VATL_RAT
ID VATL_RAT Reviewed; 155 AA.
AC P63081; P23967;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
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, Atpl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1400263; DOI=10.1093/oxfordjournals.jbchem.a123879;
RA Nezu J., Motojima K., Tamura H., Ohkuma S.;
RT "Molecular cloning of a rat liver cDNA encoding the 16 kDa subunit of
RT vacuolar H(+)-ATPases: organellar and tissue distribution of 16 kDa
RT proteolipids.";
RL J. Biochem. 112:212-219(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQC, ECO:0007744|PDB:6VQG, ECO:0007744|PDB:6VQH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(2020).
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 (PubMed:32165585). 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 (PubMed:32165585). {ECO:0000269|PubMed:32165585}.
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 (PubMed:32165585). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32165585). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32165585). Interacts with the V0
CC complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with
CC LASS2 (By similarity). Interacts with RNF182; this interaction leads to
CC ubiquitination and degradation via the proteasome pathway (By
CC similarity). {ECO:0000250|UniProtKB:P27449,
CC ECO:0000250|UniProtKB:P63082, ECO:0000269|PubMed:32165585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
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; D10874; BAA01643.1; -; mRNA.
DR EMBL; BC063154; AAH63154.1; -; mRNA.
DR PIR; JX0226; JX0226.
DR RefSeq; NP_570836.1; NM_130823.3.
DR RefSeq; XP_006245960.1; XM_006245898.1.
DR PDB; 6VQ6; EM; 3.90 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDB; 6VQ7; EM; 4.00 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDB; 6VQ8; EM; 3.90 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDB; 6VQC; EM; 3.80 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDB; 6VQG; EM; 4.20 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDB; 6VQH; EM; 4.40 A; g/h/i/j/k/l/m/n/o=1-155.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQC; -.
DR PDBsum; 6VQG; -.
DR PDBsum; 6VQH; -.
DR AlphaFoldDB; P63081; -.
DR SMR; P63081; -.
DR BioGRID; 250971; 1.
DR IntAct; P63081; 4.
DR MINT; P63081; -.
DR STRING; 10116.ENSRNOP00000008736; -.
DR PhosphoSitePlus; P63081; -.
DR SwissPalm; P63081; -.
DR jPOST; P63081; -.
DR PaxDb; P63081; -.
DR PRIDE; P63081; -.
DR Ensembl; ENSRNOT00000113937; ENSRNOP00000088542; ENSRNOG00000006542.
DR GeneID; 170667; -.
DR KEGG; rno:170667; -.
DR UCSC; RGD:621394; rat.
DR CTD; 527; -.
DR RGD; 621394; Atp6v0c.
DR eggNOG; KOG0232; Eukaryota.
DR GeneTree; ENSGT00550000074873; -.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P63081; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; P63081; -.
DR TreeFam; TF300025; -.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:P63081; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006542; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; P63081; RN.
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:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
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; ISO:RGD.
DR GO; GO:1904093; P:negative regulation of autophagic cell death; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Synapse; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..155
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071745"
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:0000305|PubMed:32165585"
SQ SEQUENCE 155 AA; 15808 MW; 880C280C5AEB0C5C CRC64;
MADIKNNPEY SSFFGVMGAS SAMVFSAMGA AYGTAKSGTG IAAMSVMRPE LIMKSIIPVV
MAGIIAIYGL VVAVLIANSL TDGITLYRSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
