VATL1_NEUCR
ID VATL1_NEUCR Reviewed; 161 AA.
AC P31413; Q7RVD6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=V-type proton ATPase subunit c {ECO:0000250|UniProtKB:P25515};
DE Short=V-ATPase subunit c {ECO:0000250|UniProtKB:P25515};
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump c subunit {ECO:0000250|UniProtKB:P25515};
GN Name=vma-3; ORFNames=12F11.130, NCU01332;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8190074; DOI=10.1007/bf00283879;
RA Sista H., Wechser M.A., Bowman B.J.;
RT "The proteolipid subunit of the Neurospora crassa vacuolar ATPase:
RT isolation of the protein and the vma-3 gene.";
RL Mol. Gen. Genet. 243:82-90(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (By similarity). {ECO:0000250|UniProtKB:P25515}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1) (By similarity). The decameric c-ring forms the proton-conducting
CC pore, and is composed of eight proteolipid subunits c, one subunit c'
CC and one subunit c'' (By similarity). {ECO:0000250|UniProtKB:P25515}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P25515};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; L07105; AAA19974.1; -; Unassigned_DNA.
DR EMBL; AL451017; CAC18222.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32182.2; -; Genomic_DNA.
DR PIR; S43893; S43893.
DR RefSeq; XP_961418.2; XM_956325.3.
DR AlphaFoldDB; P31413; -.
DR SMR; P31413; -.
DR STRING; 5141.EFNCRP00000004137; -.
DR EnsemblFungi; EAA32182; EAA32182; NCU01332.
DR GeneID; 3877578; -.
DR KEGG; ncr:NCU01332; -.
DR VEuPathDB; FungiDB:NCU01332; -.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P31413; -.
DR OMA; NFIQLGA; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:EnsemblFungi.
DR GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR GO; GO:0007033; P:vacuole organization; IEA:EnsemblFungi.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..161
FT /note="V-type proton ATPase subunit c"
FT /id="PRO_0000071760"
FT TOPO_DOM 1..8
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..91
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..161
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 138
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P25515"
SQ SEQUENCE 161 AA; 16330 MW; D7C54CD209373EB4 CRC64;
MSDLCPVYAP FFGAMGCTAA IVFTCLGASY GTAKSGVGIA AMGVLRPDLI VKNIVPVIMA
GIIGIYGLVV SVLISDALTQ DHYALYTGFI QLGAGLAVGL AGLAAGFAIG IVGDAGVRGT
AQQPRLFVGM ILILIFAEVL GLYGLIVALL MNSKATLNTS C
