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Database: UniProt
Entry: A0A0L0SJ69_ALLM3
LinkDB: A0A0L0SJ69_ALLM3
Original site: A0A0L0SJ69_ALLM3 
ID   A0A0L0SJ69_ALLM3        Unreviewed;       148 AA.
AC   A0A0L0SJ69;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN   ORFNames=AMAG_07756 {ECO:0000313|EMBL:KNE62548.1};
OS   Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS   macrogynus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE62548.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE62548.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE62548.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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. V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments.
CC       {ECO:0000256|RuleBase:RU363060}.
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). The decameric c-ring forms the proton-conducting pore, and is
CC       composed of eight proteolipid subunits c, one subunit c' and one
CC       subunit c''. {ECO:0000256|RuleBase:RU363060}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane
CC       {ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363060}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000256|ARBA:ARBA00007296, ECO:0000256|RuleBase:RU363060}.
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DR   EMBL; GG745340; KNE62548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0SJ69; -.
DR   STRING; 578462.A0A0L0SJ69; -.
DR   EnsemblFungi; KNE62548; KNE62548; AMAG_07756.
DR   VEuPathDB; FungiDB:AMAG_07756; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   OMA; TNGMPLY; -.
DR   OrthoDB; 168305at2759; -.
DR   Proteomes; UP000054350; Unassembled WGS sequence.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd18175; ATP-synt_Vo_c_ATP6C_rpt1; 1.
DR   CDD; cd18176; ATP-synt_Vo_c_ATP6C_rpt2; 1.
DR   Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 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   NCBIfam; TIGR01100; V_ATP_synt_C; 1.
DR   PANTHER; PTHR10263:SF5; V-TYPE PROTON ATPASE 16 KDA PROTEOLIPID SUBUNIT; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU363060};
KW   Ion transport {ECO:0000256|RuleBase:RU363060};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054350};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363060};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363060}; Transport {ECO:0000256|RuleBase:RU363060};
KW   Vacuole {ECO:0000256|RuleBase:RU363060}.
FT   TRANSMEM        35..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        73..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        110..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          1..60
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          77..136
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   148 AA;  14857 MW;  651AFF2257AD7893 CRC64;
     MGCTSAIVFS CFGAAYGTAK SGVGVAAMGV MRPDLIMKSV IPVVMAGIIG IYGLAVAVLI
     SDGLKQVMPL YSGFIQLGAG LAVGLSGLAA GFAIGIVGDA GVRGSAQQPR LFVGMILILI
     FAEVLGLYGL IVALIMNTKA VSDVTCQS
//
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