(data stored in ACNUC27125 zone)

HOGENOM: YEASTMITO_PE18

ID   YEASTMITO_PE18                       STANDARD;      PRT;   76 AA.
AC   YEASTMITO_PE18; P61829; P00841; Q37750;
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=ATP synthase subunit 9, mitochondrial;AltName:
DE   Full=Lipid-binding protein;AltName: Full=Oligomycin resistance protein 1;
DE   (YEASTMITO.PE18).
GN   Name=OLI1; Synonyms=ATP9, OLI3, PHO2; OrderedLocusNames=Q0130;
OS   SACCHAROMYCES CEREVISIAE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS YEASTMITO.PE18.
CC       Saccharomyces cerevisiae chromosome Mito EF2 full sequence 1..85779
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:ATP9_YEAST
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain. A homomeric c-ring of probably 10 subunits is part of the
CC       complex rotary element.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. In yeast, the
CC       dimeric form of ATP synthase consists of 17 polypeptides: alpha,
CC       beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d,
CC       E (Tim11), f, g, h, i/j and k.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the ATPase C chain family.
CC   -!- GENE_FAMILY: HOG000235245 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Saccharomyces_cerevisiae;Q0130;Q0130;Q0130.
DR   EMBL; AJ011856; - ;
DR   EMBL; J01462; - ;
DR   EMBL; L00007; - ;
DR   EMBL; L36899; - ;
DR   EMBL; V00707; - ;
DR   EMBL; X03968; - ;
DR   EMBL; X05357; - ;
DR   EMBL; X05358; - ;
DR   UniProtKB/Swiss-Prot; P61829; P00841; Q37750; -.
DR   EMBL; L00007; AAA32146.1; -; Genomic_DNA.
DR   EMBL; J01462; AAA32169.1; -; Genomic_DNA.
DR   EMBL; V00707; CAA24079.1; -; Genomic_DNA.
DR   EMBL; L36899; AAA67535.1; -; Genomic_DNA.
DR   EMBL; X03968; CAA27605.1; -; Genomic_DNA.
DR   EMBL; AJ011856; CAA09838.1; -; Genomic_DNA.
DR   PIR; A23024; LWBYA.
DR   RefSeq; NP_009319.1; NM_001184366.1.
DR   PDB; 2WPD; X-ray; 3.43 A; J/K/L/M/N/O/P/Q/R/S=1-76.
DR   PDB; 2XOK; X-ray; 3.01 A; K/L/M/N/O/P/Q/R/S/T=1-76.
DR   PDBsum; 2WPD; -.
DR   PDBsum; 2XOK; -.
DR   ProteinModelPortal; P61829; -.
DR   SMR; P61829; 1-76.
DR   DIP; DIP-3041N; -.
DR   STRING; P61829; -.
DR   TCDB; 3.A.2.1.3; H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
DR   EnsemblFungi; Q0130; Q0130; Q0130.
DR   GeneID; 854584; -.
DR   KEGG; sce:Q0130; -.
DR   NMPDR; fig|4932.3.peg.1871; -.
DR   CYGD; Q0130; -.
DR   SGD; S000007274; OLI1.
DR   eggNOG; fuNOG12572; -.
DR   OrthoDB; EOG4J9R8T; -.
DR   PhylomeDB; P61829; -.
DR   NextBio; 977052; -.
DR   ArrayExpress; P61829; -.
DR   Genevestigator; P61829; -.
DR   GermOnline; Q0130; Saccharomyces cerevisiae.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IPI:SGD.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IDA:SGD.
DR   InterPro; IPR000454; ATPase_F0-cplx_csu.
DR   InterPro; IPR020537; ATPase_F0-cplx_csu_DDCD_BS.
DR   InterPro; IPR002379; ATPase_F0/V0-cplx_csu.
DR   Gene3D; G3DSA:1.20.20.10; ATPase_F0/V0_c; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; ATPase_F0/V0_c; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
DR   HOGENOMDNA; YEASTMITO.PE18; -.
KW   Q01302C-A100026476820036002503210000011; Q01302C-A1; ATP9_YEAST;
KW   Q37673_YEAST; AJ011856; J01462; L00007; L36899; V00707; X03968; X05357;
KW   X05358;
KW   3D-structure; CF(0); Complete proteome; Direct protein sequencing;
KW   Formylation; Hydrogen ion transport; Ion transport; Lipid-binding;
KW   Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   76 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALINGVSRN PSIKDLVFPM AILGFALSEA
     TGLFCLMVSF LLLFGV
//

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