ATP8_TRIRU
ID ATP8_TRIRU Reviewed; 48 AA.
AC Q36838;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP synthase protein 8;
DE AltName: Full=A6L;
DE AltName: Full=F-ATPase subunit 8;
GN Name=ATP8;
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IP 1817.89;
RX PubMed=8593686; DOI=10.1007/bf00518168;
RA de Bievre C., Dujon B.;
RT "Organisation of the mitochondrial genome of Trichophyton rubrum. DNA
RT sequence analysis of the ND4 gene, the ATPase subunit-6 gene, the ribosomal
RT RNA small-subunit gene, the ND6 gene, the COXIII gene, the ATPase subunit-8
RT gene and six tRNA genes that correspond respectively to the tyrosine,
RT lysine, glutamine, asparagine, isoleucine and tryptophan isoacceptors.";
RL Curr. Genet. 28:553-559(1995).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR EMBL; X88896; CAA61358.1; -; Genomic_DNA.
DR PIR; S65035; S65035.
DR AlphaFoldDB; Q36838; -.
DR SMR; Q36838; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR InterPro; IPR009230; ATP_synth_su8_fun.
DR Pfam; PF05933; Fun_ATP-synt_8; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..48
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195605"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 48 AA; 5885 MW; 86634B6EC93551F1 CRC64;
MPQLIPFFFF NQVVFTLISL SFIFFVFSKY ILPWIVRLYV SRNQYNSL