VATO_BOVIN
ID VATO_BOVIN Reviewed; 205 AA.
AC Q2TA24;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=V-type proton ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 21 kDa proteolipid subunit c'' {ECO:0000305};
GN Name=ATP6V0B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(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:32764564). 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:32764564). {ECO:0000269|PubMed:32764564}.
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:32764564). 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:32764564). 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:32764564). Interacts with IFITM3
CC (By similarity). {ECO:0000250|UniProtKB:Q91V37,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; BC111150; AAI11151.1; -; mRNA.
DR RefSeq; NP_001033127.1; NM_001038038.2.
DR PDB; 6XBW; EM; 3.37 A; b=1-205.
DR PDB; 6XBY; EM; 3.79 A; b=1-205.
DR PDB; 7KHR; EM; 3.62 A; b=1-205.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; Q2TA24; -.
DR SMR; Q2TA24; -.
DR STRING; 9913.ENSBTAP00000025144; -.
DR PaxDb; Q2TA24; -.
DR PRIDE; Q2TA24; -.
DR Ensembl; ENSBTAT00000025144; ENSBTAP00000025144; ENSBTAG00000018889.
DR GeneID; 505684; -.
DR KEGG; bta:505684; -.
DR CTD; 533; -.
DR VEuPathDB; HostDB:ENSBTAG00000018889; -.
DR VGNC; VGNC:26310; ATP6V0B.
DR eggNOG; KOG0233; Eukaryota.
DR GeneTree; ENSGT00550000075120; -.
DR HOGENOM; CLU_085752_0_0_1; -.
DR InParanoid; Q2TA24; -.
DR OMA; PYAWAST; -.
DR OrthoDB; 1408246at2759; -.
DR TreeFam; TF314946; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000018889; Expressed in retina and 105 other tissues.
DR ExpressionAtlas; Q2TA24; baseline and differential.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..205
FT /note="V-type proton ATPase 21 kDa proteolipid subunit c''"
FT /id="PRO_0000285672"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..90
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..175
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 98
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000305|PubMed:32764564"
FT HELIX 5..26
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 46..79
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 128..168
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 173..197
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 205 AA; 21519 MW; D692C95BEB010018 CRC64;
MTGLVLLYSG VFVAFWACLL VVGICYTIFD LGFRFDVAWF LTETSPFMWS NLGIGLAISL
SVVGAAWGIY ITGSSIIGGG VKAPRIKTKN LVSIIFCEAV AIYGIIMAIV ISNMAEPFSA
TDPKAIGHRN YHAGYSMFGA GLTVGLSNLF CGVCVGIVGS GAALADAQNP SLFVKILIVE
IFGSAIGLFG VIVAILQTSR VKMGD
