(data stored in ACNUC941 zone)

HOGENOM: CHICK10_PE591

ID   CHICK10_PE591                        STANDARD;      PRT;   417 AA.
AC   CHICK10_PE591; P70079; Q90782;
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   Flags: Fragments;
DE   RecName: Full=Creatine kinase U-type, mitochondrial; EC=2.7.3 2;AltName:
DE   Full=Acidic-type mitochondrial creatine kinase; Short=Mia-CK;AltName:
DE   Full=Ubiquitous mitochondrial creatine kinase; Short=U-MtCK;Flags:
DE   Precursor; (CHICK10.PE591).
GN   Name=CKMT1;
OS   GALLUS GALLUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Sauropsida; Sauria; Archosauria;
OC   Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae;
OC   Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHICK10.PE591.
CC       Gallus gallus chromosome 10 WASHUC2  sequence 1..22556432 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KCRU_CHICK
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: Exists as an octamer composed of four MTCK homodimers (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and gut, weakly in
CC       testis. Also found in cell bodies of neural cells of the gray
CC       matter.
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin (By
CC       similarity).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA65266.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000232165 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Gallus_gallus;ENSGALG00000008352;ENSGALT00000013600;ENSGALP00000013585.
DR   EMBL; X95526; - ;
DR   EMBL; X96402; - ;
DR   EMBL; X96403; - ;
DR   UniProtKB/Swiss-Prot; P70079; Q90782; -.
DR   EMBL; X96403; CAA65267.1; -; Genomic_DNA.
DR   EMBL; X96402; CAA65266.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X95526; CAA64778.1; -; Genomic_DNA.
DR   IPI; IPI00586552; -.
DR   RefSeq; NP_989513.1; NM_204182.1.
DR   UniGene; Gga.13490; -.
DR   ProteinModelPortal; P70079; -.
DR   SMR; P70079; 39-417.
DR   PRIDE; P70079; -.
DR   GeneID; 374002; -.
DR   KEGG; gga:374002; -.
DR   CTD; 548596; -.
DR   eggNOG; veNOG04753; -.
DR   GeneTree; ENSGT00550000074561; -.
DR   InParanoid; P70079; -.
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; 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   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; CHICK10.PE591; -.
KW   ENSGALG00000008352fold_1320000031; ENSGALP00000013585fold_1320000031;
KW   X95526; X96402; X96403;
KW   ATP-binding; Complete proteome; Direct protein sequencing; Kinase;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Reference proteome; Transferase; Transit peptide.
SQ   SEQUENCE   417 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     PSKFGRILSS RCSAGATRQW WARGYFAAGF LLARDTVSAG ERQRWRYPPS AEYPDLRKHN
     NCMASNLTPA IYARLCDKAT PNGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAE
     LFDPVIQERH NGYNPRTMKH VTDLDASKIK FGHFDERYVL SSRVRTGRSI RGLSLPPACT
     RAERREVEKV TVEALNGLTG DLSGRYYRLS EMTEKEQQQL IDDHFLFDKP VSPLLTAAGM
     ARDWPDARGI WHNNEKTFLI WINEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
     GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
     AATGNVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL EKGQDIRIPS PVPQFRH
//

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