ID A0A3Q7R328_VULVU Unreviewed; 155 AA.
AC A0A3Q7R328;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=V-type proton ATPase proteolipid subunit {ECO:0000256|RuleBase:RU363060};
GN Name=ATP6V0C {ECO:0000313|RefSeq:XP_025840689.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025840689.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025840689.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025840689.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025840689.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment.
CC {ECO:0000256|RuleBase:RU363060}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits. {ECO:0000256|RuleBase:RU363060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00029431}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00029431}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004644};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004644}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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 RefSeq; XP_025840689.1; XM_025984904.1.
DR AlphaFoldDB; A0A3Q7R328; -.
DR SMR; A0A3Q7R328; -.
DR STRING; 9627.ENSVVUP00000012295; -.
DR Ensembl; ENSVVUT00000016082; ENSVVUP00000012295; ENSVVUG00000009051.
DR KEGG; vvp:112909098; -.
DR OMA; CDPNSAF; -.
DR OrthoDB; 168305at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
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; 2.
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:UP000286640};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 89..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 126..152
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 17..76
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 93..152
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 155 AA; 15702 MW; 333B34E4B2C38612 CRC64;
MSEAKNGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE LIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDGISLYRSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
//