA.
DR   RefSeq; NP_001156542.1; NM_001163070.1.
DR   UniGene; Ocu.3234; -.
DR   ProteinModelPortal; O77814; -.
DR   SMR; O77814; 47-413.
DR   Ensembl; ENSOCUT00000011210; ENSOCUP00000009646; ENSOCUG00000011211.
DR   GeneID; 100302412; -.
DR   CTD; 100302412; -.
DR   eggNOG; maNOG11792; -.
DR   GeneTree; ENSGT00550000074561; -.
DR   OrthoDB; EOG40VVPN; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
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; IPR014746; Gln_synth/guanido_kin_cat_dom.
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   SUPFAM; SSF48034; ATP-gua_Ptrans; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
DR   HOGENOMDNA; RABIT11_2.PE8; -.
KW   ENSOCUG00000011211820036002503210000011;
KW   KCRS_RABIT; AJ011334;
KW   ATP-binding; Kinase; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Transferase;
KW   Transit peptide.
SQ   SEQUENCE   419 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MASTFSKLLT GRNASLLFAT LGTSALTTGY LVNRQKVCAE ARDQHKLFPP SADYPDLRKH
     NNCMAECLTP SIYAKLRNKV TPNGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
     DLFDPVIKLR HNGYDPRVMK HPTDLDASKI TQGQFDERYV LSSRVRTGRS IRGLSLPPAC
     SRAERREVEN VAITALEGLK GDLAGRYYRL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
     MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
     RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
     TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGKK
//

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