VATL_SHEEP
ID VATL_SHEEP Reviewed; 155 AA.
AC O18882;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN Name=ATP6V0C; Synonyms=ATP6C, ATP6L;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hamilton N.H.R., Damak S., Palmer D.N.;
RT "Cloning of the ovine Vacuolar ATPase subunit c cDNA.";
RL Submitted (OCT-1997) 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 (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). {ECO:0000250|UniProtKB:P23956,
CC ECO:0000250|UniProtKB:P27449}.
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 (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4
CC (By similarity). Interacts with LASS2 (By similarity). Interacts with
CC RNF182; this interaction leads to ubiquitination and degradation via
CC the proteasome pathway (By similarity). {ECO:0000250|UniProtKB:P27449,
CC ECO:0000250|UniProtKB:P63082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:P27449}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AF027705; AAB84040.1; -; mRNA.
DR RefSeq; NP_001009195.1; NM_001009195.1.
DR AlphaFoldDB; O18882; -.
DR SMR; O18882; -.
DR STRING; 9940.ENSOARP00000011352; -.
DR Ensembl; ENSOART00020041385; ENSOARP00020034367; ENSOARG00020026310.
DR GeneID; 443003; -.
DR KEGG; oas:443003; -.
DR CTD; 527; -.
DR eggNOG; KOG0232; Eukaryota.
DR OrthoDB; 1534092at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
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 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; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..155
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071746"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..92
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..155
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 139
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
SQ SEQUENCE 155 AA; 15693 MW; 93A620A92613DDEF CRC64;
MSEAKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE MIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDGISLYRSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
