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Database: UniProt
Entry: A0A024U171_9STRA
LinkDB: A0A024U171_9STRA
Original site: A0A024U171_9STRA 
ID   A0A024U171_9STRA        Unreviewed;       169 AA.
AC   A0A024U171;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN   ORFNames=H310_07959 {ECO:0000313|EMBL:ETV99939.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV99939.1};
RN   [1] {ECO:0000313|EMBL:ETV99939.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV99939.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI913966; ETV99939.1; -; Genomic_DNA.
DR   RefSeq; XP_008871715.1; XM_008873493.1.
DR   AlphaFoldDB; A0A024U171; -.
DR   STRING; 157072.A0A024U171; -.
DR   EnsemblFungi; H310_07959-t26_1; H310_07959-t26_1-p1; H310_07959.
DR   EnsemblProtists; ETV99939; ETV99939; H310_07959.
DR   GeneID; 20085009; -.
DR   VEuPathDB; FungiDB:H310_07959; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   OrthoDB; 168305at2759; -.
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 C; 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; 2.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU363060};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU363060};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363060};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363060};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363060};
KW   Vacuole {ECO:0000256|RuleBase:RU363060}.
FT   TRANSMEM        16..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        99..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        136..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          20..79
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          102..161
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   169 AA;  17046 MW;  2D11550E3F034E79 CRC64;
     MLAQLASELC PTSAPFFGFM GVTSALVFAN LGAAYGTAKS GVGIASMGVM RPELVMRNII
     PVIMAGVLGI YGLIVAVIIQ GSIDVPNGKD TVYGSYTGFA HLSAGLCCGL SGLAAGMAIG
     VVGDAGVRAV GQQEKLFVGM ILILIFAEAL GLYGLIVALI LATKKSTGC
//
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